PTA_ECOLI
ID PTA_ECOLI Reviewed; 714 AA.
AC P0A9M8; P39184; P78091; P78189; P78190; Q9EUP2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Phosphate acetyltransferase;
DE EC=2.3.1.8 {ECO:0000269|PubMed:20236319};
DE AltName: Full=Phosphotransacetylase;
GN Name=pta; OrderedLocusNames=b2297, JW2294;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / KH131;
RX PubMed=7883769; DOI=10.1093/oxfordjournals.jbchem.a124616;
RA Kakuda H., Hosono K., Shiroishi K., Ichihara S.;
RT "Identification and characterization of the ackA (acetate kinase A)-pta
RT (phosphotransacetylase) operon and complementation analysis of acetate
RT utilization by an ackA-pta deletion mutant of Escherichia coli.";
RL J. Biochem. 116:916-922(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-9.
RC STRAIN=K12 / 1100;
RX PubMed=7918659; DOI=10.1016/0167-4781(94)90089-2;
RA Matsuyama A., Yamamoto-Otake H., Hewitt J., McGillivray R.T.A., Nakano E.;
RT "Nucleotide sequence of the phosphotransacetylase gene of Escherichia coli
RT strain K12.";
RL Biochim. Biophys. Acta 1219:559-562(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RC STRAIN=K12;
RX PubMed=2536666; DOI=10.1128/jb.171.1.577-580.1989;
RA Matsuyama A., Yamamoto H., Nakano E.;
RT "Cloning, expression, and nucleotide sequence of the Escherichia coli K-12
RT ackA gene.";
RL J. Bacteriol. 171:577-580(1989).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=10542166; DOI=10.1128/jb.181.21.6656-6663.1999;
RA Chang D.E., Shin S., Rhee J.S., Pan J.G.;
RT "Acetate metabolism in a pta mutant of Escherichia coli W3110: importance
RT of maintaining acetyl coenzyme A flux for growth and survival.";
RL J. Bacteriol. 181:6656-6663(1999).
RN [8]
RP FUNCTION.
RX PubMed=15687190; DOI=10.1128/jb.187.4.1266-1275.2005;
RA Shi I.Y., Stansbury J., Kuzminov A.;
RT "A defect in the acetyl coenzyme A<-->acetate pathway poisons
RT recombinational repair-deficient mutants of Escherichia coli.";
RL J. Bacteriol. 187:1266-1275(2005).
RN [9]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16080684; DOI=10.1021/bp050073s;
RA Dittrich C.R., Bennett G.N., San K.Y.;
RT "Characterization of the acetate-producing pathways in Escherichia coli.";
RL Biotechnol. Prog. 21:1062-1067(2005).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=19852855; DOI=10.1186/1475-2859-8-54;
RA Castano-Cerezo S., Pastor J.M., Renilla S., Bernal V., Iborra J.L.,
RA Canovas M.;
RT "An insight into the role of phosphotransacetylase (pta) and the
RT acetate/acetyl-CoA node in Escherichia coli.";
RL Microb. Cell Fact. 8:54-54(2009).
RN [11]
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, AND
RP CATALYTIC ACTIVITY.
RX PubMed=20236319; DOI=10.1111/j.1742-4658.2010.07617.x;
RA Campos-Bermudez V.A., Bologna F.P., Andreo C.S., Drincovich M.F.;
RT "Functional dissection of Escherichia coli phosphotransacetylase structural
RT domains and analysis of key compounds involved in activity regulation.";
RL FEBS J. 277:1957-1966(2010).
CC -!- FUNCTION: Involved in acetate metabolism (PubMed:16080684). Catalyzes
CC the reversible interconversion of acetyl-CoA and acetyl phosphate
CC (PubMed:16080684). The direction of the overall reaction changes
CC depending on growth conditions (PubMed:16080684). On minimal medium
CC acetyl-CoA is generated. In rich medium acetyl-CoA is converted to
CC acetate and allowing the cell to dump the excess of acetylation
CC potential in exchange for energy in the form of ATP (PubMed:15687190).
CC The main pathway for acetate production during exponential phase
CC (PubMed:16080684). {ECO:0000269|PubMed:15687190,
CC ECO:0000269|PubMed:16080684}.
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 Evidence={ECO:0000269|PubMed:20236319};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19522;
CC Evidence={ECO:0000269|PubMed:20236319};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19523;
CC Evidence={ECO:0000269|PubMed:20236319};
CC -!- ACTIVITY REGULATION: Inhibited by NADH and ATP. Pyruvate and PEP act as
CC activators of the acetyl phosphate forming reaction while inhibiting
CC the formation of acetyl-CoA. {ECO:0000269|PubMed:20236319}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67.2 uM for acetyl-CoA {ECO:0000269|PubMed:20236319};
CC KM=44.9 uM for acetyl phosphate {ECO:0000269|PubMed:20236319};
CC Vmax=177.4 uM/h/mg enzyme for acetyl-CoA-forming reaction
CC {ECO:0000269|PubMed:20236319};
CC Vmax=23.1 uM/h/mg enzyme for acetyl phosphate-forming reaction
CC {ECO:0000269|PubMed:20236319};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 2/2.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:20236319}.
CC -!- INTERACTION:
CC P0A9M8; P08365: chpS; NbExp=3; IntAct=EBI-555015, EBI-556499;
CC P0A9M8; P0A9I5: napD; NbExp=3; IntAct=EBI-555015, EBI-554985;
CC P0A9M8; P39332: yjgH; NbExp=2; IntAct=EBI-555015, EBI-561380;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expressed during exponential phase, decreases as cells enter
CC stationary phase at pH 7.0. Expression is inhibited at pH 6.0. Part of
CC the ackA-pta operon. {ECO:0000269|PubMed:16080684}.
