ID   RTX2C_ACTSU             Reviewed;         160 AA.
AC   P0A3I4; P15376; P55119;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=RTX-II toxin-activating lysine-acyltransferase ApxIIC;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P55132};
DE   AltName: Full=APX-IIC;
DE   AltName: Full=Cytolysin IIC;
DE            Short=CLY-IIC;
DE   AltName: Full=HLY-IIC;
DE   AltName: Full=RTX-II toxin determinant C;
DE   AltName: Full=Toxin RTX-II-activating protein C;
GN   Name=apxIIC; Synonyms=appC, ashC, clyIIC, cytC, hlyC;
OS   Actinobacillus suis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=716;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3714;
RX   PubMed=1587585; DOI=10.1128/iai.60.6.2166-2173.1992;
RA   Burrows L.L., Lo R.Y.;
RT   "Molecular characterization of an RTX toxin determinant from Actinobacillus
RT   suis.";
RL   Infect. Immun. 60:2166-2173(1992).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M90440; AAA21917.1; -; Genomic_DNA.
DR   PIR; B43834; B43834.
DR   RefSeq; WP_012263032.1; NZ_MTBX01000089.1.
DR   AlphaFoldDB; P0A3I4; -.
DR   SMR; P0A3I4; -.
DR   GeneID; 66259877; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; 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; Hemolysis; Transferase.
FT   CHAIN           1..160
FT                   /note="RTX-II toxin-activating lysine-acyltransferase
FT                   ApxIIC"
FT                   /id="PRO_0000217885"
FT   ACT_SITE        23
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
SQ   SEQUENCE   160 AA;  18662 MW;  C155726F845C1C9F CRC64;
     MMLKNDFNVL GQIAWLWANS PMHRNWSVSL LMKNVIPAIE NDQYLLLVDD GFPIAYCSWA
     KLTLESEARY VKDTNSLKID DWNAGDRIWI IDWIAPFGDS SLLYKHMRQR FPYDIGRAIR
     IYPSKKDTGK IIYLKGGKIT KKVAEKTFLQ YEQELITALQ