3.4.21.89: Signal peptidase I
This is an abbreviated version!
For detailed information about Signal peptidase I, go to the full flat file.
Word Map on EC 3.4.21.89
-
3.4.21.89
-
polyproteins
-
lipoprotein
-
preproteins
-
cleavable
-
foot-and-mouth
-
unprocessed
-
dyad
-
membrane-spanning
-
prolipoproteins
-
translocons
-
pilins
-
uncleaved
-
beta-lactamase
-
drug development
-
flavivirus
-
ompa
-
nonstructural
-
cotranslationally
-
co-translational
-
sec-dependent
-
globomycin
-
presequence
-
papain-like
-
prepeptide
-
polytopic
-
oligonucleotide-directed
-
ns2b
-
signal-anchored
-
pharmacology
-
medicine
-
analysis
- 3.4.21.89
- polyproteins
- lipoprotein
- preproteins
-
cleavable
- foot-and-mouth
-
unprocessed
-
dyad
-
membrane-spanning
- prolipoproteins
-
translocons
- pilins
-
uncleaved
- beta-lactamase
- drug development
- flavivirus
- ompa
-
nonstructural
-
cotranslationally
-
co-translational
-
sec-dependent
- globomycin
- presequence
-
papain-like
- prepeptide
-
polytopic
-
oligonucleotide-directed
- ns2b
-
signal-anchored
- pharmacology
- medicine
- analysis
Reaction
Cleavage of hydrophobic, N-terminal signal or leader sequences =
Synonyms
Bacterial leader peptidase 1, bacterial type I signal peptidase, big signal peptidase, canine signal peptidase complex, chloroplast processing peptidase, EC 3.4.99.36, Escherichia coli leader peptidase, Eukaryotic signal peptidase, Eukaryotic signal proteinase, hen oviduct signal peptidase, HOSP, imp1p, Leader peptidase, Leader peptidase I, Leader peptide hydrolase, Leader proteinase, LEP, LepB, PA1303, Pcp1, Peptidase, signal, Pilin leader peptidase, plastidic SPase I, plastidic SPase I 1, plastidic type I signal peptidase 1, Plsp1, Prokaryotic leader peptidase, Prokaryotic signal peptidase, Prokaryotic signal proteinase, Propeptidase, protease IV, Proteinase, eukaryotic signal, Proteinase, signal, PuIO prepilin peptidase, Rv2903c, SEC11, secretory protein 11, Signal peptidase, signal peptidase I, signal peptidase I-3, Signal peptidase IB, signal peptidase type I, Signal peptide hydrolase, Signal peptide peptidase, Signalase, Sip1, Sip2, Sip3, SipP (pTA1015), SipP (pTA1040), SipS, SipT, SipU, SipV, SipW, SipX, SipY, SipZ, SP, SP I, SP-I, SPase, Spase I, SPase I 1, SPase IB, SPaseI, SPC, Spc1, SPI, SPP, SpsB, thylakoidal processing peptidase, TPP, type I signal (leader) peptidase, type I signal peptidase, type I signal peptidase 1, type I signal peptidase Sec11a, type I signal peptidase Sec11b, type I SPase
ECTree
3.4.21.89 Signal peptidase IAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.21.89 - Signal peptidase I
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
I144C
50% of wild-type activity, mutant enzyme cleaves at multiple sites
I86A/I144A
mutant enzyme is able to cleave after Phe at the -1 residue
R222A
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value. Thermostability is significantly lower compared to the wild-type enzyme
R222K
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value. Thermostability is significantly lower compared to the wild-type enzyme
R315A
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value. Thermostability is significantly lower compared to the wild-type enzyme
R318A
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value
R318K
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value. Thermostability is significantly lower compared to the wild-type enzyme
R77A
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value
R77K
-
kcat is about 5.5fold smaller than the wild-type value, Km-is almost identical to wild-type value
W261F/W284F/W300F
mutant based on deletion mutant DELTA2-75. Mutant contains one remaining Trp residue and is able to insert into lipids
W261F/W284F/W310F
mutant based on deletion mutant DELTA2-75. Mutant contains one remaining Trp residue and is able to insert into lipids
W261F/W300F/W310F
mutant based on deletion mutant DELTA2-75. Mutant contains one remaining Trp residue, its solvent accesibilities are modified in the presence of signal peptide
