PSRP_MARN8
ID PSRP_MARN8 Reviewed; 271 AA.
AC A1U1U7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Maqu_1884;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM18966.1; -; Genomic_DNA.
DR RefSeq; WP_011785359.1; NC_008740.1.
DR AlphaFoldDB; A1U1U7; -.
DR SMR; A1U1U7; -.
DR STRING; 351348.Maqu_1884; -.
DR EnsemblBacteria; ABM18966; ABM18966; Maqu_1884.
DR KEGG; maq:Maqu_1884; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_1_0_6; -.
DR OMA; YAQCEFE; -.
DR OrthoDB; 980472at2; -.
DR Proteomes; UP000000998; 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..271
FT /note="Putative phosphoenolpyruvate synthase regulatory
FT protein"
FT /id="PRO_0000316698"
FT BINDING 152..159
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01062"
SQ SEQUENCE 271 AA; 30765 MW; 3FA7024F2F8FEFA6 CRC64;
MKRTAFFISD GTGLTAEALG HALLAQFEKI EFERVTVPYI DDEEKARDLV SRINKASEID
GERPLVFDTI VNGGIREIIS RADGFMVDIF GTFLNPLEQE LNSSSSYSVG KSHSINNAGS
YERRIHAVNF ALDNDDGART RHYDEADLIL IGASRSGKTP TCLYLALQYG IKAANYPITE
EDLDDQKMPA ALRPHKEKLF GLTIEPERLA TIRNERRPNS RYSSLQQCMH EIEEIELMYK
RERIPYLNTT AYSVEEISTR IMVTTGLKRH R
