ID A0A0H3C520_CAUVN Unreviewed; 301 AA.
AC A0A0H3C520;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Putative pyruvate, phosphate dikinase regulatory protein {ECO:0000256|HAMAP-Rule:MF_00921};
DE Short=PPDK regulatory protein {ECO:0000256|HAMAP-Rule:MF_00921};
DE EC=2.7.11.32 {ECO:0000256|HAMAP-Rule:MF_00921};
DE EC=2.7.4.27 {ECO:0000256|HAMAP-Rule:MF_00921};
GN OrderedLocusNames=CCNA_00001 {ECO:0000313|EMBL:ACL93468.1};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL93468.1, ECO:0000313|Proteomes:UP000001364};
RN [1] {ECO:0000313|EMBL:ACL93468.1, ECO:0000313|Proteomes:UP000001364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX PubMed=20472802; DOI=10.1128/JB.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00921};
CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC regulatory protein family. PDRP subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_00921}.
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DR EMBL; CP001340; ACL93468.1; -; Genomic_DNA.
DR RefSeq; WP_012639851.1; NC_011916.1.
DR RefSeq; YP_002515376.1; NC_011916.1.
DR AlphaFoldDB; A0A0H3C520; -.
DR GeneID; 7332728; -.
DR KEGG; ccs:CCNA_00001; -.
DR PATRIC; fig|565050.3.peg.1; -.
DR HOGENOM; CLU_046206_2_0_5; -.
DR OrthoDB; 9782201at2; -.
DR PhylomeDB; A0A0H3C520; -.
DR Proteomes; UP000001364; 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: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 {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00921};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00921}; Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_00921};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00921}.
FT BINDING 175..182
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00921"
SQ SEQUENCE 301 AA; 33170 MW; 0131E1BE60781A65 CRC64;
MVKQPLTDDP QESLAQGESE RLPPRFATYF HIHLVSDSTG ETLNAMARAV CARFTDILPI
EHIYALVRST RQLDRALEEI AGAPGVVMHT IVDPGLRAAL EEGCRKLEMP CIAALDPVIS
AMSRYLGARI STRVGAQHAL TNDYFDRIEA LDYAIAHDDG QGGQDLTQAD VILVGVSRTS
KTPTCIYLAH RGVRAANVPL VPGRPPPPEL FELKNTLIVG LITSPDRLIQ IRRNRLLSLK
ENRESDYVDA DAVRQEIIAA RRLFERQNWP VIDITRRSVE ETAAAVINLL SGGRGKVEVL
G
//
