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VIBCH:Q9KSQ6

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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) Trypsin, putative (ECO:0000313 with EMBL:AAF94359.1)
External Links
UniProt Q9KSQ6
EMBL AE003852
PIR C82228
RefSeq NP_230845.1
PDB 4LK4
PDBsum 4LK4
ProteinModelPortal Q9KSQ6
STRING 243277.VC1200
MEROPS S01.516
DNASU 2614633
EnsemblBacteria AAF94359
GeneID 2614633
KEGG vch:VC1200
PATRIC 20081488
OMA WIKSNLV
OrthoDB EOG6VMTQS
BioCyc VCHO:VC1200-MONOMER
Proteomes UP000000584
GO GO:0004252
GO:0006508
InterPro IPR020008
IPR001254
IPR018114
IPR001314
IPR009003
Pfam PF00089
PRINTS PR00722
SMART SM00020
SUPFAM SSF50494
TIGRFAMs TIGR03501
PROSITE PS50240
PS00134
PS00135

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008236

serine-type peptidase activity

PMID:21385872[1]

ECO:0000315

F

Figure 2B shows that there is a dramatic decrease in hydrolase activity when VesB is knocked out. This indicates that VesB is responsible for the hydrolase activity in the wild type Vibrio cholerae. Hydrolysis was tested for using a peptide as substrate, and therefore it is a peptidase.

In addition Figure 3B show that the serine protease inhibitor AEBSF and the serine/cysteine protease inhibitor significantly inhibited the VesB protein.

complete

GO:0051605

protein maturation by peptide bond cleavage

PMID:21385872[1]

ECO:0000315

P

Figures 5 & 6 show that VesB is involved in processing the cholera toxin A subunit. In absence of VesB, the cholera toxin A subunit remained largely uncleaved. This is also discussed in results and discussion

complete

GO:0005615

extracellular space

PMID:24459146[2]

ECO:0000314

C

Supernatant and cell extracts from three different bacteria culture strains(VesA,VesB,VesC) were subject to SDS-Page and Western blot using anti-VesB antibodies to demonstrate secretion. Figure 4b

complete
CACAO 10713

GO:0008236

serine-type peptidase activity

PMID:24459146[2]

ECO:0000315

F

When subjected to serine protease inhibitors, its protease activity was effected.Figure 2 Protease activity was measured using different commercially available synthetic peptides to determine substrate specificity and subjected to a serine peptidase specific inhibitor. Figure 3A and 3B

complete
CACAO 10716

enables

GO:0008236

serine-type peptidase activity

PMID:24459146[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:10952301[3]

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

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

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

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

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: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

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

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 2.2 Gadwal, S et al. (2014) Functional and structural characterization of Vibrio cholerae extracellular serine protease B, VesB. J. Biol. Chem. 289 8288-98 PubMed GONUTS page
  3. Heidelberg, JF et al. (2000) DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature 406 477-83 PubMed GONUTS page