PDRP2_STAES
ID PDRP2_STAES Reviewed; 272 AA.
AC Q8CR12;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Putative pyruvate, phosphate dikinase regulatory protein 2 {ECO:0000255|HAMAP-Rule:MF_00921};
DE Short=PPDK regulatory protein 2 {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=SE_2159;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05801.1; -; Genomic_DNA.
DR RefSeq; NP_765714.1; NC_004461.1.
DR RefSeq; WP_001830630.1; NZ_WBME01000005.1.
DR AlphaFoldDB; Q8CR12; -.
DR SMR; Q8CR12; -.
DR STRING; 176280.SE_2159; -.
DR EnsemblBacteria; AAO05801; AAO05801; SE_2159.
DR GeneID; 50017765; -.
DR KEGG; sep:SE_2159; -.
DR PATRIC; fig|176280.10.peg.2109; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_2_1_9; -.
DR OMA; FNNSYRF; -.
DR Proteomes; UP000001411; 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_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..272
FT /note="Putative pyruvate, phosphate dikinase regulatory
FT protein 2"
FT /id="PRO_0000196722"
FT BINDING 154..161
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ SEQUENCE 272 AA; 31037 MW; D93F2FD58C73C17D CRC64;
MKDNNEVLKL FIVSDSIGET AQRMIHATLT QFPDLTQVEI KKFPYIKDEQ EFLNVLQLAK
EQNAIVATTL VSESFNALGH QFANEHQIPY VDYMSELISI IKQHTHAKPL MESGALRKLN
DEYFKRIEAI EYSVKYDDGK HFTDIGEADA LIVGVSRTSK TPLSMYLANK GYKIANIPLV
PEVAIPDNVF QQKNLKVFGL TASPNYIANI RRNRAETLGL SSESNYNSLE RIKKELSYAE
EVFRKLNATV INTEYKSIEE SAFYIEKFLA KR
