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ADP + H2O + peptide/in
AMP + phosphate + peptide/out
ATP + H2O
ADP + phosphate
ATP + H2O + 5'-L-phenylalanyl-glycyl-floxuridine/in
ADP + phosphate + 5'-L-phenylalanyl-glycyl-floxuridine/out
-
-
-
-
?
ATP + H2O + aerolysin/in
ADP + phosphate + aerolysin/out
-
-
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
ATP + H2O + anserine/out
ADP + phosphate + anserine/in
-
-
-
-
?
ATP + H2O + beta-L-Ala-L-Lys-7-amido-4-methylcoumarin-3-acetic acid/in
ADP + phosphate + beta-L-Ala-L-Lys-7-amido-4-methylcoumarin-3-acetic acid/out
-
-
-
?
ATP + H2O + carnosine/out
ADP + phosphate + carnosine/in
-
-
-
-
?
ATP + H2O + cefadroxil/in
ADP + phosphate + cefadroxil/out
ATP + H2O + CRYQKSTEL/in
ADP + phosphate + CRYQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + D-phenylglycine-L-Dopa/in
ADP + phosphate + D-phenylglycine-L-Dopa/out
ATP + H2O + delta-aminolevulinic acid/in
ADP + phosphate + delta-aminolevulinic acid/out
ATP + H2O + EPGNTWDED/out
ADP + phosphate + EPGNTWDED/in
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
ATP + H2O + Gly-Gly/in
ADP + phosphate + Gly-Gly/out
-
-
-
-
?
ATP + H2O + Gly-L-His-Gly/in
ADP + phosphate + Gly-L-His-Gly/out
-
isoform PTR6
-
-
?
ATP + H2O + Gly-L-His/in
ADP + phosphate + Gly-L-His/out
-
isoform PTR6
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
ATP + H2O + glycylsarcosine/out
ADP + phosphate + glycylsarcosine/in
-
-
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
ATP + H2O + hemoprotein HasA/in
ADP + phosphate + hemoprotein HasA/out
-
-
-
-
?
ATP + H2O + JBP485/in
ADP + phosphate + JBP485/out
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
ATP + H2O + L-Ala-L-Ala/in
ADP + phosphate + L-Ala-L-Ala/out
ATP + H2O + L-Ala-L-Asp/in
ADP + phosphate + L-Ala-L-Asp/out
ATP + H2O + L-Ala-L-Lys/in
ADP + phosphate + L-Ala-L-Lys/out
ATP + H2O + L-Val-didanosine/in
ADP + phosphate + L-Val-didanosine/out
ATP + H2O + lacticin 481/in
ADP + phosphate + lacticin 481/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
ATP + H2O + lactococcin/in
ADP + phosphate + lactococcin/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
ATP + H2O + metalloprotease/in
ADP + phosphate + metalloprotease/out
-
metalloproteases PrtA,B,C,D
-
-
?
ATP + H2O + midodrine/in
ADP + phosphate + midodrine/out
-
-
-
-
?
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
ATP + H2O + Msmeg1704/in
ADP + phosphate + Msmeg1704/out
-
-
-
ir
ATP + H2O + Msmeg1712/in
ADP + phosphate + Msmeg1712/out
-
-
-
ir
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
ATP + H2O + NP-647/in
ADP + phosphate + NP-647/out
ATP + H2O + oseltamivir carboxylate/in
ADP + phosphate + oseltamivir carboxylate/out
ATP + H2O + oseltamivir/in
ADP + phosphate + oseltamivir/out
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
ATP + H2O + peptide/out
ADP + phosphate + peptide/in
-
ATP best substrate
-
-
?
ATP + H2O + pOA/in
ADP + phosphate + pOA/out
-
pOA, a truncated form of proOmpA with a new cysteine to allow for disulfide-loop formation
the disulfide-loop renders pOA unable to pass the channel, adding of DTT completes the translocation
-
ir
ATP + H2O + proOmpA/in
ADP + phosphate + proOmpA/out
-
-
-
-
ir
ATP + H2O + protein/in
ADP + phosphate + protein/out
Gram-negative bacteria
-
-
-
-
?
ATP + H2O + protein/out
ADP + phosphate + protein/in
-
-
-
-
?
ATP + H2O + RCYQKSTEL/in
ADP + phosphate + RCYQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRCQKSTEL/in
ADP + phosphate + RRCQKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYCKSTEL/in
ADP + phosphate + RRYCKSTEL/out
ATP + H2O + RRYNASTEL/out
ADP + phosphate + RRYNASTEL/in
-
-
-
-
?
ATP + H2O + RRYQCSTEL/in
ADP + phosphate + RRYQCSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKCTEL/in
ADP + phosphate + RRYQKCTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSCEL/in
ADP + phosphate + RRYQKSCEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSTCL/in
ADP + phosphate + RRYQKSTCL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSTEC/in
ADP + phosphate + RRYQKSTEC/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQKSTEL/out
ADP + phosphate + RRYQKSTEL/in
-
-
-
-
?
ATP + H2O + RRYQNSTCL/in
ADP + phosphate + RRYQNSTCL/out
ATP + H2O + subtilisin/in
ADP + phosphate + subtilisin/out
ATP + H2O + TVDNKTRYR/in
ADP + phosphate + TVDNKTRYR/out
-
substrate in peptide transport assay, peptide is biotin-labeled at the lysine residue
-
-
?
ATP + H2O + valacyclovir/in
ADP + phosphate + valacyclovir/out
ATP + H2O + valganciclovir/in
ADP + phosphate + valganciclovir /out
-
-
-
-
?
ATP + H2O + Zan-L-Val/in
ADP + phosphate + Zan-L-Val/out
CTP + H2O + peptide/out
CDP + phosphate + peptide/in
-
affinity for CTP is about 30fold lower compared to ATP
-
-
?
GTP + H2O + peptide/in
GDP + phosphate + peptide/out
GTP + H2O + peptide/out
GDP + phosphate + peptide/in
-
affinity for GTP is about 30fold lower compared to ATP
-
-
?
UTP + H2O + peptide/out
UDP + phosphate + peptide/in
-
affinity for UTP is about 30fold lower compared to ATP
-
-
?
additional information
?
-
ADP + H2O + peptide/in
AMP + phosphate + peptide/out
-
-
-
-
?
ADP + H2O + peptide/in
AMP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
ATP hydrolysis by SecA is required only if periplasmic loops larger than 30 amino acids have to be translocated. The signal recognition particle-dependent and SecA-dependent multiple spanning membrane protein YidC becomes SecA-independent if the large periplasmic loop connecting transmembrane domains 1 and 2 is reduced to less than 30 amino acids. The SecA dependence of a bacterial membrane protein is not solely determined by the length of the periplasmic loop but also by the presence of a down-stream TM domain
-
-
?
