ID   PSRP_VEREI              Reviewed;         273 AA.
AC   A1WJJ2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Veis_2049;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000542; ABM57799.1; -; Genomic_DNA.
DR   RefSeq; WP_011809805.1; NC_008786.1.
DR   AlphaFoldDB; A1WJJ2; -.
DR   SMR; A1WJJ2; -.
DR   STRING; 391735.Veis_2049; -.
DR   EnsemblBacteria; ABM57799; ABM57799; Veis_2049.
DR   KEGG; vei:Veis_2049; -.
DR   eggNOG; COG1806; Bacteria.
DR   HOGENOM; CLU_046206_1_0_4; -.
DR   OMA; YAQCEFE; -.
DR   OrthoDB; 980472at2; -.
DR   Proteomes; UP000000374; 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; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..273
FT                   /note="Putative phosphoenolpyruvate synthase regulatory
FT                   protein"
FT                   /id="PRO_0000316754"
FT   BINDING         153..160
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01062"
SQ   SEQUENCE   273 AA;  30694 MW;  82A6BD8EB743E13D CRC64;
     MHSRTVFFVS DGTGITAETF GNAILAQFEM KPRHVRLPFV DTVDKAHQAV RQINHCGEVE
     GKKPIVFTTL VNMEVLKTLQ DGCQGMLLDM FGTFVHPLEQ ELGIKSHHRV GRFSDASHSK
     EYSDRIAAIN FSLAHDDGQS HHDLAGADVI LVGVSRSGKT PTSLYLAMQC GLKTANYPLI
     PEDFERRQLP PALEPHRKKI FGLTIQAERL AEIRNERRPN SRYASLDNCR AEIAGAEAMM
     RRSSIRWLST TTKSIEEIAT TILQELRPER LVY