PSRP_SHEPW
ID PSRP_SHEPW Reviewed; 270 AA.
AC B8CLG1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=swp_1850;
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877;
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ28612.1; -; Genomic_DNA.
DR RefSeq; WP_020911990.1; NC_011566.1.
DR AlphaFoldDB; B8CLG1; -.
DR SMR; B8CLG1; -.
DR STRING; 225849.swp_1850; -.
DR EnsemblBacteria; ACJ28612; ACJ28612; swp_1850.
DR KEGG; swp:swp_1850; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_1_0_6; -.
DR OMA; YAQCEFE; -.
DR OrthoDB; 980472at2; -.
DR Proteomes; UP000000753; 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_1000136496"
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; 30859 MW; 65E13E20BEFE6547 CRC64;
MLRKVFYISD GTAITAEVFG HAVLSQFPLE FDALTIPFVE TEKKAEAVKA QINDCFITTG
ERPLVFHSIV KAEIRDIIYS SEGLDYDFLN TFVAPLEKQL GMPATPALHR THGKTNDSYE
ARIEAINYAM ENDDGQTMKH MDKADLILLG VSRCGKTPSS LYLSMQFGIK AANYPFTEDD
MDNLKLPDAL KRNKDKLFGL TIDPVRLHEI RQSRMSNSRY SSMRQCRMEV KEVEMMYKRE
RIPFVNTTNH SVEEIATKIL EATSLERHMF