ID   PSRP_CUPNH              Reviewed;         267 AA.
AC   Q0KA32;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=H16_A2039;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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; AM260479; CAJ93139.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0KA32; -.
DR   SMR; Q0KA32; -.
DR   STRING; 381666.H16_A2039; -.
DR   EnsemblBacteria; CAJ93139; CAJ93139; H16_A2039.
DR   KEGG; reh:H16_A2039; -.
DR   eggNOG; COG1806; Bacteria.
DR   HOGENOM; CLU_046206_1_0_4; -.
DR   OMA; YAQCEFE; -.
DR   Proteomes; UP000008210; Chromosome 1.
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..267
FT                   /note="Putative phosphoenolpyruvate synthase regulatory
FT                   protein"
FT                   /id="PRO_0000316720"
FT   BINDING         147..154
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01062"
SQ   SEQUENCE   267 AA;  30305 MW;  6C1CCC1464B7B077 CRC64;
     MFIVSDGTGI TAETFSHSIL AQFEMRFRKV RMPFVDTPEK AHIAVGKINE AFHNEGVPPI
     VFTTLVNQEA NKALRRAKAM ILDMFQTFIE PLEKELGLKS THAIGRFHQN ADTEAYKNRI
     EAINFSLAHD DGQSHKNLEE ADVILVGVSR SGKTPTSLYL AMQYGLKAAN YPLIPDDFER
     GRLPSALYAF KPKIFGLSID PQRLTEIRNE RRPGSKYAAL ENCRYEVNEA EAMMRREGIK
     WLSSTHKSIE EIATTILQEI KVDRDNY