ID   LKTC1_MANHA             Reviewed;         167 AA.
AC   P16533;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Leukotoxin-activating lysine-acyltransferase LktC serotype A1;
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 A1;
RX   PubMed=3040588; DOI=10.1128/iai.55.9.1987-1996.1987;
RA   Lo R.Y.C., Strathdee C.A., Shewen P.E.;
RT   "Nucleotide sequence of the leukotoxin genes of Pasteurella haemolytica
RT   A1.";
RL   Infect. Immun. 55:1987-1996(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype A1 / PH101;
RX   PubMed=2707120; DOI=10.1089/dna.1.1989.8.15;
RA   Highlander S.K., Chidambaram M., Engler M.J., Weinstock G.M.;
RT   "DNA sequence of the Pasteurella haemolytica leukotoxin gene cluster.";
RL   DNA 8:15-28(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
RC   STRAIN=Serotype A1 / PH101;
RX   PubMed=8359916; DOI=10.1128/iai.61.9.3942-3951.1993;
RA   Highlander S.K., Wickersham E.A., Garza O., Weinstock G.M.;
RT   "Expression of the Pasteurella haemolytica leukotoxin is inhibited by a
RT   locus that encodes an ATP-binding cassette homolog.";
RL   Infect. Immun. 61:3942-3951(1993).
RN   [4]
RP   ERRATUM OF PUBMED:8359916.
RA   Highlander S.K., Wickersham E.A., Garza O., Weinstock G.M.;
RL   Infect. Immun. 61:5431-5431(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RC   STRAIN=Serotype A1 / PH101;
RX   PubMed=2185213; DOI=10.1128/jb.172.5.2343-2350.1990;
RA   Highlander S.K., Engler M.J., Weinstock G.M.;
RT   "Secretion and expression of the Pasteurella haemolytica Leukotoxin.";
RL   J. Bacteriol. 172:2343-2350(1990).
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; M20730; AAA25528.1; -; Genomic_DNA.
DR   EMBL; M24197; AAA25542.1; -; Genomic_DNA.
DR   EMBL; M59210; AAA25537.1; -; Genomic_DNA.
DR   PIR; A30169; A30169.
DR   PIR; S29515; S29515.
DR   RefSeq; WP_006248022.1; NZ_VAJK01000035.1.
DR   AlphaFoldDB; P16533; -.
DR   SMR; P16533; -.
DR   STRING; 75985.WC39_13365; -.
DR   GeneID; 67370327; -.
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 A1"
FT                   /id="PRO_0000217879"
FT   ACT_SITE        22
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
FT   CONFLICT        157
FT                   /note="A -> R (in Ref. 2; AAA25542)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   167 AA;  19843 MW;  0D2ED2CBF2D7F1C5 CRC64;
     MNQSYFNLLG NITWLWMNSS LHKEWSCELL ARNVIPAIEN EQYMLLIDNG IPIAYCSWAD
     LNLETEVKYI KDINSLTPEE WQSGDRRWII DWVAPFGHSQ LLYKKMCQKY PDMIVRSIRF
     YPKQKELGKI AYFKGGKLDK KTAKKRFDTY QEELATALKN EFNFIKK