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Database: UniProt
Entry: A0A1H7R8T0_9BURK
LinkDB: A0A1H7R8T0_9BURK
Original site: A0A1H7R8T0_9BURK 
ID   A0A1H7R8T0_9BURK        Unreviewed;       273 AA.
AC   A0A1H7R8T0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Putative phosphoenolpyruvate synthase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
DE            Short=PEP synthase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
DE            Short=PSRP {ECO:0000256|HAMAP-Rule:MF_01062};
DE            EC=2.7.11.33 {ECO:0000256|HAMAP-Rule:MF_01062};
DE            EC=2.7.4.28 {ECO:0000256|HAMAP-Rule:MF_01062};
DE   AltName: Full=Pyruvate, water dikinase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
GN   ORFNames=SAMN05216359_11170 {ECO:0000313|EMBL:SEL56559.1};
OS   Roseateles sp. YR242.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=1855305 {ECO:0000313|EMBL:SEL56559.1, ECO:0000313|Proteomes:UP000198631};
RN   [1] {ECO:0000313|EMBL:SEL56559.1, ECO:0000313|Proteomes:UP000198631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR242 {ECO:0000313|EMBL:SEL56559.1,
RC   ECO:0000313|Proteomes:UP000198631};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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:0000256|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:0000256|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:0000256|HAMAP-
CC         Rule:MF_01062};
CC   -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC       regulatory protein family. PSRP subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01062}.
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DR   EMBL; FOAV01000011; SEL56559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7R8T0; -.
DR   STRING; 1855305.SAMN05216359_11170; -.
DR   OrthoDB; 9782201at2; -.
DR   Proteomes; UP000198631; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   HAMAP; MF_01062; PSRP; 1.
DR   InterPro; IPR005177; Kinase-pyrophosphorylase.
DR   InterPro; IPR026530; PSRP.
DR   PANTHER; PTHR31756; PYRUVATE, PHOSPHATE DIKINASE REGULATORY PROTEIN 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31756:SF3; PYRUVATE, PHOSPHATE DIKINASE REGULATORY PROTEIN 1, CHLOROPLASTIC; 1.
DR   Pfam; PF03618; Kinase-PPPase; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01062};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01062};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|HAMAP-Rule:MF_01062};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01062}.
FT   BINDING         153..160
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01062"
SQ   SEQUENCE   273 AA;  30803 MW;  9D07655790023D27 CRC64;
     MTQHTVYFVS DGTGITAETF GNSILAQFSV KARHVRRPFV DNADKAHQLV KEINETGIRE
     GQRPVVFATL VNREVLNVVR QHCEGLVLDM FGTFIAPLED EFRVKSNHRV GRFSDIAKSQ
     EYHDRIEAIN FSLAHDDGQS ARNLDSADVI LVGVSRCGKT PTSLYLAMQH GIKAANCPLI
     PEDFERGALP TPLLPHKKKC FGLTIDPERL AQVRNERRPG SKYADLMNCH YEVREAETMM
     KKAGISWLSS THKSIEEIAT TILRDIRPDR LMY
//
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