ID   PSRP_PSYCK              Reviewed;         282 AA.
AC   Q1QBY7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 72.
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=Pcryo_1035;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-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   -!- SEQUENCE CAUTION:
CC       Sequence=ABE74816.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000323; ABE74816.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041753451.1; NC_007969.1.
DR   AlphaFoldDB; Q1QBY7; -.
DR   SMR; Q1QBY7; -.
DR   STRING; 335284.Pcryo_1035; -.
DR   KEGG; pcr:Pcryo_1035; -.
DR   eggNOG; COG1806; Bacteria.
DR   HOGENOM; CLU_046206_1_0_6; -.
DR   Proteomes; UP000002425; 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..282
FT                   /note="Putative phosphoenolpyruvate synthase regulatory
FT                   protein"
FT                   /id="PRO_0000316719"
FT   BINDING         162..169
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01062"
SQ   SEQUENCE   282 AA;  31554 MW;  A892003E066A50D1 CRC64;
     MKALEVDNAQ NIRTAFFISD GTAITAETLG RAILSQFASV PFETRVLPYV DNLERAEDAV
     VQINTAYQRD GLLPLVFDTI VSPEIREKIN SAHSCNLDMY EGLIGRVAEE TGVEPDGHSG
     HAHDNVDSET YKERIDAVHF ALDNDDGART RHYHAADIIL IGVSRSGKTP TSLYLALQFG
     IRAANYPLTE EDLNDNQLPK ALREHKHKLF GLIIDTDRLV KIRQERRAGS RYSSYQQCQQ
     EQRAIQGIYT SQGIPSLDVS EMSVEEIATR ILQMTGLKRR IG