ID   PTAS_STAES              Reviewed;         329 AA.
AC   Q8CQ62;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=SE_0359;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO03956.1; -; Genomic_DNA.
DR   RefSeq; NP_763914.1; NC_004461.1.
DR   RefSeq; WP_001832032.1; NZ_WBME01000026.1.
DR   AlphaFoldDB; Q8CQ62; -.
DR   SMR; Q8CQ62; -.
DR   GeneID; 50019479; -.
DR   KEGG; sep:SE_0359; -.
DR   PATRIC; fig|176280.10.peg.334; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_019723_0_1_9; -.
DR   OrthoDB; 9805787at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000001411; 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; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 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   NCBIfam; TIGR00651; pta; 1.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF000428; P_Ac_trans; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Transferase.
FT   CHAIN           1..329
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179146"
SQ   SEQUENCE   329 AA;  35088 MW;  2B49E15055B99C0A CRC64;
     MADLLSVLQD KLSGKNVKIV LPEGEDERVL IAATQLQKTD YVSPIVLGNE DNIKSLASKH
     ALDLTQIEII DPATSELKDE LVDAFVERRK GKATKEQAVE LLDNVNYFGT MLVYTGKAEG
     LVSGAAHSTG DTVRPALQII KTKPGVSRTS GIFFMIKGDE QYIFGDCAIN PELDAQGLAE
     IAVESAKSAQ SFGMDPKVAM LSFSTKGSAK SDDVTKVQEA LKLAQEKAEA DQLDHVVIDG
     EFQFDAAIVP SVAEKKAPGA KIQGDANVFV FPSLEAGNIG YKIAQRLGGY DAVGPVLQGL
     NSPVNDLSRG CSTEDVYNLS IITAAQALQ
//