ATP + H2O
ADP + phosphate
-
ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli
-
-
?
ATP + H2O
ADP + phosphate
-
SEcA drives a constant rate of preprotein translocation consistent with a stepping mechanism of translocation. The delay in full-length translocation for longer preproteins is dependent on the SecA motor function. The rate of protein translocation is controlled by the ATP concentration and is independent from the length of the preprotein
-
-
?
ATP + H2O
ADP + phosphate
-
SecB, a small cytosolic chaperone, captures the precursor polypeptides before they fold and delivers them to the membrane translocon through interactions with SecA. Both SecB and SecA display twofold symmetry and yet the complex between the two is stabilized by contacts that are distributed asymmetrically
-
-
?
ATP + H2O
ADP + phosphate
-
the preprotein binding domain is a preprotein receptor and a physical bridge connecting bound preproteins to the DEAD motor
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
SecA2 plays a role in Mycobacterium tuberculosis inhibition of the immune response, which is likely important for survival in the host and pathogenesis
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + cefadroxil/in
ADP + phosphate + cefadroxil/out
-
preferable substrate
-
-
?
ATP + H2O + cefadroxil/in
ADP + phosphate + cefadroxil/out
-
preferable substrate
-
-
?
ATP + H2O + cefadroxil/in
ADP + phosphate + cefadroxil/out
-
preferable substrate
-
-
?
ATP + H2O + D-phenylglycine-L-Dopa/in
ADP + phosphate + D-phenylglycine-L-Dopa/out
-
-
-
-
?
ATP + H2O + D-phenylglycine-L-Dopa/in
ADP + phosphate + D-phenylglycine-L-Dopa/out
-
-
-
-
?
ATP + H2O + D-phenylglycine-L-Dopa/in
ADP + phosphate + D-phenylglycine-L-Dopa/out
-
-
-
-
?
ATP + H2O + delta-aminolevulinic acid/in
ADP + phosphate + delta-aminolevulinic acid/out
-
-
-
-
?
ATP + H2O + delta-aminolevulinic acid/in
ADP + phosphate + delta-aminolevulinic acid/out
-
-
-
-
?
ATP + H2O + delta-aminolevulinic acid/in
ADP + phosphate + delta-aminolevulinic acid/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
-
?
ATP + H2O + glycyl-sarcosine/in
ADP + phosphate + glycyl-sarcosine/out
-
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
-
-
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
-
-
-
-
?
ATP + H2O + guanidine oseltamivir carboxylate-L-Val/in
ADP + phosphate + guanidine oseltamivir carboxylate-L-Val/out
-
-
-
-
?
ATP + H2O + JBP485/in
ADP + phosphate + JBP485/out
-
JBP485 is cyclo-trans-4-L-hydroxyprolyl-L-serine
-
-
?
ATP + H2O + JBP485/in
ADP + phosphate + JBP485/out
-
JBP485 is cyclo-trans-4-L-hydroxyprolyl-L-serine
-
-
?
ATP + H2O + JBP485/in
ADP + phosphate + JBP485/out
-
JBP485 is cyclo-trans-4-L-hydroxyprolyl-L-serine
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-L-Ala/in
ADP + phosphate + L-Ala-L-Ala/out
K0.5 value 0.023 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Ala/in
ADP + phosphate + L-Ala-L-Ala/out
K0.5 value 0.057 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Asp/in
ADP + phosphate + L-Ala-L-Asp/out
K0.5 value 0.058 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Asp/in
ADP + phosphate + L-Ala-L-Asp/out
K0.5 value 0.129 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Lys/in
ADP + phosphate + L-Ala-L-Lys/out
K0.5 value 0.142 mM at -140 mV
-
-
?
ATP + H2O + L-Ala-L-Lys/in
ADP + phosphate + L-Ala-L-Lys/out
K0.5 value 0.167 mM at -140 mV
-
-
?
ATP + H2O + L-Val-didanosine/in
ADP + phosphate + L-Val-didanosine/out
-
didanosine is also named Videx or 5'-O-2'-3'-dideoxydidanosine
-
-
?
ATP + H2O + L-Val-didanosine/in
ADP + phosphate + L-Val-didanosine/out
-
didanosine is also named Videx or 5'-O-2'-3'-dideoxydidanosine
-
-
?
ATP + H2O + L-Val-didanosine/in
ADP + phosphate + L-Val-didanosine/out
-
didanosine is also named Videx or 5'-O-2'-3'-dideoxydidanosine
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
-
-
-
ir
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
-
-
-
ir
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + NP-647/in
ADP + phosphate + NP-647/out
-
NP-647 is L-pGlu-(2-propyl)-L-His-L-ProNH2
-
-
?
ATP + H2O + NP-647/in
ADP + phosphate + NP-647/out
-
NP-647 is L-pGlu-(2-propyl)-L-His-L-ProNH2
-
-
?
ATP + H2O + NP-647/in
ADP + phosphate + NP-647/out
-
NP-647 is L-pGlu-(2-propyl)-L-His-L-ProNH2
-
-
?
ATP + H2O + oseltamivir carboxylate/in
ADP + phosphate + oseltamivir carboxylate/out
-
the enzyme is not implicated in the oral absorption of oseltamivir carboxylate
-
-
?
ATP + H2O + oseltamivir carboxylate/in
ADP + phosphate + oseltamivir carboxylate/out
-
the enzyme is not implicated in the oral absorption of oseltamivir carboxylate
-
-
?
ATP + H2O + oseltamivir/in
ADP + phosphate + oseltamivir/out
-
the enzyme is not implicated in the oral absorption of oseltamivir
-
-
?
ATP + H2O + oseltamivir/in
ADP + phosphate + oseltamivir/out
-
the enzyme is not implicated in the oral absorption of oseltamivir
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
TAPL is a half-type ABC transporter that localizes in lysosome and putatively conveys peptides from cytosol to lysosome
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
the enzyme translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + RRYCKSTEL/in
ADP + phosphate + RRYCKSTEL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYCKSTEL/in
ADP + phosphate + RRYCKSTEL/out
-
substrate in peptide transport assay, fluorescein coupled via a cyteine residue
-
-
?
ATP + H2O + RRYQNSTCL/in
ADP + phosphate + RRYQNSTCL/out
-
peptide transport assay, fluorescein is coupled via the cysteine
-
-
?
ATP + H2O + RRYQNSTCL/in
ADP + phosphate + RRYQNSTCL/out
-
substrate in peptide transport assay, fluorescein coupled via a cyteine residue
-
-
?
ATP + H2O + subtilisin/in
ADP + phosphate + subtilisin/out
-
-
-
-
?
