ID   PDRP_BRUAB              Reviewed;         279 AA.
AC   Q57AJ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Putative pyruvate, phosphate dikinase regulatory protein {ECO:0000255|HAMAP-Rule:MF_00921};
DE            Short=PPDK regulatory protein {ECO:0000255|HAMAP-Rule:MF_00921};
DE            EC=2.7.11.32 {ECO:0000255|HAMAP-Rule:MF_00921};
DE            EC=2.7.4.27 {ECO:0000255|HAMAP-Rule:MF_00921};
GN   OrderedLocusNames=BruAb1_2042;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
CC   -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC       involved in the regulation of the pyruvate, phosphate dikinase (PPDK)
CC       by catalyzing its phosphorylation/dephosphorylation.
CC       {ECO:0000255|HAMAP-Rule:MF_00921}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate,
CC         phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-histidyl/O-
CC         phospho-L-threonyl-[pyruvate, phosphate dikinase];
CC         Xref=Rhea:RHEA:43692, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:61977,
CC         ChEBI:CHEBI:83586, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         EC=2.7.11.32; Evidence={ECO:0000255|HAMAP-Rule:MF_00921};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(tele)-phospho-L-histidyl/O-phospho-L-threonyl-
CC         [pyruvate, phosphate dikinase] + phosphate = diphosphate + N(tele)-
CC         phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase];
CC         Xref=Rhea:RHEA:43696, Rhea:RHEA-COMP:10650, Rhea:RHEA-COMP:10651,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:61977, ChEBI:CHEBI:83586; EC=2.7.4.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00921};
CC   -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC       regulatory protein family. PDRP subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00921}.
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DR   EMBL; AE017223; AAX75343.1; -; Genomic_DNA.
DR   RefSeq; WP_002965131.1; NC_006932.1.
DR   AlphaFoldDB; Q57AJ1; -.
DR   SMR; Q57AJ1; -.
DR   EnsemblBacteria; AAX75343; AAX75343; BruAb1_2042.
DR   GeneID; 55591637; -.
DR   KEGG; bmb:BruAb1_2042; -.
DR   HOGENOM; CLU_046206_2_0_5; -.
DR   Proteomes; UP000000540; Chromosome I.
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_00921; PDRP; 1.
DR   InterPro; IPR005177; Kinase-pyrophosphorylase.
DR   InterPro; IPR026565; PPDK_reg.
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; Nucleotide-binding; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..279
FT                   /note="Putative pyruvate, phosphate dikinase regulatory
FT                   protein"
FT                   /id="PRO_0000316641"
FT   BINDING         153..160
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ   SEQUENCE   279 AA;  30481 MW;  452110EFCD636FA5 CRC64;
     MTRPLSYFHL HLISDATGET LLAAGRAAAA QYANARAIEH IYPLIRTEKQ LRKVLEGIDA
     EPGIVLYTVV DQKLAAIIDE SCADMGVPSV SVLEPVLNTF QSYLGAPAHR RASAQHVLNA
     DYFRRIDALN FMMEHDDGQL PLDIEEADVI IVGISRTSKT PTSIYLANRG IKAANVPLVL
     GIPVPEILFA AKRPLIVGLV ATAERISQIR QNRPLGNIPS LDTGLYTDRV SISEELAYAR
     NLCNRHGWPI IDVSRRSIEE TAAAILALLR NGKKEGSSS
//