PSRP_PSEPK
ID PSRP_PSEPK Reviewed; 272 AA.
AC Q88L54;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=PP_2081;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN67695.1; -; Genomic_DNA.
DR RefSeq; NP_744231.1; NC_002947.4.
DR RefSeq; WP_010953083.1; NC_002947.4.
DR AlphaFoldDB; Q88L54; -.
DR SMR; Q88L54; -.
DR STRING; 160488.PP_2081; -.
DR EnsemblBacteria; AAN67695; AAN67695; PP_2081.
DR KEGG; ppu:PP_2081; -.
DR PATRIC; fig|160488.4.peg.2193; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_1_0_6; -.
DR OMA; YAQCEFE; -.
DR PhylomeDB; Q88L54; -.
DR BioCyc; PPUT160488:G1G01-2219-MON; -.
DR Proteomes; UP000000556; 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..272
FT /note="Putative phosphoenolpyruvate synthase regulatory
FT protein"
FT /id="PRO_0000196691"
FT BINDING 152..159
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01062"
SQ SEQUENCE 272 AA; 30824 MW; 2CD0B92F37D2E4D9 CRC64;
MKRTAFFISD GTGITAETLG QSLLAQFESI PFNKFTRPYI DSPDKARVMV QQINAAAERD
GVRPIIFDTI VNQDIREILA TSNGFMIDIF SSFLSPLEQE LIAHSSYSVG KSHSIGGNSN
YMERIEAVNF ALDNDDGART HYYDKADLIL VGVSRCGKTP TCLYMAMQFG IRAANYPLTE
DDMERLQLPA VLKKHHSKLF GLTIDPDRLT AIRHERKPNS RYSSFAQCEF EVREVESLFR
RENIPNINST HFSVEEISAK ILVEKGVERR FK