ATP + H2O + subtilisin/in
ADP + phosphate + subtilisin/out
-
-
-
-
?
ATP + H2O + valacyclovir/in
ADP + phosphate + valacyclovir/out
-
-
-
-
?
ATP + H2O + valacyclovir/in
ADP + phosphate + valacyclovir/out
-
-
-
-
?
ATP + H2O + valacyclovir/in
ADP + phosphate + valacyclovir/out
-
-
-
-
?
ATP + H2O + Zan-L-Val/in
ADP + phosphate + Zan-L-Val/out
-
-
-
-
?
ATP + H2O + Zan-L-Val/in
ADP + phosphate + Zan-L-Val/out
-
-
-
-
?
ATP + H2O + Zan-L-Val/in
ADP + phosphate + Zan-L-Val/out
-
-
-
-
?
GTP + H2O + peptide/in
GDP + phosphate + peptide/out
-
-
-
-
?
GTP + H2O + peptide/in
GDP + phosphate + peptide/out
-
-
-
-
?
additional information
?
-
dipeptide transport by AtPTR1 is electrogenic and dependent on protons but not sodium. Transport activity is voltage-dependent, and currents increase supralinearly with more negative membrane potentials and do not saturate. The voltage dependence of the apparent affinities differes between Ala-Ala, Ala-Lys, and Ala-Asp and is not conserved between the two transporters AtPTR1 and AtPTR5. The apparent affinity of AtPTR1 for these dipeptides is pH-dependent and decreases with decreasing proton concentration
-
-
?
additional information
?
-
dipeptide transport by AtPTR1 is electrogenic and dependent on protons but not sodium. Transport activity is voltage-dependent, and currents increase supralinearly with more negative membrane potentials and do not saturate. The voltage dependence of the apparent affinities differes between Ala-Ala, Ala-Lys, and Ala-Asp and is not conserved between the two transporters AtPTR1 and AtPTR5. The apparent affinity of AtPTR1 for these dipeptides is pH-dependent and decreases with decreasing proton concentration
-
-
?
additional information
?
-
dipeptide transport by AtPTR5 is electrogenic and dependent on protons but not sodium. Transport activity is voltage-dependent, and currents increase supralinearly with more negative membrane potentials and do not saturate. The voltage dependence of the apparent affinities differes between Ala-Ala, Ala-Lys, and Ala-Asp and is not conserved between the two transporters AtPTR1 and AtPTR5
-
-
?
additional information
?
-
dipeptide transport by AtPTR5 is electrogenic and dependent on protons but not sodium. Transport activity is voltage-dependent, and currents increase supralinearly with more negative membrane potentials and do not saturate. The voltage dependence of the apparent affinities differes between Ala-Ala, Ala-Lys, and Ala-Asp and is not conserved between the two transporters AtPTR1 and AtPTR5
-
-
?
additional information
?
-
no substrate: His-Ala, Ala-Ala, Ala-Lys, Ala-Asp
-
-
?
additional information
?
-
no substrate: His-Ala, Ala-Ala, Ala-Lys, Ala-Asp
-
-
?
additional information
?
-
-
Caenorhabditis elegans requires ABC transporters HAF-4 and HAF-9, which are highly homologous to human lysosomal peptide transporter TAPL
-
-
?
additional information
?
-
-
one intact nucleotide-binding domain within a dimer is sufficient for ATP hydrolysis. One ATP-binding site of the dimer is able to function independently of the hydrolytic capability of the neighboring ATP-binding site. Sequential mechanism of ATP hydrolysis in the intact HlyB transporter
-
-
?
additional information
?
-
-
ATPase activity associated with transporter associated with antigen processing, TAP. Role of TAP in peptide loading of MHC molecules and the overall process of antigen presentation
-
-
?
additional information
?
-
-
coordinated dialogue between peptide binding site, nucleotide-binding domain, and the translocation site
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
the enzyme binds ATP, ADP, GTP, and dATP, UTP, and CTP to a lower extent, but not AMP
-
-
?
additional information
?
-
-
permeation of cationic antimicrobial di- and tripeptides derived from lactoferricin and test for interaction with PEPT1, none serves as a substrate
-
-
?
additional information
?
-
-
using the two-electrode, voltage-clamp technique at Xenopus laevis oocytes, strong hPEPT1-specific inward transport currents are recorded for glycylsarcosine, anserine and carnosine, but not for glycine
-
-
?
additional information
?
-
-
isoform PTR6 shows substrate selectivity for di- and tripeptides
-
-
?
additional information
?
-
-
the enzyme binds ATP, ADP, GTP, and dATP, UTP, and CTP to a lower extent, but not AMP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + H2O
ADP + phosphate
ATP + H2O + aerolysin/in
ADP + phosphate + aerolysin/out
-
-
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
ATP + H2O + hemoprotein HasA/in
ADP + phosphate + hemoprotein HasA/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
ATP + H2O + lacticin 481/in
ADP + phosphate + lacticin 481/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
ATP + H2O + lactococcin/in
ADP + phosphate + lactococcin/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
ATP + H2O + metalloprotease/in
ADP + phosphate + metalloprotease/out
-
metalloproteases PrtA,B,C,D
-
-
?
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
ATP + H2O + Msmeg1704/in
ADP + phosphate + Msmeg1704/out
-
-
-
ir
ATP + H2O + Msmeg1712/in
ADP + phosphate + Msmeg1712/out
-
-
-
ir
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
ATP + H2O + protein/in
ADP + phosphate + protein/out
Gram-negative bacteria
-
-
-
-
?
ATP + H2O + subtilisin/in
ADP + phosphate + subtilisin/out
additional information
?
-
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
-
ir
ATP + H2O
ADP + phosphate
-
ATP hydrolysis by SecA is required only if periplasmic loops larger than 30 amino acids have to be translocated. The signal recognition particle-dependent and SecA-dependent multiple spanning membrane protein YidC becomes SecA-independent if the large periplasmic loop connecting transmembrane domains 1 and 2 is reduced to less than 30 amino acids. The SecA dependence of a bacterial membrane protein is not solely determined by the length of the periplasmic loop but also by the presence of a down-stream TM domain
-
-
?
ATP + H2O
ADP + phosphate
-
ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
SecA2 plays a role in Mycobacterium tuberculosis inhibition of the immune response, which is likely important for survival in the host and pathogenesis
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O
ADP + phosphate
-
-
-
ir
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + alpha-haemolysin/in
ADP + phosphate + alpha-haemolysin/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + formyl-methionyl-leucine-phenylalanine/in
ADP + phosphate + formyl-methionyl-leucine-phenylalanine/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/in
ADP + phosphate + L-Ala-gamma-D-Glu-meso-diaminopimelic acid/out
-
-
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + lactococcin G/in
ADP + phosphate + lactococcin G/out
-
lactococcal bacteriocin
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + major histocompatibility complex class I molecules/in
ADP + phosphate + major histocompatibility complex class I molecules/out
-
-
-
-
?
