Information on EC 3.6.3.23 - oligopeptide-transporting ATPase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.6.3.23
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RECOMMENDED NAME
GeneOntology No.
oligopeptide-transporting ATPase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + oligopeptide/out = ADP + phosphate + oligopeptide/in
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric acid anhydride
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (oligopeptide-importing)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A bacterial enzyme that imports di- and oligopeptides.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozyme AtOPT6
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Manually annotated by BRENDA team
strain N40
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Manually annotated by BRENDA team
strain SS320
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Manually annotated by BRENDA team
strain SS320
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
no activity in: Xanthomonas campestris
pv. campestris
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Manually annotated by BRENDA team
group A streptococci, i.e. GAS, strains SW507 and A-20, genes oppA, oppB, oppC, oppD, and oppF, encoding isozymes OppA, OppB, OppC, OppD, and OppF
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Manually annotated by BRENDA team
ami genes encoded peptide transporter system, strains LMD-9, GCNRZ1066, and LMG18311 posessing two or three oligopeptide-binding proteins
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Manually annotated by BRENDA team
orf7, isozyme oppA1; ATCC 24076, genes oppA1 and oppA2
SwissProt
Manually annotated by BRENDA team
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette, ABC, transporter
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Manually annotated by BRENDA team
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette, ABC, transporter
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Manually annotated by BRENDA team
bldK, a gene cluster that encodes the components of an oligopeptide permease family of the ATP-binding cassette, ABC, transporter
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Manually annotated by BRENDA team
gene oppA
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + AtCLE19p12/out
ADP + phosphate + AtCLE19p12/in
show the reaction diagram
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in Xenopus laevis oocytes, injected with AtOPT6 cRNA
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?
ATP + H2O + bradykinin/out
ADP + phosphate + bradykinin/in
show the reaction diagram
ATP + H2O + CLE/out
ADP + phosphate + CLE/in
show the reaction diagram
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in Xenopus laevis oocytes, injected with AtOPT6 cRNA, CLE is transported by AtOPT6 with high affinity
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?
ATP + H2O + GGFL/out
ADP + phosphate + GGFL/in
show the reaction diagram
ATP + H2O + GGFM/out
ADP + phosphate + GGFM/in
show the reaction diagram
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in Xenopus laevis oocytes, injected with AtOPT6 cRNA
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?
ATP + H2O + GSH/out
ADP + phosphate + GSH/in
show the reaction diagram
ATP + H2O + GSSG/out
ADP + phosphate + GSSG/in
show the reaction diagram
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in Xenopus laevis oocytes, injected with ScOPT1 cRNA
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?
ATP + H2O + KLG/out
ADP + phosphate + KLG/in
show the reaction diagram
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in Xenopus laevis oocytes, injected with AtOPT6 cRNA
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?
ATP + H2O + KLGL/out
ADP + phosphate + KLGL/in
show the reaction diagram
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in Xenopus laevis oocytes, injected with AtOPT6 cRNA
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?
ATP + H2O + KLLLG/out
ADP + phosphate + KLLLG/in
show the reaction diagram
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in Xenopus laevis oocytes, injected with AtOPT6 cRNA
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?
ATP + H2O + KLLLLG/out
ADP + phosphate + KLLLLG/in
show the reaction diagram
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in Xenopus laevis oocytes, injected with AtOPT6 cRNA
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?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
show the reaction diagram
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
show the reaction diagram
ATP + H2O + phosphinotricyl-alanyl-alanine/out
ADP + phosphate + phosphinotricyl-alanyl-alanine/in
show the reaction diagram
ATP + H2O + phytochelatin/out
ADP + phosphate + phytochelatin/in
show the reaction diagram
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + bradykinin/out
ADP + phosphate + bradykinin/in
show the reaction diagram
Q9LCV8
i.e. RPPGFSPFR, specific for isozyme OppA2
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?
ATP + H2O + oligopeptide/out
ADP + phosphate + oligopeptide/in
show the reaction diagram
ATP + H2O + olipopeptide/out
ADP + phosphate + oligopeptide/in
show the reaction diagram
ATP + H2O + phosphinotricyl-alanyl-alanine/out
ADP + phosphate + phosphinotricyl-alanyl-alanine/in
show the reaction diagram
Q9LCV8
import of the toxic tripeptide, isozymes OppA1 and OppA2
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?