W284F/W300F/W310F
mutant based on deletion mutant DELTA2-75. Mutant contains one remaining Trp residue, its solvent accesibilities are modified in the presence of signal peptide
S36A
D215A
-
Vmax is 1.8fold lower than wild-type value, kcat is 1.8 fold lower than wild-type enzyme
D277A
-
Vmax is 1.6fold higher than wild-type value, kcat is 1.6fold higher than wild-type enzyme
E226A
-
Vmax is 1.35fold higher than wild-type value, kcat is 1.3fold higher than wild-type enzyme
E227A
-
Vmax is is nearly identical to wild-type value, kcat nearly identical to wild-type enzyme
H191A
-
Vmax is 1.84fold lower than wild-type value, kcat is 1.9fold lower than wild-type enzyme
K150A
-
Vmax is 1.5fold higher than wild-type value, kcat is 1.4fold higher than wild-type enzyme
K209A
-
Vmax is 1.7fold lower than wild-type value, kcat is 1.8fold lower than wild-type enzyme
R221A
-
Vmax is 7.8fold lower than wild-type value, kcat is 8fold lower than wild-type enzyme
R250A
-
Vmax is 1.5fold higher than wild-type value, kcat is 1.4fold higher than wild-type enzyme
S128A
-
Vmax is 6.9 fold higher than wild-type value, kcat is 6.2fold higher than wild-type enzyme
S184A
-
Vmax is 4fold lower than wild-type value, kcat is 4fold lower than wild-type enzyme
Y165A
-
Vmax is 2.3fold higher than wild-type value, kcat is 2.3fold higher than wild-type enzyme
P91S
-
construction of LepB(P91S) mutant strain DBS600 via allelic exchange and site-directed mutagenesis to introduce the point mutation. The mutant can be complemented by expression of wild-type SPase from Yersinia pestis or Escherichia coli
additional information
additional information
-
disruption of PLSP1 expression by a T-DNA insertion causes a seedling lethal phenotype in which development of internal membranes was severely retarded in cotyledon plastids. Construction of a plsp1-null mutant. Plastids that lack Plsp1 accumulate vesicles of variable sizes in the stroma, and they cause a reduction in accumulation of thylakoid proteins and that Plsp1 is involved in maturation of two additional lumenal proteins, OE23 and plastocyanin. OE33 associates with the stromal vesicles of the mutant plastids. Accumulation of improperly processed forms of Toc75 in the plastid envelope does not disrupt normal plant development, presence of posttranscriptional suppression of thylakoid protein accumulation in plsp1-1 plants, phenotype, overview
additional information
construction of a N-terminally truncated enzyme lacking amino acids 1-134 and a full-length mature form containing the trans-membrane domain but lacking the transit peptide. N-terminally truncated variant shows very poor activity with PsbO substrate
additional information
-
construction of a N-terminally truncated enzyme lacking amino acids 1-134 and a full-length mature form containing the trans-membrane domain but lacking the transit peptide. N-terminally truncated variant shows very poor activity with PsbO substrate
additional information
using a heterologous system, targeting of Arabidopsis thaliana Plsp1 to pea chloroplasts/chloroplast membranes is performed
additional information
-
using a heterologous system, targeting of Arabidopsis thaliana Plsp1 to pea chloroplasts/chloroplast membranes is performed
additional information
-
expression of a soluble form of signal peptidase, which lacks the two transmembrane domains, SPase I DELTA2-75
additional information
-
variant DELTA2-75 is a soluble form of signal peptidase, which lacks the two transmembrane domains
additional information
generation of a DELTA2-76 truncated enzyme mutant by deletion. The mutant is soluble and lacks both N-terminal transmembrane domains
additional information
-
generation of a DELTA2-76 truncated enzyme mutant by deletion. The mutant is soluble and lacks both N-terminal transmembrane domains
additional information
-