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
-
-
-
ir
ATP + H2O + Msmeg1704 in
ADP + phosphate + Msmeg1704 out
-
-
-
ir
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + muramyl dipeptide/in
ADP + phosphate + muramyl dipeptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
TAPL is a half-type ABC transporter that localizes in lysosome and putatively conveys peptides from cytosol to lysosome
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
the enzyme translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + peptide/in
ADP + phosphate + peptide/out
-
-
-
-
?
ATP + H2O + subtilisin/in
ADP + phosphate + subtilisin/out
-
-
-
-
?
ATP + H2O + subtilisin/in
ADP + phosphate + subtilisin/out
-
-
-
-
?
additional information
?
-
-
Caenorhabditis elegans requires ABC transporters HAF-4 and HAF-9, which are highly homologous to human lysosomal peptide transporter TAPL
-
-
?
additional information
?
-
-
ATPase activity associated with transporter associated with antigen processing, TAP. Role of TAP in peptide loading of MHC molecules and the overall process of antigen presentation
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
-
ABCB10 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis. ABCB10 plays physiological role in antigen processing
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB2 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB3 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB8 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
additional information
?
-
-
ABCB9 is involved in intracellular trafficking and compartmentalization of peptides. Peptide translocation requires ATP hydrolysis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(4-bromophenyl)-5-cyano-4-oxopyrimidine)
-
-
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(biphenyl-4-yl)-5-cyano-4-oxopyrimidine)
-
compound does not show antimicrobial activity
2-((4-azidobenzyl)thio)-4-(4-(benzyloxy)phenyl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile
good antimicrobial inhibition with MIC of 12.5 microM
2-((4-azidobenzyl)thio)-6-oxo-4-(4-phenoxyphenyl)-1,6-dihydropyrimidine-5-carbonitrile
good antimicrobial inhibition with MIC of 18.2 microM
2-(benzylsulfanyl)-4-(biphenyl-4-yl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile
-
exhibits most potent inhibition effects against strain NR698 with increased outer membrane permeability
3-biphenyl-L-alanyl-L-arginine methyl ester
-
peptide derived from lactoferricin, at 1 mM, 10% inhibition of glycylsarcosine-induced current
4-(gamma-aminobutanoyl)-Lys
-
azide
1.5 mM azide decrease the transport of the cell-surface glycoprotein mutant GspB736flag, 15 mM nearly prevent transport of GspB736flag, azide have no effect on ATP hydrolysis activity of the recombinant protein 6His-SecA; 1.5 mM azide markedly decrease the transport of the cell-surface glycoprotein mutant GspB736flag, 15 mM nearly prevent transport of GspB736flag, azide have no effect on ATP hydrolysis activity of the recombinant protein 6His-SecA2
Carbonyl cyanide m-chlorophenylhydrazone
10 mM, 20% residual activity; 10 mM, 26% residual activity
cisplatin
-
IC50 value for growth inhibition of cell line PC-3 0.0033 mM, DU-145 0.0045 mM, 2008 0.0194 mM, C-13 0.117 mM, L-540 0.0025 mM
diethyl dicarbonate
10 mM, 0.4% residual activity; 10 mM, 0.6% residual activity
erythrosin B
-
the potency in inhibiting the truncated SecA ATPase correlates with the ability to inhibit the biologically relevant protein translocation activity of SecA and also translates into antibacterial effects
Fv fragment of the monoclonal antibody mAb148.3
-
Fv binding to the C terminus of TAP1
-
ICP47
-
herpes simplex virus protein
-
KCl
-
no ATPase activity above 300 mM
L-Phe-L-Ala
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala; in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe
L-Phe-L-Phe
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe. Phe-Ala reduces leak currents by binding to the substrate-binding site with a high apparent affinity
L-Trp-L-Ala
in the absence of dipeptides, transporter shows proton-dependent leak currents that are inhibited by Phe-Ala, Trp-Ala, and Phe-Phe
N-ethylmaleimide
10 mM, 12% residual activity; 10 mM, 14% residual activity
NaCl
-
no ATPase activity above 300 mM
Rose bengal
-
the potency in inhibiting the truncated SecA ATPase correlates with the ability to inhibit the biologically relevant protein translocation activity of SecA and also translates into antibacterial effects
RWR-NH(benzyl)
-
peptide derived from lactoferricin, at 1 mM, 87% inhibition of glycylsarcosine-induced current, peptide can also impair membrane protein functions in an unspecific manner
RWR-NH2
-
peptide derived from lactoferricin, at 1 mM, 15% inhibition of glycylsarcosine-induced current
ubiquitin-like specific protease 18
-
-
-
[AuIIIBr2(dtc-Sar-Aib-O(t-Bu))]
-
IC50 value for growth inhibition of cell line PC-3 0.0008 mM, DU-145 0.0014 mM, 2008 0.0045 mM, C-13 0.0037 mM, L-540 0.0015 mM
[AuIIICl2(dtc-Sar-Aib-O(t-Bu))]
-
IC50 value for growth inhibition of cell line PC-3 0.0011 mM, DU-145 0.0022 mM, 2008 0.0047 mM, C-13 0.0051 mM, L-540 0.0017 mM
additional information
-
Insertion of charged amino acid residues into the preprotein proOmpA strongly inhibits SecA translocation ATPase activity. Stretches of positively charged residues are much stronger translocation inhibitors and suppressors of the preprotein-stimulated SecA ATPase activity than negatively charged residues.
