ID   LKTCB_MANHA             Reviewed;         167 AA.
AC   P55121;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Leukotoxin-activating lysine-acyltransferase LktC serotype A11;
DE            Short=Leukotoxin C;
DE            Short=Toxin-activating protein C;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P55132};
GN   Name=lktC;
OS   Mannheimia haemolytica (Pasteurella haemolytica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Mannheimia.
OX   NCBI_TaxID=75985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype A11;
RX   PubMed=8225575; DOI=10.1128/iai.61.12.5001-5007.1993;
RA   Burrows L.L., Olah-Winfield E., Lo R.Y.C.;
RT   "Molecular analysis of the leukotoxin determinants from Pasteurella
RT   haemolytica serotypes 1 to 16.";
RL   Infect. Immun. 61:5001-5007(1993).
CC   -!- FUNCTION: Involved in fatty acylation of the protoxin (LktA) at two
CC       internal lysine residues, thereby converting it to the active toxin.
CC       {ECO:0000250|UniProtKB:P16461}.
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   -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U01215; AAB36688.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P55121; -.
DR   SMR; P55121; -.
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..167
FT                   /note="Leukotoxin-activating lysine-acyltransferase LktC
FT                   serotype A11"
FT                   /id="PRO_0000217881"
FT   ACT_SITE        22
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
SQ   SEQUENCE   167 AA;  19753 MW;  0F4FA5D4E04CF795 CRC64;
     MNQSYFNLLG NITWLWMNSP LHKEWSCELL ARNVIPAIEN EQYMLLIDDG IPVAYCSWAD
     LNLENEVKYI KDISSLTLEE WQSGDRRWII DWVAPFGHSQ LLYKKMCQKY PDMIVRSIRF
     QPNQKSVGKI SYFKGGKLDK KTAKKRFDTY QEELATALKN EFNFIKK