VIBCH:Q9KS12

Species (Taxon ID)	Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). (243277)
Gene Name(s)	No Information Provided.
Protein Name(s)	RTX toxin RtxA (ECO:0000313 with EMBL:AAF94608.1)
External Links
UniProt	Q9KS12
EMBL	AE003852
PIR	C82199
RefSeq	NP_231094.1 WP_010895441.1
PDB	3EEB 3FZY 3GCD
PDBsum	3EEB 3FZY 3GCD
ProteinModelPortal	Q9KS12
STRING	243277.VC1451
MEROPS	C80.001
EnsemblBacteria	AAF94608
GeneID	2613957
KEGG	vch:VC1451
PATRIC	20081964
KO	K10953
OMA	NIFTHIG
OrthoDB	EOG6BS8KR
BioCyc	VCHO:VC1451-MONOMER
EvolutionaryTrace	Q9KS12
Proteomes	UP000000584
GO	GO:0005509 GO:0019836 GO:0031640 GO:0009405
Gene3D	2.150.10.10 3.40.50.1820
InterPro	IPR029058 IPR020972 IPR020974 IPR011509 IPR011049
Pfam	PF11713 PF11647 PF07634
SUPFAM	SSF51120 SSF53474

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0009404	toxin metabolic process	PMID:19465933^[1]	ECO:0000315			P	Figures 3,4 and 5 describe the conserved domain of the cysteine protease domain and show that it is actively catabolizing products. #5 shows the cysteine protease domain binding site in vitro	complete CACAO 10132
part_of	GO:0020002	host cell plasma membrane	PMID:20212166^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0031640	killing of cells of other organism	PMID:10952301^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	NCBI_gi:4455065	P	Seeded From UniProt	complete
involved_in	GO:0019836	hemolysis by symbiont of host erythrocytes	PMID:10952301^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	NCBI_gi:4455065	P	Seeded From UniProt	complete
involved_in	GO:0009405	pathogenesis	PMID:10952301^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	NCBI_gi:4455065	P	Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:10952301^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	NCBI_gi:4455065	F	Seeded From UniProt	complete
involved_in	GO:0090527	actin filament reorganization	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR032074	P	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:17464284^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0018262	isopeptide cross-linking	PMID:19465933^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:19465933^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016540	protein autoprocessing	PMID:19465933^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:19465933^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009405	pathogenesis	PMID:19465933^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0000822	inositol hexakisphosphate binding	PMID:19465933^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016540	protein autoprocessing	PMID:18591243^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:18591243^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000822	inositol hexakisphosphate binding	PMID:18591243^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000822	inositol hexakisphosphate binding	PMID:18845756^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016540	protein autoprocessing	PMID:18845756^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:18845756^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0018262	isopeptide cross-linking	PMID:17464284^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:17464284^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016540	protein autoprocessing	PMID:17464284^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009405	pathogenesis	PMID:17464284^[4]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:11032799^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0009405	pathogenesis	PMID:11032799^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018262	isopeptide cross-linking	PMID:11032799^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:11032799^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018262	isopeptide cross-linking	PMID:16954226^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:16954226^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:16954226^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:16954226^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0018262	isopeptide cross-linking	PMID:15199181^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:15199181^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018153	isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine	PMID:19015515^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:19015515^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016881	acid-amino acid ligase activity	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0018153	isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:11032799^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0009405	pathogenesis	PMID:11032799^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018262	isopeptide cross-linking	PMID:11032799^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:11032799^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018262	isopeptide cross-linking	PMID:16954226^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:16954226^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:16954226^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:16954226^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0018262	isopeptide cross-linking	PMID:15199181^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:15199181^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0018153	isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine	PMID:19015515^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:19015515^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0018153	isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0030042	actin filament depolymerization	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0016881	acid-amino acid ligase activity	PMID:23029200^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0016540	protein autoprocessing	PMID:19620709^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004197	cysteine-type endopeptidase activity	PMID:19620709^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000822	inositol hexakisphosphate binding	PMID:19620709^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008234	cysteine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0788	F	Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	P	Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
part_of	GO:0030430	host cell cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1035	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
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
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P	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
enables	GO:0016874	ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0436	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	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
involved_in	GO:0009405	pathogenesis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0843	P	Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	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:0008289	lipid binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0446	F	Seeded From UniProt	complete
part_of	GO:0044164	host cell cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0384	C	Seeded From UniProt	complete
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Shen, A et al. (2009) Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin. Nat. Chem. Biol. 5 469-78 PubMed GONUTS page
↑ Geissler, B et al. (2010) Identification of a conserved membrane localization domain within numerous large bacterial protein toxins. Proc. Natl. Acad. Sci. U.S.A. 107 5581-6 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Heidelberg, JF et al. (2000) DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature 406 477-83 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Sheahan, KL et al. (2007) Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain. EMBO J. 26 2552-61 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Prochazkova, K & Satchell, KJ (2008) Structure-function analysis of inositol hexakisphosphate-induced autoprocessing of the Vibrio cholerae multifunctional autoprocessing RTX toxin. J. Biol. Chem. 283 23656-64 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Lupardus, PJ et al. (2008) Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain. Science 322 265-8 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 ^7.7 Fullner, KJ & Mekalanos, JJ (2000) In vivo covalent cross-linking of cellular actin by the Vibrio cholerae RTX toxin. EMBO J. 19 5315-23 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 ^8.7 Cordero, CL et al. (2006) The Actin cross-linking domain of the Vibrio cholerae RTX toxin directly catalyzes the covalent cross-linking of actin. J. Biol. Chem. 281 32366-74 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Sheahan, KL et al. (2004) Identification of a domain within the multifunctional Vibrio cholerae RTX toxin that covalently cross-links actin. Proc. Natl. Acad. Sci. U.S.A. 101 9798-803 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Kudryashov, DS et al. (2008) Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proc. Natl. Acad. Sci. U.S.A. 105 18537-42 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 ^11.7 ^11.8 ^11.9 Kudryashova, E et al. (2012) Glutamyl phosphate is an activated intermediate in actin crosslinking by actin crosslinking domain (ACD) toxin. PLoS ONE 7 e45721 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Prochazkova, K et al. (2009) Structural and molecular mechanism for autoprocessing of MARTX toxin of Vibrio cholerae at multiple sites. J. Biol. Chem. 284 26557-68 PubMed GONUTS page