-
anserine
-
inhibits uptake of glycylsarcosine
anserine
-
inhibits uptake of glycylsarcosine
carnosine
-
inhibits uptake of glycylsarcosine
carnosine
-
inhibits uptake of glycylsarcosine
cefaclor
-
L-Lys-L-Lys
-
Mg2+
-
-
Mg2+
-
2 mM Mg2+ blocks SecA ATPase activity almost completely, the inhibition is abolishable by binding of SecA to the protein channel SecYEG in proteoliposomes (1 micromol)
orthovanadate
-
IC50: 0.016 mM, competitive
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0.002 - 0.02
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(4-bromophenyl)-5-cyano-4-oxopyrimidine)
0.002 - 0.05
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(biphenyl-4-yl)-5-cyano-4-oxopyrimidine)
0.0024
2-((4-azidobenzyl)thio)-4-(4-(benzyloxy)phenyl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile
Escherichia coli
37°C, pH not specified in the publication
0.0022
2-((4-azidobenzyl)thio)-6-oxo-4-(4-phenoxyphenyl)-1,6-dihydropyrimidine-5-carbonitrile
Escherichia coli
37°C, pH not specified in the publication
0.06
2-(benzylsulfanyl)-4-(biphenyl-4-yl)-6-oxo-1,6-dihydropyrimidine-5-carbonitrile
Escherichia coli
-
recombinant SecA, pH 7.6, 40°C
0.025
eosin Y
Escherichia coli
-
truncated SecA without the C-terminal regulatory domain, 40°C, pH 7.6
0.002
erythrosin B
Escherichia coli
-
truncated SecA without the C-terminal regulatory domain, 40°C, pH 7.6
0.016
orthovanadate
Escherichia coli
-
IC50: 0.016 mM, competitive
0.0005
Rose bengal
Escherichia coli
-
truncated SecA without the C-terminal regulatory domain, pH 7.6, 40°C
2.7
RWR-NH2
Homo sapiens
-
pH 7.4, 22°C
additional information
beta-Ala-Lys
0.002
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(4-bromophenyl)-5-cyano-4-oxopyrimidine)
Escherichia coli
-
EcN68, the N-terminal fragment of SecA without the C-terminal regulatory domain, pH 7.6, 40°C
0.02
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(4-bromophenyl)-5-cyano-4-oxopyrimidine)
Escherichia coli
-
recombinant SecA, pH 7.6, 40°C
0.002
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(biphenyl-4-yl)-5-cyano-4-oxopyrimidine)
Escherichia coli
-
EcN68, the N-terminal fragment of SecA without the C-terminal regulatory domain, pH 7.6, 40°C
0.05
2,2'-(alpha,alpha'-xylene)bis(sulfanediyl)bis-(6-(biphenyl-4-yl)-5-cyano-4-oxopyrimidine)
Escherichia coli
-
recombinant SecA, pH 7.6, 40°C
0.08
alafosfalin
Escherichia coli
mutant K274I, pH 7.5, temperature not specified in the publication
0.11
alafosfalin
Escherichia coli
wild-type, pH 7.5, temperature not specified in the publication
0.39
alafosfalin
Escherichia coli
mutant M154K, pH 7.5, temperature not specified in the publication
0.44
alafosfalin
Escherichia coli
mutant V252E, pH 7.5, temperature not specified in the publication
0.59
alafosfalin
Escherichia coli
mutant L190V, pH 7.5, temperature not specified in the publication
0.71
alafosfalin
Escherichia coli
mutant F197I, pH 7.5, temperature not specified in the publication
1.5
alafosfalin
Escherichia coli
mutant L324V, pH 7.5, temperature not specified in the publication
0.12
L-Ala-L-Ala
Escherichia coli
mutant M154K, pH 7.5, temperature not specified in the publication
0.31
L-Ala-L-Ala
Escherichia coli
mutant K274I, pH 7.5, temperature not specified in the publication
0.32
L-Ala-L-Ala
Escherichia coli
mutant L190V, pH 7.5, temperature not specified in the publication
0.33
L-Ala-L-Ala
Escherichia coli
mutant V252E, pH 7.5, temperature not specified in the publication
0.33
L-Ala-L-Ala
Escherichia coli
wild-type, pH 7.5, temperature not specified in the publication
0.48
L-Ala-L-Ala
Escherichia coli
mutant F197I, pH 7.5, temperature not specified in the publication
0.56
L-Ala-L-Ala
Escherichia coli
mutant L324V, pH 7.5, temperature not specified in the publication
additional information
beta-Ala-Lys
Escherichia coli
IC50 value range between 0.1 and 1 mM for wild-type and E20-mutants, and increase to above 10 mM for mutant E388Q, pH not specified in the publication, temperature not specified in the publication
additional information
beta-Ala-Lys
Escherichia coli
-
IC50 value range between 0.1 and 1 mM for wild-type and E20-mutants, and increase to above 10 mM for mutant E388Q, pH not specified in the publication, temperature not specified in the publication
additional information
Gly-Lys
Escherichia coli
IC50 value range between 0.1 and 1 mM for wild-type and E20-mutants, and increase to about 2 mM for mutant E388Q, pH not specified in the publication, temperature not specified in the publication
additional information
Gly-Lys
Escherichia coli
-
IC50 value range between 0.1 and 1 mM for wild-type and E20-mutants, and increase to about 2 mM for mutant E388Q, pH not specified in the publication, temperature not specified in the publication
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0.0000003
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP and 1 mM orthovanadate
0.00000035
-
peptide transport rate, wild type, in the presence of 3 mM ATP and 500 microM competitor peptide RRYQKSTEL
0.00000039
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM AMP
0.00000156
-
peptide transport rate, wild type, in the presence of 3 mM ATP
0.000003
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-eggPG, 9 to 1
0.000004
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPE, 9 to 1
0.000006
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine heart lipids
0.000011
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine brain lipids
0.000023
-
peptide transport rate, TAPL reconstituted in liposomes prepared from bovine liver lipids
0.000028
-
peptide transport rate
0.000045
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 100% phosphatidylcholine
0.00007
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 90% DOPS
0.000075
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPA, 9 to 1
0.000095
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 10% DOPS
0.000112
-
peptide transport rate
0.000115
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 70% phosphatidylcholine
0.000135
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, DOPC-DOPS, 9 to 1
0.000245
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 70% DOPS
0.00026
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 30% DOPS
0.00028
-
peptide transport rate
0.000295
-
peptide transport rate
0.00042
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids
0.000423
-
peptide transport rate, TAPL reconstitution in liposomes composed of DOPC and 50% DOPS
0.000477
-
peptide transport rate
0.000505
-
peptide transport rate, TAPL reconstitution in Eschericha coli liposomes, for comparison
0.000533
-
peptide transport rate
0.000535
-
peptide transport rate, TAPL reconstitution in liposomes of defined lipid composition, for comparison in Eschericha coli liposomes
0.00055
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, no phosphatidylcholine
0.000673
-
peptide transport rate
0.000715
-
peptide transport rate
0.001
PaSecAN236, liposome
0.00127
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 50% phosphatidylcholine
0.00129
-
peptide transport rate
0.00132
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 10% phosphatidylcholine
0.00168
-
peptide transport rate, TAPL reconstituted in liposomes prepared from Escherichia coli lipids, 30% phosphatidylcholine
0.052
PaSecAN236, PaSecAL43P, liposome
1.93
-
pH 7.4, 32°C, substrate RRYNASTEL
2.02
-
pH 7.4, 32°C, substrate RRYQKSTEL
