RTX3C_ACTPL
ID RTX3C_ACTPL Reviewed; 173 AA.
AC Q04474;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=RTX-III toxin-activating lysine-acyltransferase ApxIIC;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P55132};
DE AltName: Full=APX-IIIC;
DE AltName: Full=Cytolysin IIIC;
DE Short=CLY-IIIC;
DE AltName: Full=RTX-III toxin determinant C;
DE AltName: Full=Toxin RTX-III-activating protein C;
GN Name=apxIIIC; Synonyms=clyIIIC, rtxC;
OS Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=715;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=405 / Serotype 8;
RX PubMed=8432615; DOI=10.1128/iai.61.3.947-954.1993;
RA Jansen R., Briaire J., Kamp E.M., Gielkens A.L.J., Smits M.A.;
RT "Cloning and characterization of the Actinobacillus pleuropneumoniae-RTX-
RT toxin III (ApxIII) gene.";
RL Infect. Immun. 61:947-954(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype 2;
RX PubMed=8494611; DOI=10.1089/dna.1993.12.351;
RA Chang Y.-F., Shi J., Ma D.-P., Shin S.J., Lein D.H.;
RT "Molecular analysis of the Actinobacillus pleuropneumoniae RTX toxin-III
RT gene cluster.";
RL DNA Cell Biol. 12:351-362(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=405 / Serotype 8;
RX PubMed=7927703; DOI=10.1128/iai.62.10.4411-4418.1994;
RA Jansen R., Briaire J., van Geel A.B.M., Kamp E.M., Gielkens A.L.J.,
RA Smits M.A.;
RT "Genetic map of the Actinobacillus pleuropneumoniae RTX-toxin (Apx)
RT operons: characterization of the ApxIII operons.";
RL Infect. Immun. 62:4411-4418(1994).
CC -!- FUNCTION: Protein-lysine acyltransferase that catalyzes fatty acylation
CC of the protoxin, 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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P55132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X68815; CAA48710.1; -; Genomic_DNA.
DR EMBL; L12145; AAA21923.1; -; Genomic_DNA.
DR EMBL; X80055; CAA56357.1; -; Genomic_DNA.
DR PIR; A49219; A49219.
DR RefSeq; WP_005605169.1; NZ_UIFY01000002.1.
DR AlphaFoldDB; Q04474; -.
DR SMR; Q04474; -.
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; Transferase.
FT CHAIN 1..173
FT /note="RTX-III toxin-activating lysine-acyltransferase
FT ApxIIC"
FT /id="PRO_0000217886"
FT ACT_SITE 29
FT /evidence="ECO:0000250|UniProtKB:P55132"
FT ACT_SITE 98
FT /evidence="ECO:0000250|UniProtKB:P55132"
SQ SEQUENCE 173 AA; 20422 MW; 3E9AFDDB031E2192 CRC64;
MSYKNVKNLT DDFTTLGHIA WLWANSPLHK EWSISLFTKN ILPAIQHDQY ILLMRDEFPV
AFCSWANLTL TNEVKYVRDV TSLTFEDWNS GERKWLIDWI APFGDNNTLY RYMRKKFPNE
VFRAIRVYPG STEAKIIHVQ GGQINKFTAK KLIQQYQEEL IQVLNNHKKI VRG
