ID   PTAS_STAEQ              Reviewed;         329 AA.
AC   Q5HRF7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=SERP0236;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000029; AAW53623.1; -; Genomic_DNA.
DR   RefSeq; WP_002445772.1; NC_002976.3.
DR   AlphaFoldDB; Q5HRF7; -.
DR   SMR; Q5HRF7; -.
DR   STRING; 176279.SERP0236; -.
DR   EnsemblBacteria; AAW53623; AAW53623; SERP0236.
DR   KEGG; ser:SERP0236; -.
DR   eggNOG; COG0280; Bacteria.
DR   HOGENOM; CLU_019723_0_1_9; -.
DR   OMA; TMLVKMG; -.
DR   OrthoDB; 1301815at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000531; 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..329
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000179147"
SQ   SEQUENCE   329 AA;  35101 MW;  395A4A4AECB12A49 CRC64;
     MADLLSVLQD KLSGKNVKIV LPEGEDERVL IAATQLQKTD YVSPIVLGNE DNIKSLASKH
     ALDLTQIEII DPATSELKDE LVDAFVERRK GKATKEQAVE LLDNVNYFGT MLVYTGKAEG
     LVSGAAHSTG DTVRPALQII KTKPGVSRTS GIFFMIKGDE QYIFGDCAIN PELDAQGLAE
     IAVESAKSAQ SFGMNPKVAM LSFSTKGSAK SDDVTKVQEA LKLAQEKAEA DQLEHVVIDG
     EFQFDAAIVP SVAEKKAPGA KIQGDANVFV FPSLEAGNIG YKIAQRLGGY DAVGPVLQGL
     NSPVNDLSRG CSTEDVYNLS IITAAQALQ