ID   PTAS_HELPJ              Reviewed;         519 AA.
AC   Q9ZKU4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=jhp_0841;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + phosphate = acetyl phosphate + CoA;
CC         Xref=Rhea:RHEA:19521, ChEBI:CHEBI:22191, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.8;
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the CobB/CobQ family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the phosphate
CC       acetyltransferase and butyryltransferase family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD06419.1; -; Genomic_DNA.
DR   PIR; D71881; D71881.
DR   RefSeq; WP_001191463.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKU4; -.
DR   SMR; Q9ZKU4; -.
DR   STRING; 85963.jhp_0841; -.
DR   EnsemblBacteria; AAD06419; AAD06419; jhp_0841.
DR   KEGG; hpj:jhp_0841; -.
DR   PATRIC; fig|85963.30.peg.126; -.
DR   eggNOG; COG0280; Bacteria.
DR   OMA; TMLVKMG; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000804; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008959; F:phosphate acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.10750; -; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   InterPro; IPR004614; P_AcTrfase.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   TIGRFAMs; TIGR00651; pta; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..519
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179131"
FT   REGION          196..519
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   519 AA;  56738 MW;  3E5A71FC8BBBAD37 CRC64;
     MQSLWIYPED TEVLGAACKS LLKALKPRYQ KIALFSPISG GCEGFGECES LSSLEVHSAI
     DKQKALELVS TAQEELLFET ILKRYDELQS THDFVINLGY APKFFLNALL DLNTILAKHL
     NAPVVAVAQT SLDHLKAMHS HILKKEAPFA IGLFVGETLE KPHFLSASLC KQQCELEASA
     IENLLQTKSE IITPLAFQRS LEKKAKKQIK KVVLPESEDE RILKAAHRLN LMGAVGLILL
     GDKEAINSQA KNLNLNLENV EIINPNTSHY REEFAKSLYE LRKSKGLSEQ EAERLALDKT
     YFATMLVHLG YAHAMVSGVN HTTAETIRPA LQIIKTKPGV SLVSSVFLMC LDTQVFVFGD
     CAIIPNPSPK ELAEIATTSA QTAKQFNIAP KVALLSYATG NSAQGEMIDK INEALTIVQK
     LDPQLEIDGP LQFDASIDKG VAKKKMPNSQ VAGQASVFIF PDLNAGNIAY KAVQRSAKAV
     AIGPILQGLN KPINDLSRGA LVEDIVNTVL ISAIQAQDY