0.00000022
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP
0.00000022
-
peptide transport rate, wild type, in the presence of 3 mM ATP and 1 mM orthovanadate
0.00000026
-
peptide transport rate, K545A/H699A mutant, in the presence of 3 mM ATP and 500 microM competitor peptide RRYQKSTEL
0.00000026
-
peptide transport rate, wild type, in the presence of 3 mM AMP
0.0065
PaSecAL43P, liposome
0.0065
PaSecAN236, PaSecAL43P
additional information
-
10 nM Pi/min/nM SecA in presence of Escherichia coli PE/anionic phospholipid membranes
additional information
-
425 mol ATP/min/mol SecA in presence of 0.2 micromol preprotein translocation substrate proOmpA in urea
additional information
-
in ATPase translocation activity assay with preprotein translocation substrate proOmpA: circa 0.8 mM ATP/2 micromol SecA after 1 min, mutant SecA proteins with deletions of amino acids between 2-11 shows ATPase translocation activity around 0.25 mM ATP/2 micromol SecA after 1 min
additional information
-
translocation ATPase activity: 0.9 nmol phosphate/microgramm SecA/min, mutants lacking 2 to 11 residues of the amino terminus of SecA shows defect translocation ATPase activities (below 0.1 nmol phosphate/microgramm/min)
additional information
circa 1.8 pMol Pi/pMol 6His-SecA2/min, measured in an assay containing 2.5 mM Mg2+
additional information
circa 1.8 pMol Pi/pMol 6His-SecA2/min, measured in an assay containing 2.5 mM Mg2+
additional information
-
circa 1.8 pMol Pi/pMol 6His-SecA2/min, measured in an assay containing 2.5 mM Mg2+
additional information
circa 7 pMol phosphate/pMol 6His-SecA/min measured in an assay containing 0.1 mM Mg2+
additional information
circa 7 pMol phosphate/pMol 6His-SecA/min measured in an assay containing 0.1 mM Mg2+
additional information
-
circa 7 pMol phosphate/pMol 6His-SecA/min measured in an assay containing 0.1 mM Mg2+
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dimer
-
-
dimer
-
covalently dimerized SecA is functional in protein translocation
dimer
-
is the active form of the enzyme. ATP-promoted dimerization of HlyB-nucleotide binding domain might involve formation of two interconvertible forms: a readily dissociable active dimer and a more stable, reversibly inactive form of the dimer
dimer
-
membrane-bound SEcA dimer exists and is required for effective protein translocation
dimer
2 * 102000, gel filtration, furthermore electron paramagnetic resonance spectroscopy used to identify the interactive binding surface of SecA
dimer
-
chemical cross-linking experiments, dimerization is necessary for the translocation ATPase activity of SecA, monomer-dimer equilibrium is altered in SecA mutants: mutants lacking 2 to 11 residues of the amino terminus of SecA failed to form dimers at 1microM SecA and 300 nM KCl, determination by gel filtration controlling eluate by photodiode array UV/Vis detector, a differential refractometer and a static, multiangle laser light scattering detector
dimer
-
SDS-PAGE (verified by gel filtration)
dimer
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of 65 nM at 30 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
dimer
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of Kd of 161 nM at 30 mM KCl, and a Kd of 618 nM at 150 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
dimer
-
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of Kd of 161 nM at 30 mM KCl, and a Kd of 618 nM at 150 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
-
dimer
-
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of 65 nM at 30 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
-
dimer
-
2 * 34000, SDS-PAGE
dimer
-
TtSecA forms parallel (head-to-head) dimers that are reminiscent of open scissors. The dimer interface is abundant in bulky Arg and Lys side-chains from both subunits, which stack on one another to form a basic zipper that is highly conserved
heterodimer
-
TAP1, TAP2
heterodimer
-
1 * 70000 (TAP1) + 1 * 72000 (TAP2), SDS-PAGE
homodimer
-
2 * 70000, SDS-PAGE
homodimer
-
TAPL forms a homodimer in the membrane and under the solubilized conditions
homodimer
-
dissected in TMD0 (residues 1-142), containing a C-terminal myc-tag, and the core complex (residues 143-766), which consists of the cytosolic linker L0. Core-TAPL is essential and sufficient for peptide transport
homodimer
2 * 17100, isoform PEPT1, X-ray crystallography
homodimer
-
TAPL forms a homodimer in the membrane and under the solubilized conditions
homodimer
2 * 20100, isoform PEPT2, X-ray crystallography
monomer
X-ray diffraction reveals that the dimeric SecA ATPase dissociates in monomers during protein translocation
monomer
-
crystallization data of recombinant nucleotide-binding domain
monomer
-
SecA functions as a monomer during protein translocation in vivo
monomer
-
under most conditions, only the monomer form can be detected, indicating that dimers are very unstable. Monomers can interact at least transiently and are the important species during ATP hydrolysis
monomer
-
under most conditions, only the monomer form can be detected, indicating that dimers are very unstable. Monomers can interact at least transiently and are the important species during ATP hydrolysis
-
monomer
-
X-ray diffraction reveals that the dimeric SecA ATPase dissociates in monomers during protein translocation
additional information
-
ABC transporter
additional information
-
ExeA, cytoplasmic domain with ATP-binding site
additional information
-
ABC transporter
additional information
-
ABC transporter
additional information
-
ABC transporter
additional information
-
SpaB, homology to HlyB of Escherichia coli
additional information
-
SpaT, another ABC transporter encoded in the subtilin operon, role concluded from homologies to other ABC transporters
additional information
-
components involved are SpaF and SpaG, function concluded from similarities with ABC transporters belonging to the HisP subfamily where the ATP binding sites are located in the N-terminal part of the protein
additional information
-
ABC transporter
-
additional information
-
SpaT, another ABC transporter encoded in the subtilin operon, role concluded from homologies to other ABC transporters
-
additional information
-
components involved are the membrane fusion protein PrtE, the outer membrane protein PrtF, and the ABC protein PrtD
additional information
-
ABC transporter
additional information
-
ABC transporter
additional information
-
ABC transporter
additional information
-
components involved are two helper proteins and the ABC protein: membrane fusion protein (MFP), outer membrane protein (OMP), and the ABC protein
additional information
-
components involved are two helper proteins and the ABC protein: membrane fusion protein (MFP), outer membrane protein (OMP), and the ABC protein
additional information
-
ABC protein HlyB and membrane fusion protein HylD
additional information
-
ABC protein HlyB and membrane fusion protein HylD
additional information
the dimer, crosslinked by disulfide bridges, is inactive, the monomer is active
additional information
residues Leu6, the amino terminus (residues 2 to 11) in the nucleotide binding domain, Phe263 in the preprotein binding domain, and Tyr794 and Arg805 in the intramolecular regulator of the ATPase 1 domain are involved in ecSecA dimerization
additional information
Gram-negative bacteria
-
ABC transporter
additional information
Gram-negative bacteria
