ID   RTXC_VIBCH              Reviewed;         153 AA.
AC   Q9X4W3; Q9JQ03;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Lysine-acyltransferase RtxC;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P55132};
GN   Name=rtxC; OrderedLocusNames=VC_1450;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=9927695; DOI=10.1073/pnas.96.3.1071;
RA   Lin W., Fullner K.J., Clayton R., Sexton J.A., Rogers M.B., Calia K.E.,
RA   Calderwood S.B., Fraser C., Mekalanos J.J.;
RT   "Identification of a vibrio cholerae RTX toxin gene cluster that is tightly
RT   linked to the cholera toxin prophage.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1071-1076(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=4260B / Serotype O139;
RX   PubMed=19900531; DOI=10.1016/j.micpath.2009.11.001;
RA   Cheong T.G., Chan M., Kurunathan S., Ali S.A., ZiNing T., Zainuddin Z.F.,
RA   Lalitha P., Ravichandran M.;
RT   "Construction and characterization of rtxA and rtxC mutants of auxotrophic
RT   O139 Vibrio cholerae.";
RL   Microb. Pathog. 48:85-90(2010).
CC   -!- FUNCTION: Catalyzes fatty acylation of the protoxin (RtxA) at internal
CC       lysine residues, thereby converting it to the active toxin.
CC       {ECO:0000250|UniProtKB:P55132}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + L-lysyl-[protein] = H(+) + holo-[ACP] +
CC         N(6)-(fatty acyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:70667, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14125, Rhea:RHEA-
CC         COMP:17946, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:138651, ChEBI:CHEBI:189854;
CC         Evidence={ECO:0000250|UniProtKB:P55132};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70668;
CC         Evidence={ECO:0000250|UniProtKB:P55132};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking RtxC do not show reduced toxicity
CC       (PubMed:19900531). However, the RtxA toxin displays reduced actin
CC       cross-linking activity (PubMed:19900531).
CC       {ECO:0000269|PubMed:19900531}.
CC   -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF119150; AAD21058.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF94607.1; -; Genomic_DNA.
DR   PIR; B82199; B82199.
DR   RefSeq; NP_231093.1; NC_002505.1.
DR   RefSeq; WP_001881196.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9X4W3; -.
DR   SMR; Q9X4W3; -.
DR   STRING; 243277.VC_1450; -.
DR   DNASU; 2613956; -.
DR   EnsemblBacteria; AAF94607; AAF94607; VC_1450.
DR   GeneID; 57740103; -.
DR   GeneID; 66939345; -.
DR   KEGG; vch:VC_1450; -.
DR   PATRIC; fig|243277.26.peg.1380; -.
DR   eggNOG; COG2994; Bacteria.
DR   HOGENOM; CLU_116529_1_0_6; -.
DR   OMA; CNWAFLS; -.
DR   BioCyc; VCHO:VC1450-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009404; P:toxin metabolic process; IEA:InterPro.
DR   InterPro; IPR003996; RTX_toxin-activating_protC_bac.
DR   Pfam; PF02794; HlyC; 1.
DR   PRINTS; PR01489; RTXTOXINC.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytolysis; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..153
FT                   /note="Lysine-acyltransferase RtxC"
FT                   /id="PRO_0000217887"
FT   ACT_SITE        32
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
SQ   SEQUENCE   153 AA;  17895 MW;  31089224943F4449 CRC64;
     MSITHQPANL TLAQIQQMIG GVMLLSQHSP LHRRYVVAEW LQRILPAFEL NQFCYYEDEH
     GRPIAFCNWA FVSEQIRDEL LSGVREISPS DWRSGQQIYI PEMIAPFGHG REVVNDLRRR
     VFLPWQGQKV CTVRGKVDAQ NDRCIRKVQW FSI