ID   PDRP_GEOSM              Reviewed;         270 AA.
AC   C6DY36;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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=GM21_0226;
OS   Geobacter sp. (strain M21).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter; unclassified Geobacter.
OX   NCBI_TaxID=443144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M21;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Lovley D.;
RT   "Complete sequence of Geobacter sp. M21.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001661; ACT16311.1; -; Genomic_DNA.
DR   RefSeq; WP_012773938.1; NC_012918.1.
DR   AlphaFoldDB; C6DY36; -.
DR   SMR; C6DY36; -.
DR   STRING; 443144.GM21_0226; -.
DR   EnsemblBacteria; ACT16311; ACT16311; GM21_0226.
DR   KEGG; gem:GM21_0226; -.
DR   eggNOG; COG1806; Bacteria.
DR   HOGENOM; CLU_046206_2_1_7; -.
DR   OMA; YAQCEFE; -.
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; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..270
FT                   /note="Putative pyruvate, phosphate dikinase regulatory
FT                   protein"
FT                   /id="PRO_1000213452"
FT   BINDING         147..154
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ   SEQUENCE   270 AA;  31283 MW;  AE9D08204F249029 CRC64;
     MYHVYLLSDA TGETVERVAR AALTQFRDVD IRLRRMGQIR NREDILRALD EVDRAPGIIF
     YTLVNTELAQ FVRNEVEARQ LEAVDLITPL LYKLAEFLEM RPQKLPGLQY EMNSEYYRRM
     EAVDFTVKQD DGQEPRNLHK ADIVLIGVSR SSKTPLSMYL AHKGYKVANV PIIQGIDPPG
     ELEEVEPERV VGLIIDTQRL VDIRSARLRN LRQSPRGSYA DYRQVEEELS YCRRFYRAHP
     AWLVIDVTNK SVEESAAEIL SRLHGDIRHD