[PMID:19465933-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 Shen, A et al. (2009) Mechanistic and structural insights into the proteolytic activation of Vibrio cholerae MARTX toxin. Nat. Chem. Biol. 5 469-78 PubMed GONUTS page

[PMID:20212166-2] Geissler, B et al. (2010) Identification of a conserved membrane localization domain within numerous large bacterial protein toxins. Proc. Natl. Acad. Sci. U.S.A. 107 5581-6 PubMed GONUTS page

[PMID:10952301-3] 3.0 ^3.1 ^3.2 ^3.3 Heidelberg, JF et al. (2000) DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae. Nature 406 477-83 PubMed GONUTS page

[PMID:17464284-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 Sheahan, KL et al. (2007) Autoprocessing of the Vibrio cholerae RTX toxin by the cysteine protease domain. EMBO J. 26 2552-61 PubMed GONUTS page

[PMID:18591243-5] 5.0 ^5.1 ^5.2 Prochazkova, K & Satchell, KJ (2008) Structure-function analysis of inositol hexakisphosphate-induced autoprocessing of the Vibrio cholerae multifunctional autoprocessing RTX toxin. J. Biol. Chem. 283 23656-64 PubMed GONUTS page

[PMID:18845756-6] 6.0 ^6.1 ^6.2 Lupardus, PJ et al. (2008) Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain. Science 322 265-8 PubMed GONUTS page

[PMID:11032799-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 ^7.7 Fullner, KJ & Mekalanos, JJ (2000) In vivo covalent cross-linking of cellular actin by the Vibrio cholerae RTX toxin. EMBO J. 19 5315-23 PubMed GONUTS page

[PMID:16954226-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 ^8.7 Cordero, CL et al. (2006) The Actin cross-linking domain of the Vibrio cholerae RTX toxin directly catalyzes the covalent cross-linking of actin. J. Biol. Chem. 281 32366-74 PubMed GONUTS page

[PMID:15199181-9] 9.0 ^9.1 ^9.2 ^9.3 Sheahan, KL et al. (2004) Identification of a domain within the multifunctional Vibrio cholerae RTX toxin that covalently cross-links actin. Proc. Natl. Acad. Sci. U.S.A. 101 9798-803 PubMed GONUTS page

[PMID:19015515-10] 10.0 ^10.1 ^10.2 ^10.3 Kudryashov, DS et al. (2008) Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Proc. Natl. Acad. Sci. U.S.A. 105 18537-42 PubMed GONUTS page

[PMID:23029200-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 ^11.7 ^11.8 ^11.9 Kudryashova, E et al. (2012) Glutamyl phosphate is an activated intermediate in actin crosslinking by actin crosslinking domain (ACD) toxin. PLoS ONE 7 e45721 PubMed GONUTS page

[PMID:19620709-12] 12.0 ^12.1 ^12.2 Prochazkova, K et al. (2009) Structural and molecular mechanism for autoprocessing of MARTX toxin of Vibrio cholerae at multiple sites. J. Biol. Chem. 284 26557-68 PubMed GONUTS page

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VIBCH:Q9KS12

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