ID   LTXC_AGGAC              Reviewed;         168 AA.
AC   P16461;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Leukotoxin-activating lysine-acyltransferase LtxC;
DE            Short=Leukotoxin C;
DE            Short=Toxin-activating protein C;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P55132};
GN   Name=ltxC {ECO:0000303|PubMed:8300209};
GN   Synonyms=AaLtc {ECO:0000303|PubMed:2670940},
GN   lktC {ECO:0000303|PubMed:2318535};
OS   Aggregatibacter actinomycetemcomitans (Actinobacillus
OS   actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JP2;
RX   PubMed=2670940; DOI=10.1016/s0021-9258(19)84850-0;
RA   Lally E.T., Golub E.E., Kieba I.R., Taichman N.S., Rosenbloom J.,
RA   Rosenbloom J.C., Gibson C.W., Demuth D.R.;
RT   "Analysis of the Actinobacillus actinomycetemcomitans leukotoxin gene.
RT   Delineation of unique features and comparison to homologous toxins.";
RL   J. Biol. Chem. 264:15451-15456(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JP2;
RX   PubMed=2318535; DOI=10.1128/iai.58.4.920-929.1990;
RA   Kraig E., Dailey T., Kolodrubetz D.;
RT   "Nucleotide sequence of the leukotoxin gene from Actinobacillus
RT   actinomycetemcomitans: homology to the alpha-hemolysin/leukotoxin gene
RT   family.";
RL   Infect. Immun. 58:920-929(1990).
RN   [3]
RP   INDUCTION, AND GENE NAME.
RC   STRAIN=652, and JP2;
RX   PubMed=8300209; DOI=10.1128/iai.62.2.501-508.1994;
RA   Brogan J.M., Lally E.T., Poulsen K., Kilian M., Demuth D.R.;
RT   "Regulation of Actinobacillus actinomycetemcomitans leukotoxin expression:
RT   analysis of the promoter regions of leukotoxic and minimally leukotoxic
RT   strains.";
RL   Infect. Immun. 62:501-508(1994).
RN   [4]
RP   FUNCTION IN MODIFICATION OF LTXA, AND DISRUPTION PHENOTYPE.
RC   STRAIN=JP2N;
RX   PubMed=19450669; DOI=10.1016/j.gene.2009.05.002;
RA   Balashova N.V., Shah C., Patel J.K., Megalla S., Kachlany S.C.;
RT   "Aggregatibacter actinomycetemcomitans LtxC is required for leukotoxin
RT   activity and initial interaction between toxin and host cells.";
RL   Gene 443:42-47(2009).
CC   -!- FUNCTION: Required for full activity and modification of the LtxA
CC       leukotoxin. Involved in fatty acid modification of the protoxin at two
CC       internal lysine residues, thereby converting it to the active toxin.
CC       {ECO:0000269|PubMed:19450669}.
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   -!- INDUCTION: Levels of toxin expression vary greatly among strains.
CC       Highly leukotoxic strains (JP2-type strains) produce more LtxA protein
CC       and ltx mRNA than minimally leukotoxic strains (652-type strains).
CC       Variations are probably due to different types of promoters.
CC       {ECO:0000269|PubMed:8300209}.
CC   -!- DISRUPTION PHENOTYPE: Mutants can express and secrete the LtxA
CC       leukotoxin, but LtxA lacks both leukotoxic and erythrolytic activities,
CC       and is unable to cause a change in intracellular calcium levels in host
CC       cells. {ECO:0000269|PubMed:19450669}.
CC   -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M27399; AAA21921.1; -; Genomic_DNA.
DR   EMBL; X16829; CAA34730.1; -; Genomic_DNA.
DR   PIR; B37205; B37205.
DR   RefSeq; WP_005545611.1; NZ_VSEW01000001.1.
DR   AlphaFoldDB; P16461; -.
DR   SMR; P16461; -.
DR   STRING; 714.ACT75_09600; -.
DR   eggNOG; COG2994; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; 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   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..168
FT                   /note="Leukotoxin-activating lysine-acyltransferase LtxC"
FT                   /id="PRO_0000217878"
FT   ACT_SITE        23
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
FT   CONFLICT        9
FT                   /note="M -> V (in Ref. 2; CAA34730)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   168 AA;  19793 MW;  9602C0369FCAF332 CRC64;
     MEKNNNFEML GYVAWLWANS PLHRNWSLSL LAINVLPAIQ YGQYTLLMRD GVPIAFCSWA
     NLSLENEIKY LEDVSSLVYD DWNSGDRKWF IDWIAPFGHN YVLYKHMRKS FPYDLFRSIR
     VYKGSSEGKI TEFHGGKVDK QLANKIFQQY HFELINELKN KSEVISIN