ID A0A264W5J0_9BACL Unreviewed; 278 AA.
AC A0A264W5J0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
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 ORFNames=CF394_04765 {ECO:0000313|EMBL:OZS78853.1};
OS Tetzosporium hominis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Tetzosporium.
OX NCBI_TaxID=2020506 {ECO:0000313|EMBL:OZS78853.1, ECO:0000313|Proteomes:UP000217065};
RN [1] {ECO:0000313|EMBL:OZS78853.1, ECO:0000313|Proteomes:UP000217065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VT-49 {ECO:0000313|EMBL:OZS78853.1,
RC ECO:0000313|Proteomes:UP000217065};
RA Tetz G., Tetz V.;
RT "Tetzosporium hominis gen.nov. sp.nov.";
RL Submitted (JUL-2017) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZS78853.1}.
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DR EMBL; NOKQ01000187; OZS78853.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A264W5J0; -.
DR OrthoDB; 9782201at2; -.
DR Proteomes; UP000217065; Unassembled WGS sequence.
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}; Pyruvate {ECO:0000313|EMBL:OZS78853.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217065};
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 156..163
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00921"
SQ SEQUENCE 278 AA; 31515 MW; E6A738FB41019028 CRC64;
MIFKESDLVH IFIISDSIGE TGELVAKAAL SQFEDVYHKA RIKRFTHIDS LEYIQEIVDL
AKSHQAIIIY TLVRDDMKQQ VAILSEMAGV EAIDLMGPVI EKFEKVIGIH AMQEPGLVRR
LDEDYFAKIE AVEFAVKYDD GRDPRGLLQA DIVLVGVSRT SKTPLSQYLA NKRWKVANVP
LVPEVDPPEE LFHIDPAKCF GLVINPEKLN SIRRERLKAI GLSDEANYAK IERIQEELKH
FHAVVDRIGC EVIDVTNRAV EETANIIISK RQESTKQL
//