-
ABC transporter
additional information
Gram-negative bacteria
-
components involved are two helper proteins and the ABC protein: membrane fusion protein (MFP), outer membrane protein (OMP), and the ABC protein
additional information
Gram-negative bacteria
-
components involved are two helper proteins and the ABC protein: membrane fusion protein (MFP), outer membrane protein (OMP), and the ABC protein
additional information
-
TAP1 and TAP 2
additional information
-
ABC transporter
additional information
-
ABC transporter
additional information
-
ABC transporter
additional information
-
components involved are encoded by lctF, lctE and lctG, role concluded from homologies to other ABC transporters
additional information
-
LcnC with one ATP binding domain in its C-terminus
additional information
-
LagD, role concluded from homologies to other ABC transporters
additional information
-
ABC transporter
-
additional information
-
LagD, role concluded from homologies to other ABC transporters
-
additional information
-
TAP1 and TAP 2
additional information
-
TAP1 and TAP 2
additional information
-
ABC protein HasA and membrane fusion protein HasE
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G55A
-
mutation in the potential ATP-binding site in ExeA, decreased rate of aerolysin secretion
G55D
-
mutation in the potential ATP-binding site in ExeA, decreased rate of aerolysin secretion
G55V
-
mutation in the potential ATP-binding site in ExeA, decreased rate of aerolysin secretion
D209N
-
mutant of SecA capable of binding, but not hydrolysing ATP
E210Q
-
mutant of SecA capable of binding, but not hydrolysing ATP
K539M
-
introduction of a Walker A mutation in the haf-4 construct. The mutation in ATP-binding site of HAF-4 inhibits the maturation of granules as dominant-negative effects. The inactive form of HAF-4 does not rescue the phenotype
A123V
partial loss of uptake
A264P
partial loss of uptake
A285V
complete loss of uptake
A303G
partial loss of uptake
A68P
complete loss of uptake
Cys-less
mutant for analyzing the interaction and regulatory domains of SecA
D209A
-
a dominant-negative mutant, binds ATP but is unable to hydrolyze it and is inactive in proOmpA translocation. Mutant generates a translocation intermediate of 18 kDa. Further addition of wild-type SecA causes its translocation into either mature OmpA or another intermediate of 28 kDa that can be translocated into mature by a proton motive force. The addition of excess D209N SecA during translocation causes a topology inversion of SecG
D630M
-
ATPase activity is 0.6% of wild-type activity
E20D
mutant is not affected by the bulk pH in the range tested, no dramatic change in IC50 value for peptides Gly-Lys, beta-Ala-Lys
E20Q
mutant is not affected by the bulk pH in the range tested, no dramatic change in IC50 value for peptides Gly-Lys, beta-Ala-Lys
E388D
increase in IC50 value for peptides Gly-Lys, beta-Ala-Lys, increase in pH-optimum
E388Q
increase in IC50 value for peptides Gly-Lys, beta-Ala-Lys, increase in pH-optimum
E400C
mutant for analyzing the interaction and regulatory domains of SecA
E400C/R642C
mutant for analyzing the interaction and regulatory domains of SecA
E400R
mutant for analyzing the interaction and regulatory domains of SecA
E400R/A628T
mutant for analyzing the interaction and regulatory domains of SecA
E400R/E619K
mutant for analyzing the interaction and regulatory domains of SecA
E400R/H620P
mutant for analyzing the interaction and regulatory domains of SecA
E400R/I627T
mutant for analyzing the interaction and regulatory domains of SecA
E400R/L610P
mutant for analyzing the interaction and regulatory domains of SecA
E400R/M607T
mutant for analyzing the interaction and regulatory domains of SecA
E400R/N629D
mutant for analyzing the interaction and regulatory domains of SecA
E56G
complete loss of uptake
E635C
mutant for analyzing the interaction and regulatory domains of SecA
F197I
change in selectivity
F289L
complete loss of uptake
F289S
complete loss of uptake
F301I
complete loss of uptake
G101D
partial loss of uptake
G127D
partial loss of uptake
G78C
complete loss of uptake
G86R
partial loss of uptake
I100V
no membrane localization
I122N
partial loss of uptake
I60N
complete loss of uptake
Ile3A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
K108R
mutant, defective in ATP binding and protein translocation in vitro, as well as biologically inactive in vivo
K274I
change in selectivity
K508M
-
ATPase activity is 1.3% of wild-type activity
L136R
complete loss of uptake
L137H
no membrane localization
L190V
change in selectivity
L2A/I3A
mutation does not substantially affect SecA dimerization
L324V
change in selectivity
L98R
complete loss of uptake
Leu2A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
Leu5A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
Leu6A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
M154K
change in selectivity
M295K
complete loss of uptake
N196K
partial loss of uptake
N300I
complete loss of uptake
N300Y
partial loss of uptake
N306I
partial loss of uptake
N95
truncated version of Escherichia coli SecA, the last 70 residues are lacking
N95CC
two cysteines are introduced into a truncated version of Escherichia coli SecA, at position 636 and 801, the last 70 residues are lacking, mutant is dimeric and fully functional
P326Q
partial loss of uptake
P624C
-
insoluble mutant protein
P624L
-
insoluble mutant protein
P624R
-
insoluble mutant protein
P624S
-
insoluble mutant protein
Phe10A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
Q320L
complete loss of uptake
R305C
partial loss of uptake
R400R/M607T
mutant for analyzing the interaction and regulatory domains of SecA
R642C
mutant for analyzing the interaction and regulatory domains of SecA
R642E
mutant for analyzing the interaction and regulatory domains of SecA
R642E/A628T
mutant for analyzing the interaction and regulatory domains of SecA
R642E/E619K
mutant for analyzing the interaction and regulatory domains of SecA
R642E/H620P
mutant for analyzing the interaction and regulatory domains of SecA
R642E/I627T
mutant for analyzing the interaction and regulatory domains of SecA
R642E/L610P
mutant for analyzing the interaction and regulatory domains of SecA
R642E/M607T
mutant for analyzing the interaction and regulatory domains of SecA
R642E/N629D
mutant for analyzing the interaction and regulatory domains of SecA
R656C
mutant for analyzing the interaction and regulatory domains of SecA
S59P
complete loss of uptake
SecADELTA11/N95
monomeric SecA derivative mutant, which lacks extreme terminal residues and shows in vitro and in vivo activities
T297A
complete loss of uptake
V252E
change in selectivity
V548A
-
insoluble mutant protein
V9A/F10A
mutation enhances dissociation by 8fold with respect to that of wild-type SecA
Val9A
mutation completely blocks dimerization of SecA in 300 mM KCl buffer
Y477W
-
KM-value for ATP is 1.75fold higher than wild-type value. kcat for ATP is 4.3fold higher than wild-type value
D630M
-
ATPase activity is 0.6% of wild-type activity
-
K508M
-
ATPase activity is 1.3% of wild-type activity
-
P624L
-
insoluble mutant protein
-
P624S
-
insoluble mutant protein
-
V548A
-
insoluble mutant protein
-
coreTAP1
-
mutant, delta2-122
coreTAP2
-
mutant, delta2-122
D668E
-
mutation in the nucleotide-binding domain of TAP1
D668E/Q701H
-
TAP1 mutant
D668E/Q710H
-
mutation in the nucleotide-binding domain of TAP1