ATP + H2O + polar amino acid/out
ADP + phosphate + polar amino acid/in
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4',4'-diisothiocyanostilbene-2,2'-disulfonate
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i.e. DIDS
4',4'-diisothiocyanostylbene-2',2'-disulfonic acid
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0.5 mM, about 25% residual activity
5'-fluorosulfonyl-benzoyladenosine
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1 mM, about 25% residual activity
Trypsin
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tryptic digestion of OppA was protected by ATP and ADP but not by GTP or CTP
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18
ATP
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pH 7.5, 37°C
additional information
additional information
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PepT1 shows an increase in apparent substrate affinity at acidic pH, kinetics at pH 6.0-8.0, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
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or lower, substrate binding proteins OppA2, OppA3
additional information
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PepT1 activity is pH-dependent and shows an increase in apparent substrate affinity at acidic pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
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substrate binding protein OppA1
6 - 8
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pH-dependent activity, kinetics, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 4.7
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isoelectric focusing, OppA3
5.5
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isoelectric focusing, OppA5
6
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isoelectric focusing, OppA1; isoelectric focusing, OppA2; isoelectric focusing, OppA4
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PepT1 is expressed in the epithelium throughout the digestive system except the esophagus and sphincter regions
Manually annotated by BRENDA team
expression of PepT1 increases during development when the larvae are feeded with zooplankton instead of rotifers
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32800
x * 32800, deduced from gene sequence, membrane component of permease system
36000
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x * 36000, SDS-PAGE
58000
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x * 58000, mature enzyme, SDS-PAGE
59000
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x * 59000, Opp-3, SDS-PAGE
60000
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x * 60000, recombinant selenium-labeled, detagged soluble AppA, SDS-PAGE
60700
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x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
60800
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x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
61000
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x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
61700
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x * 61700, calculated from amino acid sequence
62400
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x * 59900, OppA1, x * 60700, OppA2, x * 62400, OppA3, x * 60800, OppA4, x * 61000, OppA5
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
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molecular dynamics simulations, with the protein maintaing the overall open structure and shape, and structure modelling
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lipoprotein
additional information
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OppA is complexed with proline-rich endogenous peptides, MALDI tandem mass spectrometry peptide analysis, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified soluble form of AppA in complex with a nonapeptide, hanging drop vapour diffusion method, unlabeled enzyme from 12-14% PEG 8000, 0.1-0.2 M zinc acetate, 0.1 M MES, pH 6.5, or Tris-HCl, pH 7.5, selenium-labeled enzyme from 16-18% PEG 8000, 0.1 M zinc acetate, and 0.1 M MES, pH 6.5, or Tris-HCl, pH 7.5, cryoprotection by 25% v/v glycerol, X-ray diffraction structure determination and analysis at 2.3-1.6 A resolution, selenium-based anomalous scattering and molecular replacement methods
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OppA in the open-and closed-liganded conformation, complexed with bradykinin, the nonapeptide RPPGFSPFR, hanging drop vapour diffusion method, 0.001 ml of protein solution are mixed with 10 mg/ml ligand-free OppA, 9 mM Na-MES, pH 6.0, 9 mM NaCl and 1 mM peptide, is mixed with 0.001 ml of reservoir solution containing 0.2 M NaCl, 0.1 M Na-HEPES, pH 7.0, and 20% PEG 6000, 12 weeks at room temperature, X-ray diffraction structure determination and analysis at 1.3 and 2.5 A resolution, respectively
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50.6
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purified recombinant enzyme displays a melting temperature of 50.6°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; TALON metal affinity resin column chromatography
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OppA without lipid anchor is produced in the cytoplasm of Lactobacillus lactis where endogenous peptides are available for binding. These peptides bind so tightly that they remain associated with the protein throughout the purification, they can be removed from the protein only by guanidium chloride treatment generating ligand-free OppA
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recombinant His-tagged wild-type and mutant enzymes from Lactococcus lactis by nickel affinity chromatography
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recombinant refolded and soluble His-tagged OppA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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recombinant selenium-labeled maltose-binding fusion protein by amylose affinity chromatography, cleavage of the fusion protein by factor Xa, further purification by ion exchange chromatography and gel filtration, to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Escherichia coli BL21(DE3) cells
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cloning and gene organization of the bldK locus, overview
cloning in Escherichia coli JM109, PepT1 translation in Xenopus oocytes
