PTA_YERPE
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 25-MAY-2022, entry version 93.
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; Proteobacteria; 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; Q7CJ96; -.
DR DNASU; 1146567; -.
DR EnsemblBacteria; AAM85189; AAM85189; y1620.
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 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 Gene3D; 3.40.1390.20; -; 1.
DR Gene3D; 3.40.50.10750; -; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF07085; DRTGG; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF006107; PhpActrans_proteobac; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75138; SSF75138; 1.
DR TIGRFAMs; TIGR00651; pta; 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