ID   PTA_YERPE               Reviewed;         717 AA.
AC   Q7CJ96; Q74T19;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 99.
DE   RecName: Full=Phosphate acetyltransferase;
DE            EC=2.3.1.8;
DE   AltName: Full=Phosphotransacetylase;
GN   Name=pta; OrderedLocusNames=YPO2567, y1620, YP_2378;
OS   Yersinia pestis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
CC   -!- FUNCTION: Involved in acetate metabolism. {ECO:0000250}.
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   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The N-terminal region seems to be important for proper
CC       quaternary structure. The C-terminal region contains the substrate-
CC       binding site (By similarity). {ECO:0000250}.
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; AE009952; AAM85189.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS62583.1; -; Genomic_DNA.
DR   EMBL; AL590842; CAL21192.1; -; Genomic_DNA.
DR   PIR; AE0313; AE0313.
DR   RefSeq; YP_002347528.1; NC_003143.1.
DR   AlphaFoldDB; Q7CJ96; -.
DR   SMR; Q7CJ96; -.
DR   IntAct; Q7CJ96; 2.
DR   STRING; 214092.YPO2567; -.
DR   PaxDb; 214092-YPO2567; -.
DR   DNASU; 1146567; -.
DR   EnsemblBacteria; AAS62583; AAS62583; YP_2378.
DR   KEGG; ype:YPO2567; -.
DR   KEGG; ypk:y1620; -.
DR   KEGG; ypm:YP_2378; -.
DR   PATRIC; fig|214092.21.peg.2990; -.
DR   eggNOG; COG0280; Bacteria.
DR   eggNOG; COG0857; Bacteria.
DR   HOGENOM; CLU_019723_2_2_6; -.
DR   OMA; FFMCLAD; -.
DR   OrthoDB; 9808984at2; -.
DR   UniPathway; UPA00340; UER00459.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; 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   CDD; cd03109; DTBS; 1.
DR   Gene3D; 3.40.50.10950; -; 1.
DR   Gene3D; 3.40.1390.20; HprK N-terminal domain-like; 1.
DR   Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR010766; DRTGG.
DR   InterPro; IPR016475; P-Actrans_bac.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004614; P_AcTrfase.
DR   InterPro; IPR042113; P_AcTrfase_dom1.
DR   InterPro; IPR042112; P_AcTrfase_dom2.
DR   InterPro; IPR002505; PTA_PTB.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   NCBIfam; TIGR00651; pta; 1.
DR   PANTHER; PTHR43356; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43356:SF3; PHOSPHATE ACETYLTRANSFERASE; 1.
DR   Pfam; PF13500; AAA_26; 1.
DR   Pfam; PF07085; DRTGG; 1.
DR   Pfam; PF01515; PTA_PTB; 1.
DR   PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR   SUPFAM; SSF75138; HprK N-terminal domain-like; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..717
FT                   /note="Phosphate acetyltransferase"
FT                   /id="PRO_0000405555"
FT   REGION          390..717
FT                   /note="Phosphate acetyltransferase"
SQ   SEQUENCE   717 AA;  77402 MW;  4AB841751C30C2A3 CRC64;
     MSRTIMLIPT GTSVGLTSVS LGVIRSMEQK GVSLSVFKPI AQPRAGNDAP DQTTTIIRAN
     SSITAAEPLN MNYVETLLSS NQQDVLMEEI VARYHENTKD AEVVLVEGLV PTRKHQFANA
     LNYEIAKTLN AEIVFVIALG NDSPDQLKER IELARSSFGG SKNKNITGVI INKLNAPVDE
     QGRTRPDLSE IFDDSTKASV ANIDPSQLFA NSPIPVLGCV PWSFELIATR AIDMAKHLNA
     RIINEGDIKT RRVKSVTFCA RSIPHMLEHF RPGSLLVTSA DRPDVLVSAC LAAMNGVEIG
     AILLTGGYAI DDRINNLCER AFQTGLPVFM VDTNTWQTSL SLQSFNLEVP ADDHERVEKL
     QNYVASHISS EWIDSLTAAS ERPRRLSPPA FRYELTELAR KAGKRIVLPE GDEPRTIKAA
     SICAERGIAT CVLLGNPEEI QRVATSQGVE LGKGVEIIDP VAVREQYVPR LVELRKSKGM
     TEVVAREQLE DNVVLGTLML EKGEVDGLVS GAVHTTANTI RPPLQLIKTA PGSSLVSSVF
     FMLLPDQVLV YGDCAINPDP TAEQLSEIAI QSADSAAAFG IEPRVAMISY STGNSGAGSD
     VEKVREATRL AQEKRPDLII DGPLQYDAAI MADVAKSKAP NSPVAGRATV FIFPDLNTGN
     TTYKAVQRSA DLISIGPMLQ GMRKPVNDLS RGALVDDIVY TVALTAIQSA QADSAAS
//