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VIBCH:HLYA

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Species (Taxon ID) Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). (243277)
Gene Name(s) hlyA
Protein Name(s) Hemolysin
External Links
UniProt P09545
EMBL Y00557
M36855
X51746
AE003853
PIR A41462
A82486
RefSeq NP_232618.1
PDB 1XEZ
PDBsum 1XEZ
ProteinModelPortal P09545
SMR P09545
MINT MINT-8391645
STRING 243277.VCA0219
TCDB 1.C.14.1.1
DNASU 2612877
EnsemblBacteria AAF96131
GeneID 2612877
KEGG vch:VCA0219
PATRIC 20085001
eggNOG NOG264759
KO K10948
OMA HVAFYLN
OrthoDB EOG61KBCC
BioCyc VCHO:VCA0219-MONOMER
EvolutionaryTrace P09545
Proteomes UP000000584
GO GO:0020002
GO:0016021
GO:0030246
GO:0042802
GO:0044179
Gene3D 2.70.240.10
InterPro IPR022220
IPR016183
IPR000772
Pfam PF12563
PF07968
PF00652
SMART SM00458
SUPFAM SSF50370
SSF56959
PROSITE PS50231

Annotations

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

enables

GO:0042802

identical protein binding

PMID:22934938[1]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P09545

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:19854900[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P09545

F

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0090729

P

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016183

C

Seeded From UniProt

complete

involved_in

GO:0051715

cytolysis in other organism

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016183

P

Seeded From UniProt

complete

involved_in

GO:0044179

hemolysis in other organism

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0354

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0033644

host cell membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1043

C

Seeded From UniProt

complete

enables

GO:0090729

toxin activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0800

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0030246

carbohydrate binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0430

F

Seeded From UniProt

complete

part_of

GO:0020002

host cell plasma membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1032
UniProtKB-SubCell:SL-0375

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

involved_in

GO:0019835

cytolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0204

P

Seeded From UniProt

complete

Notes

References

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

  1. Paul, K & Chattopadhyay, K (2012) Single point mutation in Vibrio cholerae cytolysin compromises the membrane pore-formation mechanism of the toxin. FEBS J. 279 4039-51 PubMed GONUTS page
  2. Dutta, S et al. (2010) Three-dimensional structure of different functional forms of the Vibrio cholerae hemolysin oligomer: a cryo-electron microscopic study. J. Bacteriol. 192 169-78 PubMed GONUTS page