ID   PDRP_AGRVS              Reviewed;         273 AA.
AC   B9JXT9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=Avi_0001;
OS   Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS   S4)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=311402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4 / ATCC BAA-846;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000633; ACM34969.1; -; Genomic_DNA.
DR   RefSeq; WP_012654499.1; NC_011989.1.
DR   AlphaFoldDB; B9JXT9; -.
DR   SMR; B9JXT9; -.
DR   STRING; 311402.Avi_0001; -.
DR   EnsemblBacteria; ACM34969; ACM34969; Avi_0001.
DR   KEGG; avi:Avi_0001; -.
DR   eggNOG; COG1806; Bacteria.
DR   HOGENOM; CLU_046206_2_0_5; -.
DR   OMA; YAQCEFE; -.
DR   OrthoDB; 980472at2; -.
DR   Proteomes; UP000001596; Chromosome 1.
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_00921; PDRP; 1.
DR   InterPro; IPR005177; Kinase-pyrophosphorylase.
DR   InterPro; IPR026565; PPDK_reg.
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..273
FT                   /note="Putative pyruvate, phosphate dikinase regulatory
FT                   protein"
FT                   /id="PRO_1000149696"
FT   BINDING         153..160
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ   SEQUENCE   273 AA;  30182 MW;  B29E39944CFA39CA CRC64;
     MENRKNFFHL HLISDSTGET LISAGRAAAV QFPHSNPIEH VYPLVRNRRQ ADAVLQSIDK
     EPGIVLYTIV DPELADFIDR RCIEIGVPSV NVLEPVIGTF QAYLGPLARR RVGAQHVMNA
     DYFARIEALN YTMDHDDGQM AEDYDQADVV LVGISRTSKT PTSIYLANRG IKTANIPIVP
     DSPLPESLFA AKGPLIVGLI ATSDRISQVR GHRELGTVSG FDPSDYTDRA SIAEELKYAR
     SLCARHNWPV IDVTRRSIEE TAAAIIALRA KPR