PSRP_ECOLI
ID PSRP_ECOLI Reviewed; 277 AA.
AC P0A8A4; P03822; P46137; P76203;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Phosphoenolpyruvate synthase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062};
DE Short=PEP synthase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062};
DE Short=PSRP {ECO:0000255|HAMAP-Rule:MF_01062};
DE EC=2.7.11.33 {ECO:0000255|HAMAP-Rule:MF_01062};
DE EC=2.7.4.28 {ECO:0000255|HAMAP-Rule:MF_01062};
DE AltName: Full=Pyruvate, water dikinase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062};
GN Name=ppsR {ECO:0000255|HAMAP-Rule:MF_01062}; Synonyms=ydiA;
GN OrderedLocusNames=b1703, JW1693;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
RC STRAIN=K12;
RA Holzschu D.L., McElver J.A., Liao C.C., Berry A.;
RT "The cloning and sequence of the E. coli pps gene.";
RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-277.
RX PubMed=1677907; DOI=10.1016/0378-1119(91)90544-l;
RA Hudson G.S., Rellos P., Davidson B.E.;
RT "Two promoters control the aroH gene of Escherichia coli.";
RL Gene 102:87-91(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-277.
RX PubMed=6167722; DOI=10.1016/0022-2836(81)90334-x;
RA Zurawski G., Gunsalus R.P., Brown K.D., Yanofsky C.;
RT "Structure and regulation of aroH, the structural gene for the tryptophan-
RT repressible 3-deoxy-D-arabino-heptulosonic acid-7-phosphate synthetase of
RT Escherichia coli.";
RL J. Mol. Biol. 145:47-73(1981).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=20044937; DOI=10.1186/1471-2091-11-1;
RA Burnell J.N.;
RT "Cloning and characterization of Escherichia coli DUF299: a bifunctional
RT ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria.";
RL BMC Biochem. 11:1-1(2010).
CC -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC involved in the regulation of the phosphoenolpyruvate synthase (PEPS)
CC by catalyzing its phosphorylation/dephosphorylation.
CC {ECO:0000255|HAMAP-Rule:MF_01062, ECO:0000269|PubMed:20044937}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-
CC phosphate + AMP + H(+); Xref=Rhea:RHEA:46020, Rhea:RHEA-COMP:11425,
CC Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378, ChEBI:CHEBI:43176,
CC ChEBI:CHEBI:68546, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.11.33; Evidence={ECO:0000255|HAMAP-Rule:MF_01062,
CC ECO:0000269|PubMed:20044937};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[pyruvate, water dikinase]-phosphate + H(+) + phosphate =
CC [pyruvate, water dikinase] + diphosphate; Xref=Rhea:RHEA:48580,
CC Rhea:RHEA-COMP:11425, Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:43176, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:68546; EC=2.7.4.28; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01062, ECO:0000269|PubMed:20044937};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20044937}.
CC -!- INTERACTION:
CC P0A8A4; P33643: rluD; NbExp=3; IntAct=EBI-548302, EBI-558026;
CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC regulatory protein family. PSRP subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01062}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M69116; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC74773.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15472.2; -; Genomic_DNA.
DR EMBL; M69116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M38266; AAA23496.1; -; Genomic_DNA.
DR EMBL; V00261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G64928; QQECAD.
DR RefSeq; NP_416218.1; NC_000913.3.
DR RefSeq; WP_000368046.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P0A8A4; -.
DR SMR; P0A8A4; -.
DR BioGRID; 4260288; 14.
DR BioGRID; 850567; 4.
DR DIP; DIP-47885N; -.
DR IntAct; P0A8A4; 14.
DR STRING; 511145.b1703; -.
DR jPOST; P0A8A4; -.
DR PaxDb; P0A8A4; -.
DR PRIDE; P0A8A4; -.
DR EnsemblBacteria; AAC74773; AAC74773; b1703.
DR EnsemblBacteria; BAA15472; BAA15472; BAA15472.
DR GeneID; 66674403; -.
DR GeneID; 946207; -.
DR KEGG; ecj:JW1693; -.
DR KEGG; eco:b1703; -.
DR PATRIC; fig|1411691.4.peg.554; -.
DR EchoBASE; EB1122; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_1_0_6; -.
DR InParanoid; P0A8A4; -.
DR OMA; YAQCEFE; -.
DR PhylomeDB; P0A8A4; -.
DR BioCyc; EcoCyc:EG11132-MON; -.
DR PRO; PR:P0A8A4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0043531; F:ADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:EcoCyc.
DR GO; GO:0016776; F:phosphotransferase activity, phosphate group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033673; P:negative regulation of kinase activity; IDA:EcoCyc.
DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:EcoCyc.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006468; P:protein phosphorylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01062; PSRP; 1.
DR InterPro; IPR005177; Kinase-pyrophosphorylase.
DR InterPro; IPR026530; PSRP.
DR PANTHER; PTHR31756; PTHR31756; 1.
DR Pfam; PF03618; Kinase-PPPase; 1.
PE 1: Evidence at protein level;
KW Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..277
FT /note="Phosphoenolpyruvate synthase regulatory protein"
FT /id="PRO_0000196659"
FT BINDING 157..164
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01062"
SQ SEQUENCE 277 AA; 31211 MW; 25508DEEC2E342CA CRC64;
MDNAVDRHVF YISDGTAITA EVLGHAVMSQ FPVTISSITL PFVENESRAR AVKDQIDAIY
HQTGVRPLVF YSIVLPEIRA IILQSEGFCQ DIVQALVAPL QQEMKLDPTP IAHRTHGLNP
NNLNKYDARI AAIDYTLAHD DGISLRNLDQ AQVILLGVSR CGKTPTSLYL AMQFGIRAAN
YPFIADDMDN LVLPASLKPL QHKLFGLTID PERLAAIREE RRENSRYASL RQCRMEVAEV
EALYRKNQIP WINSTNYSVE EIATKILDIM GLSRRMY
