PTAS_STAES
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 25-MAY-2022, entry version 97.
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; Firmicutes; 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 STRING; 176280.SE_0359; -.
DR EnsemblBacteria; AAO03956; AAO03956; SE_0359.
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 OMA; TMLVKMG; -.
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; 3.40.50.10750; -; 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; 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