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. {ECO:0000269|PubMed:20236319}.
CC -!- DISRUPTION PHENOTYPE: Severe impairment of growth in anaerobic
CC conditions, as well as in growth on minimal medium. Increased
CC sensitivity to environmental changes. Poor starvation survival and
CC slower growth on glucose, fructose, tryptone broth, or pyruvate, but
CC normal growth on glycerol or succinate. {ECO:0000269|PubMed:10542166,
CC ECO:0000269|PubMed:16080684, ECO:0000269|PubMed:19852855}.
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; D17576; BAA04502.1; -; Genomic_DNA.
DR EMBL; D21123; BAA04663.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75357.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16136.1; -; Genomic_DNA.
DR PIR; G65001; G65001.
DR PIR; JX0357; JX0357.
DR PIR; S50130; S50130.
DR RefSeq; NP_416800.1; NC_000913.3.
DR RefSeq; WP_000086722.1; NZ_STEB01000008.1.
DR PDB; 7T85; X-ray; 2.00 A; A=1-220.
DR PDBsum; 7T85; -.
DR AlphaFoldDB; P0A9M8; -.
DR SMR; P0A9M8; -.
DR BioGRID; 4261500; 351.
DR BioGRID; 851119; 1.
DR DIP; DIP-35815N; -.
DR IntAct; P0A9M8; 28.
DR STRING; 511145.b2297; -.
DR SWISS-2DPAGE; P0A9M8; -.
DR jPOST; P0A9M8; -.
DR PaxDb; P0A9M8; -.
DR PRIDE; P0A9M8; -.
DR EnsemblBacteria; AAC75357; AAC75357; b2297.
DR EnsemblBacteria; BAA16136; BAA16136; BAA16136.
DR GeneID; 66673820; -.
DR GeneID; 946778; -.
DR KEGG; ecj:JW2294; -.
DR KEGG; eco:b2297; -.
DR PATRIC; fig|1411691.4.peg.4437; -.
DR EchoBASE; EB4147; -.
DR eggNOG; COG0280; Bacteria.
DR eggNOG; COG0857; Bacteria.
DR InParanoid; P0A9M8; -.
DR OMA; FFMCLAD; -.
DR PhylomeDB; P0A9M8; -.
DR BioCyc; EcoCyc:PHOSACETYLTRANS-MON; -.
DR BioCyc; MetaCyc:PHOSACETYLTRANS-MON; -.
DR BRENDA; 2.3.1.8; 2026.
DR SABIO-RK; P0A9M8; -.
DR UniPathway; UPA00340; UER00459.
DR PRO; PR:P0A9M8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008959; F:phosphate acetyltransferase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0019413; P:acetate biosynthetic process; IMP:EcoCyc.
DR GO; GO:0045733; P:acetate catabolic process; IMP:EcoCyc.
DR GO; GO:0006083; P:acetate metabolic process; IMP:CACAO.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IMP:EcoCyc.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7883769,
FT ECO:0000269|PubMed:7918659"
FT CHAIN 2..714
FT /note="Phosphate acetyltransferase"
FT /id="PRO_0000179129"
FT REGION 391..714
FT /note="Phosphate acetyltransferase"
FT CONFLICT 20..50
FT /note="SLGVIRAMERKGVRLSVFKPIAQPRTGGDAP -> AWRDPCNGTQRRSSERF
FT QTYRSAAYRWRCA (in Ref. 2; BAA04663)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..209
FT /note="KL -> NV (in Ref. 1; BAA04502 and 2; BAA04663)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..271
FT /note="SIPHMLEHF -> QHSAHAGAL (in Ref. 2; BAA04663)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7T85"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:7T85"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:7T85"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:7T85"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:7T85"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:7T85"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:7T85"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:7T85"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:7T85"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:7T85"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:7T85"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:7T85"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:7T85"
SQ SEQUENCE 714 AA; 77172 MW; B45AF0C93494A04C CRC64;
MSRIIMLIPT GTSVGLTSVS LGVIRAMERK GVRLSVFKPI AQPRTGGDAP DQTTTIVRAN
SSTTTAAEPL KMSYVEGLLS SNQKDVLMEE IVANYHANTK DAEVVLVEGL VPTRKHQFAQ
SLNYEIAKTL NAEIVFVMSQ GTDTPEQLKE RIELTRNSFG GAKNTNITGV IVNKLNAPVD
EQGRTRPDLS EIFDDSSKAK VNNVDPAKLQ ESSPLPVLGA VPWSFDLIAT RAIDMARHLN
ATIINEGDIN TRRVKSVTFC ARSIPHMLEH FRAGSLLVTS ADRPDVLVAA CLAAMNGVEI
GALLLTGGYE MDARISKLCE RAFATGLPVF MVNTNTWQTS LSLQSFNLEV PVDDHERIEK
VQEYVANYIN ADWIESLTAT SERSRRLSPP AFRYQLTELA RKAGKRIVLP EGDEPRTVKA
AAICAERGIA TCVLLGNPAE INRVAASQGV ELGAGIEIVD PEVVRESYVG RLVELRKNKG
MTETVAREQL EDNVVLGTLM LEQDEVDGLV SGAVHTTANT IRPPLQLIKT APGSSLVSSV
FFMLLPEQVY VYGDCAINPD PTAEQLAEIA IQSADSAAAF GIEPRVAMLS YSTGTSGAGS
DVEKVREATR LAQEKRPDLM IDGPLQYDAA VMADVAKSKA PNSPVAGRAT VFIFPDLNTG
NTTYKAVQRS ADLISIGPML QGMRKPVNDL SRGALVDDIV YTIALTAIQS AQQQ
