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VIBCH:Q9KLE3

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Species (Taxon ID) Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). (243277)
Gene Name(s) No Information Provided.
Protein Name(s) Serine protease, putative (ECO:0000313 with EMBL:AAF96701.1)
External Links
UniProt Q9KLE3
EMBL AE003853
PIR B82415
RefSeq NP_233189.1
ProteinModelPortal Q9KLE3
STRING 243277.VCA0803
MEROPS S01.515
DNASU 2612776
EnsemblBacteria AAF96701
GeneID 2612776
KEGG vch:VCA0803
PATRIC 20086154
OMA AHCVDYQ
OrthoDB EOG6VMTQS
BioCyc VCHO:VCA0803-MONOMER
Proteomes UP000000584
GO GO:0008233
GO:0004252
GO:0006508
InterPro IPR001254
IPR018114
IPR001314
IPR009003
Pfam PF00089
PRINTS PR00722
SMART SM00020
SUPFAM SSF50494
PROSITE PS50240
PS00134
PS00135

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0051605

protein maturation by peptide bond cleavage

PMID:21385872[1]

ECO:0000315

P

Fig 5 A-B VesA is responsible for the majority of the proteolytic cleavage of the Cholerae Toxin A subunit. In absence of VesA up to 80% of the Cholerae Toxin remained unprocessed

complete

GO:0008236

serine-type peptidase activity

PMID:21385872[1]

ECO:0000315

F

Figure 2B shows that VesA participates in hydrolysis of peptide bonds-i.e. peptidase activity.In addition overexpression of VesA resulted in an increase in enzymatic activity (Fig 3A). Figure 3A show that the serine protease inhibitor AEBSF and the serine/cysteine protease inhibitor significantly inhibited the VesA protein.

complete

enables

GO:0008233

peptidase activity

PMID:10952301[2]

ECO:0000250

sequence similarity evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

involved_in

GO:0006508

proteolysis

PMID:10952301[2]

ECO:0000250

sequence similarity evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

enables

GO:0004252

serine-type endopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001254
InterPro:IPR001314
InterPro:IPR018114

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001254
InterPro:IPR001314
InterPro:IPR018114

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0008236

serine-type peptidase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0720

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Sikora, AE et al. (2011) Proteomic analysis of the Vibrio cholerae type II secretome reveals new proteins, including three related serine proteases. J. Biol. Chem. 286 16555-66 PubMed GONUTS page
  2. 2.0 2.1 Heidelberg, JF et al. (2000) DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature 406 477-83 PubMed GONUTS page