CYAC_BORPE
ID CYAC_BORPE Reviewed; 185 AA.
AC P0A3I5; Q45359;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Protein-lysine palmitoyltransferase CyaC {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:11031260, ECO:0000269|PubMed:32461253, ECO:0000269|PubMed:33011179};
DE AltName: Full=Cyclolysin-activating lysine-acyltransferase CyaC {ECO:0000305};
GN Name=cyaC {ECO:0000303|PubMed:1987161};
GN Synonyms=hlyC {ECO:0000303|PubMed:1987161}; OrderedLocusNames=BP0758;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1987161; DOI=10.1128/jb.173.2.720-726.1991;
RA Barry E.M., Weiss A.A., Ehrmann I.E., Gray M.C., Hewlett E.L.,
RA Mary Goodwin M.S.;
RT "Bordetella pertussis adenylate cyclase toxin and hemolytic activities
RT require a second gene, cyaC, for activation.";
RL J. Bacteriol. 173:720-726(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
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).
RN [3]
RP FUNCTION.
RX PubMed=7939682; DOI=10.1126/science.7939682;
RA Hackett M., Guo L., Shabanowitz J., Hunt D.F., Hewlett E.L.;
RT "Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella
RT pertussis.";
RL Science 266:433-435(1994).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8973351; DOI=10.1016/s0378-1119(96)00412-x;
RA Westrop G.D., Hormozi E.K., Da Costa N.A., Parton R., Coote J.G.;
RT "Bordetella pertussis adenylate cyclase toxin: proCyaA and CyaC proteins
RT synthesised separately in Escherichia coli produce active toxin in vitro.";
RL Gene 180:91-99(1996).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-30; HIS-33; CYS-67;
RP SER-68; ALA-140 AND ARG-141.
RX PubMed=11031260; DOI=10.1074/jbc.m006463200;
RA Basar T., Havlicek V., Bezouskova S., Hackett M., Sebo P.;
RT "Acylation of lysine 983 is sufficient for toxin activity of Bordetella
RT pertussis adenylate cyclase. Substitutions of alanine 140 modulate
RT acylation site selectivity of the toxin acyltransferase CyaC.";
RL J. Biol. Chem. 276:348-354(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF SER-30 AND HIS-33.
RX PubMed=33011179; DOI=10.1016/j.abb.2020.108615;
RA Yentongchai M., Thamwiriyasati N., Imtong C., Li H.C., Angsuthanasombat C.;
RT "Preferential modification of CyaA-hemolysin by CyaC-acyltransferase
RT through the catalytic Ser30-His33 dyad in esterolysis of palmitoyl-donor
RT substrate devoid of acyl carrier proteins.";
RL Arch. Biochem. Biophys. 694:108615-108615(2020).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32461253; DOI=10.1074/jbc.ra120.014122;
RA Osickova A., Khaliq H., Masin J., Jurnecka D., Sukova A., Fiser R.,
RA Holubova J., Stanek O., Sebo P., Osicka R.;
RT "Acyltransferase-mediated selection of the length of the fatty acyl chain
RT and of the acylation site governs activation of bacterial RTX toxins.";
RL J. Biol. Chem. 295:9268-9280(2020).
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 (PubMed:7939682,
CC PubMed:8973351, PubMed:33011179, PubMed:32461253). Has strong
CC preference for palmitoyl-CoA (hexadecanoyl-CoA) substrate, compared to
CC other acyl-CoA substrates such as myristoyl-CoA (tetradecanoyl-CoA)
CC (PubMed:33011179, PubMed:32461253). {ECO:0000269|PubMed:32461253,
CC ECO:0000269|PubMed:33011179, ECO:0000269|PubMed:7939682,
CC ECO:0000269|PubMed:8973351}.
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:0000269|PubMed:11031260, ECO:0000269|PubMed:32461253,
CC ECO:0000269|PubMed:33011179};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70616;
CC Evidence={ECO:0000269|PubMed:11031260, ECO:0000269|PubMed:32461253,
CC ECO:0000269|PubMed:33011179};
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:0000269|PubMed:32461253};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70652;
CC Evidence={ECO:0000269|PubMed:32461253};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P55132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8973351}.
CC -!- SIMILARITY: Belongs to the RTX toxin acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M57286; AAA22971.1; -; Genomic_DNA.
DR EMBL; BX640413; CAE41065.1; -; Genomic_DNA.
DR PIR; A39137; A39137.
DR RefSeq; NP_879577.1; NC_002929.2.
DR RefSeq; WP_010929994.1; NZ_CP039022.1.
DR AlphaFoldDB; P0A3I5; -.
DR SMR; P0A3I5; -.
DR STRING; 257313.BP0758; -.
DR GeneID; 56480996; -.
DR GeneID; 66436637; -.
DR KEGG; bpe:BP0758; -.
DR PATRIC; fig|257313.5.peg.812; -.
DR eggNOG; COG2994; Bacteria.
DR HOGENOM; CLU_116529_0_1_4; -.
DR OMA; WLWMHSP; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018031; F:peptidyl-lysine N6-palmitoyltransferase activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acyltransferase; Cytolysis; Cytoplasm; Reference proteome; Transferase;
KW Virulence.
FT CHAIN 1..185
FT /note="Protein-lysine palmitoyltransferase CyaC"
FT /id="PRO_0000217890"
FT ACT_SITE 33
FT /evidence="ECO:0000305|PubMed:11031260"
FT ACT_SITE 102
FT /evidence="ECO:0000250|UniProtKB:P55132"
FT MUTAGEN 30
FT /note="S->R,W: Abolished protein-lysine
FT palmitoyltransferase activity and ability to activate
FT CyaA."
FT /evidence="ECO:0000269|PubMed:11031260,
FT ECO:0000269|PubMed:33011179"
FT MUTAGEN 33
FT /note="H->S,D: Abolished protein-lysine
FT palmitoyltransferase activity and ability to activate
FT CyaA."
FT /evidence="ECO:0000269|PubMed:11031260,
FT ECO:0000269|PubMed:33011179"
FT MUTAGEN 67
FT /note="C->S: Does not affect ability to activate CyaA."
FT /evidence="ECO:0000269|PubMed:11031260"
FT MUTAGEN 68
FT /note="S->T: Does not affect ability to activate CyaA."
FT /evidence="ECO:0000269|PubMed:11031260"
FT MUTAGEN 140
FT /note="A->G: Reduced ability to activate CyaA; impaired
FT ability to palmitoylate CyaA at two sites."
FT /evidence="ECO:0000269|PubMed:11031260"
FT MUTAGEN 140
FT /note="A->G: Reduced ability to activate CyaA; impaired
FT ability to palmitoylate CyaA at two sites; almost only
FT acetylate CyaA at 'Lys-983'."
FT /evidence="ECO:0000269|PubMed:11031260"
FT MUTAGEN 141
FT /note="R->L,K: Does not affect ability to activate CyaA."
FT /evidence="ECO:0000269|PubMed:11031260"
FT CONFLICT 155
FT /note="A -> T (in Ref. 1; AAA22971)"
FT /evidence="ECO:0000305"
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
