ID   PSRP_SHESW              Reviewed;         270 AA.
AC   A1RIV6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative 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   OrderedLocusNames=Sputw3181_1764;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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   -!- 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};
CC   -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC       regulatory protein family. PSRP subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01062}.
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DR   EMBL; CP000503; ABM24601.1; -; Genomic_DNA.
DR   RefSeq; WP_011789098.1; NC_008750.1.
DR   AlphaFoldDB; A1RIV6; -.
DR   SMR; A1RIV6; -.
DR   GeneID; 45042701; -.
DR   KEGG; shw:Sputw3181_1764; -.
DR   HOGENOM; CLU_046206_1_0_6; -.
DR   OMA; YAQCEFE; -.
DR   Proteomes; UP000002597; Chromosome.
DR   GO; GO:0043531; F:ADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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: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   3: Inferred from homology;
KW   Kinase; Nucleotide-binding; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..270
FT                   /note="Putative phosphoenolpyruvate synthase regulatory
FT                   protein"
FT                   /id="PRO_0000316741"
FT   BINDING         150..157
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01062"
SQ   SEQUENCE   270 AA;  30732 MW;  40E4A4363458693A CRC64;
     MAPKVFYISD GTAITAEVFG HAVLSQFPLE FESLTIPFVE TLAKAEQVKR QINDCFITTG
     ERPLVFHSIV KAEIRDIIYS SEGVDYDFLN TFVAPLEQHL GVSASPVVHR THGKANHGYE
     ARIDAINFAM DNDDGQTMKH MDQADLILLG VSRCGKTPSS LYLSMQFGIK AANYPFTEDD
     MDNLKLPEAL KRNKKKLFGL TIDPVRLHEI RQSRMENSRY SSLKQCRLEV KEVEMMFKRE
     RIPYIDTTNH SVEEIATKIL DVTGLERHMF