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DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression using the pAN701 plasmid
expressed in Lactococcus lactis strain NZ9000
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expressed in lung, liver and spleen of mice
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expression of Arabidopsis thaliana AtOPT6 in oocytes by swapping the 5'-untranslated region of AtOPT6 with the 5'-UTR of ScOPT1 from Saccharomyces cerevisiae
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expression of C-terminal His6-tagged OppA, OppA I602C, and OppBCDF His6-tag on C-terminus of OppC in Lactococcus lactis
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four opp operons, opp-1, opp-2, opp-3, and opp-4, plus an opp-5A gene encoding a putative peptide-binding protein, DNA and amino acid sequence determination and analysis, opp-1, opp-2, opp-3, and opp-4 operons are polycistronic and opp-5A is monocistronic, transcriptional profiles and sequence comparison. Gene opp-3, which encodes proteins most similar to known peptide transport proteins, displays the highest expression level, overview
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gene appA, expression of soluble form of AppA fused to maltose-binding protein in Escherichia coli strain B834 periplasm
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gene oppA, DNA and amino acid sequence determination and analysis, expression of the wild-type enzyme in Escherichia coli strain BL21(DE3)
gene oppA, DNA and amino acid sequence determination and anaylsis, expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) as mainly insoluble protein
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library construction and subcloning in Escherichia coli strains XL-1 Blue and SM10, opp gene cluster encoding five isozymes OppA, OppB, OppC, OppD, and OppF, DNA and amino acid sequence determination and analysis; library construction and subcloning in Escherichia coli strains XL-1 Blue and SM10, opp gene cluster encoding five isozymes OppA, OppB, OppC, OppD, and OppF, DNA and amino acid sequence determination and analysis; library construction and subcloning in Escherichia coli strains XL-1 Blue and SM10, opp gene cluster encoding five isozymes OppA, OppB, OppC, OppD, and OppF, DNA and amino acid sequence determination and analysis; library construction and subcloning in Escherichia coli strains XL-1 Blue and SM10, opp gene cluster encoding five isozymes OppA, OppB, OppC, OppD, and OppF, DNA and amino acid sequence determination and analysis; library construction and subcloning in Escherichia coli strains XL-1 Blue and SM10, opp gene cluster encoding five isozymes OppA, OppB, OppC, OppD, and OppF, DNA and amino acid sequence determination and analysis, expression in Vibrio fluvialis and Escherichia coli
operon of genes oppA1, oppA2, oppB, oppC, oppD, oppF
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opp, genome-wide transcriptional profiling
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optimization of AtOPT6 expression in oocytes by swapping the 5'-untranslated region of AtOPT6 with the 5'-UTR of ScOPT1 from Saccharomyces cerevisiae
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PepT1 expression as sense and antisense construct
the expression of the OppA proteins is individually regulated, alternative sigma factors, RpoS and RpoN, regulate the expression of oppA5 but not that of other oppA genes, while BosR/Fur homologue interacts with the oppA4 promoter and another candidate transcription factor, EbfC, interacts with the oppA5 promoter, overview
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the two genes oppA1 and oppA2 encoding oligopeptide permeases are located in the clavulinic acid cluster, DNA and amino acid sequence determination and analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CgOpt1 expression is induced by iodoacetic acid. Iodoacetic acid enhances spore formation and causes changes in colony morphology in the wild-type strain, but has no effect on spore formation or colony morphology of the cgopt1-silenced mutants
enzyme expression is upregulated in abscesses and iron-restricted culture medium
transcription of bldKB-g is significantly reduced in the DELTAadpA mutant strain compared with the wild-type strain
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D449N
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OppA mutant, able to grow in presence of 0.02 mg/ml of the toxic tripeptide bialaphos, reduced sporulation rate
E239K
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OppA mutant, able to grow in presence of 0.32 mg/ml of the toxic tripeptide bialaphos, drastically reduced sporulation rate
E259K
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OppA mutant, able to grow in presence of 0.16 mg/ml of the toxic tripeptide bialaphos
G299E
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OppA mutant, able to grow in presence of 0.16 mg/ml of the toxic tripeptide bialaphos, reduced sporulation rate
G337R
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OppA mutant, able to grow in presence of 0.01 mg/ml of the toxic tripeptide bialaphos, increased sporulation rate
G466E
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OppA mutant, able to grow in presence of 0.02 mg/ml of the toxic tripeptide bialaphos, reduced sporulation rate
R443H
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OppA mutant, able to grow in presence of 0.16 mg/ml of the toxic tripeptide bialaphos, drastically reduced sporulation rate
I602C
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OppA mutant, comparison to the wild-type enzyme in reconstitution in the membrane, substrate binding, and catalysis
K875R
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Oppa, decrease in ATPhydrolysis to 15% of wild-tpe
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
OppA and OppBCDF are reconstituted into giant unilamellar vesicles, overview
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solubilization and refolding of recombinant insoluble His-tagged OppA expressed in Escherichia coli strain BL21(DE3) by dilution with 100fold volumes of refolding buffer, PBS, pH 7.4, containing 1 M urea, 10% glycerol, 0.005% Tween 20, 0.5 mM PMSF and 5 mM DTT, and maintainance under vigorous agitation at 4°C for 8 h
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