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Database: UniProt
Entry: A0A264W5J0_9BACL
LinkDB: A0A264W5J0_9BACL
Original site: A0A264W5J0_9BACL 
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
//
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