PDRP2_LISW6
ID PDRP2_LISW6 Reviewed; 270 AA.
AC A0AJX1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=lwe1885;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(2006).
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; AM263198; CAK21303.1; -; Genomic_DNA.
DR RefSeq; WP_011702652.1; NC_008555.1.
DR AlphaFoldDB; A0AJX1; -.
DR SMR; A0AJX1; -.
DR STRING; 386043.lwe1885; -.
DR EnsemblBacteria; CAK21303; CAK21303; lwe1885.
DR GeneID; 61189786; -.
DR KEGG; lwe:lwe1885; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_2_1_9; -.
DR OMA; YAQCEFE; -.
DR OrthoDB; 980472at2; -.
DR Proteomes; UP000000779; 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..270
FT /note="Putative pyruvate, phosphate dikinase regulatory
FT protein 2"
FT /id="PRO_0000316695"
FT BINDING 151..158
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ SEQUENCE 270 AA; 30082 MW; EBCB91F5AE632454 CRC64;
MEKSVIIYVI SDAIGETAQH IIRAVTAQFS LNKPADIRRH AFIRDEKALL ETLEEAKAAD
GIVVQTLVQS PLAEYATDFC AQNNIPNIDL LHTLTAAVEA KTGLKSKQDP GNMRRLDSNY
FDRIAAIEFA VKYDDCKDPR GLIDADIVLV GVSRTSKTPL SSFLANQNWK VANVPLVPEI
PIPDELFQIP NERIIGLTTT PEKLAQIRKV RLKSIGLDES SSYSSEKRIL EELEYGYDTF
KKLGCQVIHV EDKAIEETAA LITEIITSYH
