ID   CYAC_BORPA              Reviewed;         185 AA.
AC   P0A3I7; Q45359;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Protein-lysine palmitoyltransferase CyaC {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:P0A3I5};
DE   AltName: Full=Cyclolysin-activating lysine-acyltransferase CyaC {ECO:0000305};
GN   Name=cyaC {ECO:0000250|UniProtKB:P0A3I5}; Synonyms=hlyC;
GN   OrderedLocusNames=BPP0320;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Protein-lysine palmitoyltransferase that catalyzes
CC       palmitoylation of the protoxin (CyaA) at two internal lysine residues,
CC       thereby converting it to the active toxin.
CC       {ECO:0000250|UniProtKB:P0A3I5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-[ACP] + L-lysyl-[protein] = H(+) + holo-[ACP] +
CC         N(6)-hexadecanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:70615, Rhea:RHEA-
CC         COMP:9652, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:14175, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78483, ChEBI:CHEBI:138936;
CC         Evidence={ECO:0000250|UniProtKB:P0A3I5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70616;
CC         Evidence={ECO:0000250|UniProtKB:P0A3I5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-[ACP] + L-lysyl-[protein] = H(+) + holo-
CC         [ACP] + N(6)-[(9Z)-hexadecenoyl]-L-lysyl-[protein];
CC         Xref=Rhea:RHEA:70651, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10800, Rhea:RHEA-COMP:17945, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:64479, ChEBI:CHEBI:83989,
CC         ChEBI:CHEBI:189851; Evidence={ECO:0000250|UniProtKB:P0A3I5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70652;
CC         Evidence={ECO:0000250|UniProtKB:P0A3I5};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P55132}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A3I5}.
CC   -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE40061.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX640423; CAE40061.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_010929994.1; NC_002928.3.
DR   AlphaFoldDB; P0A3I7; -.
DR   SMR; P0A3I7; -.
DR   EnsemblBacteria; CAE40061; CAE40061; BPP0320.
DR   GeneID; 56480996; -.
DR   GeneID; 66436637; -.
DR   KEGG; bpa:BPP0320; -.
DR   HOGENOM; CLU_116529_0_1_4; -.
DR   Proteomes; UP000001421; Chromosome.
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; Virulence.
FT   CHAIN           1..185
FT                   /note="Protein-lysine palmitoyltransferase CyaC"
FT                   /id="PRO_0000217889"
FT   ACT_SITE        33
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000250|UniProtKB:P55132"
SQ   SEQUENCE   185 AA;  20480 MW;  7923EBC14A71C2D5 CRC64;
     MLPSAQAPSL LNPTDDFAAL GNIAWLWMNS PMHRDWPVHL LARNTLAPIQ LGQYILLRCN
     DVPVAYCSWA LMDADTELSY VMAPSSLGGN AWNCGDRLWI IDWIAPFSRD DNRALRRALA
     ERHPDSVGRS LRVRRGGDTA RVKEYRGRAL DAAAARAQLD RYHAELIAGL RASNGGYAPR
     GRGTA