D668N/Q701A
-
TAP1 mutant
DELTAN1-2TAP1
-
mutant, delta2-89
DELTAN1-2TAP2
-
mutant, delta2-44
DELTAN1-3TAP1
-
mutant, delta2-132
DELTAN1TAP1
-
mutant, delta2-44
DELTAN1TAP2
-
mutant, delta2-44
E632D/H661Q
-
TAP2 mutant
E632Q/H661A
-
TAP2 mutant
E632Q/H662A
-
TAP2 mutant
K545A/H699A
-
TAPL double mutant
Q710H
-
mutation in the nucleotide-binding domain of TAP1
K115A
mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity
K115R
mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity
K115A
-
mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity
-
K115R
-
mutant, substitution of the conserved lysine in the Walker A motif eliminates ATP binding and affects the biological activity
-
PaSecAN236
N-terminal 236 amino acids of PaSecA
TAP2DELTATM1
-
mutant, amino acids 2-42 are removed
TAP2DELTATM2
-
mutant, amino acids 2-88 are removed
TAP2DELTATM3
-
mutant, amino acids 2-128 are removed
TAP2DELTATM4
-
mutant, amino acids 2-185 are removed
TAP2DELTATM5
-
mutant, amino acids 2-241 are removed
E599Q
-
3000fold reduction of ATPase activity compared to wild-type
SecA2DELTA1-990
mutant, cloned into different plamids, construction of different strains
SecA2DELTA1732-2397 7
mutant, cloned into different plamids, construction of different strains
SecA2DELTA1768-2028
mutant, cloned into different plamids, construction of different strains
SecA2DELTA991-1749
mutant, cloned into different plamids, construction of different strains
E485R/E488R/R367E
mutation leads to a closed conformation of the clamp, the C-loop remains inside the clamp
R367E
mutation of a conserved residue, results in significant lateral opening of the clamp, which leads to increased dissociation of the substrate
E485R/E488R/R367E
-
mutation leads to a closed conformation of the clamp, the C-loop remains inside the clamp
-
R367E
-
mutation of a conserved residue, results in significant lateral opening of the clamp, which leads to increased dissociation of the substrate
-
additional information
-
large in-frame deletion of SpaT, not translocation is interrupted, but proteolytic cleavage of the leader segment while the precurser resides in the cell wall
additional information
-
large in-frame deletion of SpaT, not translocation is interrupted, but proteolytic cleavage of the leader segment while the precurser resides in the cell wall
-
additional information
-
the loss-of-function mutants for haf-4 and haf-9, constructed by RNAi mechanism, exhibit granular defects in late larval and young adult intestinal cells, associated with decreased brood size, prolonged defecation cycle, and slow growth. The intestinal granular phenotype is rescued by the overexpression of the GFP-tagged wild-type protein, but not by the ATP-unbound form of HAF-4, overview
additional information
deletion of SecA1 failed, unless a copy of the gene is provided in trans on a plasmid, thus SecA1 belongs to the housekeeping genes
additional information
deletion of SecA1 failed, unless a copy of the gene is provided in trans on a plasmid, thus SecA1 belongs to the housekeeping genes
additional information
deletion of SecA2 failed, unless a copy of the gene is provided in trans on a plasmid, thus SecA2 belongs to the housekeeping genes
additional information
deletion of SecA2 failed, unless a copy of the gene is provided in trans on a plasmid, thus SecA2 belongs to the housekeeping genes
additional information
a collection of 63 monocysteine mutants for the 901-aminoacid-residue SecA protein is generated for topological analysis of the protein
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a collection of 63 monocysteine mutants for the 901-aminoacid-residue SecA protein is generated for topological analysis of the protein
additional information
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SecY-SecA interactions are studied by an in vivo site-directed cross-linking technique
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analysis of the function of the two-helix finger of the SecA ATPase via point mutations
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screening of a library of mutants to identify amino acids critical for peptide transport and identification of 35 single point mutations that result in a full or partial loss of transport activity
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screening of a library of mutants to identify amino acids critical for peptide transport and identification of 35 single point mutations that result in a full or partial loss of transport activity
additional information
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construction of SecA N-terminal deletion mutants. The first small helix, the linker and part of the second helix (residues 2-22) are dispensable for SecA activity in complementing the growth of a SecA temperature-sensitive mutant. Deletions of N-terminal aminoacyl residues 23-25 result in severe progressive retardation of growth. A decrease of SecA activity caused by N-terminal deletions correlates to the loss of SecA membrane binding, formation of lipid-specific domains and channel activity. The N-terminal aminoacyl residues 23-25 play a critical role for SecA binding to membranes and the N-terminal limit of SecA for activity is at the 25th amino acid
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mutant pairs of TAP1/TAP2 with mutation in ABC signature motif, C-loop. Chimera with two canonical C-loops show highest transport activity, chimera with two degenerate C-loops have lowest transport rates. All single mutants and chimera show similar activities in peptide or ATP binding
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knockdown of the ABC transporter enzyme in WM793B cells by shRNA leads to increases the sensitivity of cells to doxorubicin and reduces the cell survival, overview
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analysis of the function of SecA1 and SecA2 via several mutants
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analysis of the function of SecA1 and SecA2 via several mutants
additional information
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analysis of the function of SecA1 and SecA2 via several mutants
additional information
analysis of the function of SecA1 and SecA2 via several mutants
additional information
analysis of the function of SecA1 and SecA2 via several mutants
additional information
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analysis of the function of SecA1 and SecA2 via several mutants
additional information
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isoform PTR6 is able to complement transport defects in a yeast ptr2 mutant strain
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analysis of the function of SecA via mutants and SecA-SecA2-chimeras
additional information
analysis of the function of SecA via mutants and SecA-SecA2-chimeras
additional information
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analysis of the function of SecA via mutants and SecA-SecA2-chimeras
additional information
analysis of the function of SecA2 via mutants and SecA-SecA2-chimeras
additional information
analysis of the function of SecA2 via mutants and SecA-SecA2-chimeras
additional information
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analysis of the function of SecA2 via mutants and SecA-SecA2-chimeras
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