ID   PTAS_TREPA              Reviewed;         336 AA.
AC   O83132;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=TP_0094;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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: Belongs to the phosphate acetyltransferase and
CC       butyryltransferase family. {ECO:0000305}.
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DR   EMBL; AE000520; AAC65090.1; -; Genomic_DNA.
DR   PIR; B71366; B71366.
DR   RefSeq; WP_010881543.1; NC_021490.2.
DR   AlphaFoldDB; O83132; -.
DR   SMR; O83132; -.
DR   IntAct; O83132; 22.
DR   STRING; 243276.TPANIC_0094; -.
DR   EnsemblBacteria; AAC65090; AAC65090; TP_0094.
DR   GeneID; 57878634; -.
DR   KEGG; tpa:TP_0094; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_019723_0_1_12; -.
DR   OMA; TMLVKMG; -.
DR   OrthoDB; 1301815at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000811; 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; IPR012147; P_Ac_Bu_trans.
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   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   TIGRFAMs; TIGR00651; pta; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..336
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179150"
SQ   SEQUENCE   336 AA;  36538 MW;  C22586DE303135AE CRC64;
     MTFVESMQRR AVLAQKRLVL PEACEQRTLE AARLIVFRNI AAKVFLVGCE RDIKNTADRC
     GIDLTDMVVI DPSVSKHRDQ FAERYFQKRK HKGISLAQAA EDMRDPLRFA AMMLDQGHAD
     AMVAGAENTT ARVLRAGLTI IGTLPSVKTA SSCFVMDTNN PRLGGTRGLF IFSDCAVIPT
     PTAEQLADIA CSAAESCRTF IGEEPTVALL SYSTKGSGGD SDENILRVRE AVRILHERRV
     DFTFDGELQL DAALVPKITE KKAPHSPITG KVNTLVFPDL SSGNIGYKLV QRLSDADAYG
     PFLQGFAKPL SDLSRGCSVE DIVAACAVTL VQSNGR