construction of a null mutant of SPase I is not possible, suggesting that SPase I is an essential gene for parasite survival. The obtained heterozygote mutant by disrupting one allele of SPase I show significantly reduced level of infectivity in bone marrow-derived macrophages. The heterozygote mutants are unable to cause cutaneous lesion in susceptible BALB/c mice. Comparison of in vivo infectivity potential of DELTAspase::NEO/SPase heterozygote mutant and wild-type parasites, overview
additional information
-
construction of a null mutant of SPase I is not possible, suggesting that SPase I is an essential gene for parasite survival. The obtained heterozygote mutant by disrupting one allele of SPase I show significantly reduced level of infectivity in bone marrow-derived macrophages. The heterozygote mutants are unable to cause cutaneous lesion in susceptible BALB/c mice. Comparison of in vivo infectivity potential of DELTAspase::NEO/SPase heterozygote mutant and wild-type parasites, overview
-
additional information
inactivation of sipM by targeted gene disruption cannot be achieved, indicating its essential role for cell viability
additional information
-
inactivation of sipM by targeted gene disruption cannot be achieved, indicating its essential role for cell viability
additional information
-
a truncated derivative of SpsB, which is nine amino acids longer at the N-terminus compared to the self-cleavage product, retains activity
additional information
generation of Staphylococcus aureus bacteria lacking the SPase I SpsB, KIM6+ phoP knockout strain
additional information
-
generation of Staphylococcus aureus bacteria lacking the SPase I SpsB, KIM6+ phoP knockout strain
additional information
generation of the biofilm mutant, DELTASSA_0351, that is deficient in type I signal peptidase (SPase). Although the growth curve of the DSSA_0351 mutant shows no significant difference from that of the wild-type strain SK36, biofilm assays using both microtitre plate assay and confocal laser scanning microscopy (CLSM) confirmed a sharp reduction in biofilm formation in the mutant compared to the wild-type strain and the paralogous mutant DSSA_0849. Evaluation of the functional impact of SPase on biofilm formation, transcriptome analysis compared to wild-type, overview. The growth rates of the wild-type, DSSA_0849 and DSSA_0351 strains are not significantly different. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
additional information
-
generation of the biofilm mutant, DELTASSA_0351, that is deficient in type I signal peptidase (SPase). Although the growth curve of the DSSA_0351 mutant shows no significant difference from that of the wild-type strain SK36, biofilm assays using both microtitre plate assay and confocal laser scanning microscopy (CLSM) confirmed a sharp reduction in biofilm formation in the mutant compared to the wild-type strain and the paralogous mutant DSSA_0849. Evaluation of the functional impact of SPase on biofilm formation, transcriptome analysis compared to wild-type, overview. The growth rates of the wild-type, DSSA_0849 and DSSA_0351 strains are not significantly different. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
additional information
-
generation of the biofilm mutant, DELTASSA_0351, that is deficient in type I signal peptidase (SPase). Although the growth curve of the DSSA_0351 mutant shows no significant difference from that of the wild-type strain SK36, biofilm assays using both microtitre plate assay and confocal laser scanning microscopy (CLSM) confirmed a sharp reduction in biofilm formation in the mutant compared to the wild-type strain and the paralogous mutant DSSA_0849. Evaluation of the functional impact of SPase on biofilm formation, transcriptome analysis compared to wild-type, overview. The growth rates of the wild-type, DSSA_0849 and DSSA_0351 strains are not significantly different. Proteomic analysis of mutant strain DELTASSA_0351, list of transcripts that are differentially regulated in DELTASSA_0351
-
additional information
-
a truncated protein without the N-terminal 54 residues and putative transmembrane domain, exhibits high peptidase activity, and is used as the wild-type protein
