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Database: UniProt
Entry: A0A0C2HDY1_9STAP
LinkDB: A0A0C2HDY1_9STAP
Original site: A0A0C2HDY1_9STAP 
ID   A0A0C2HDY1_9STAP        Unreviewed;       274 AA.
AC   A0A0C2HDY1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=SN16_00335 {ECO:0000313|EMBL:KIH71850.1};
OS   Salinicoccus roseus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Salinicoccus.
OX   NCBI_TaxID=45670 {ECO:0000313|EMBL:KIH71850.1, ECO:0000313|Proteomes:UP000031546};
RN   [1] {ECO:0000313|EMBL:KIH71850.1, ECO:0000313|Proteomes:UP000031546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W12 {ECO:0000313|EMBL:KIH71850.1,
RC   ECO:0000313|Proteomes:UP000031546};
RA   Wang H., Yu B.;
RT   "Genome sequences of high lactate-tolerant strain Salinicoccus roseus W12
RT   with industrial interest.";
RL   Submitted (JAN-2015) 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:KIH71850.1}.
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DR   EMBL; JXII01000001; KIH71850.1; -; Genomic_DNA.
DR   RefSeq; WP_040104627.1; NZ_JXII01000001.1.
DR   AlphaFoldDB; A0A0C2HDY1; -.
DR   STRING; 45670.SN16_00335; -.
DR   GeneID; 77843986; -.
DR   OrthoDB; 9782201at2; -.
DR   Proteomes; UP000031546; 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}; Reference proteome {ECO:0000313|Proteomes:UP000031546};
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         151..158
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00921"
SQ   SEQUENCE   274 AA;  30677 MW;  6E7953716A221010 CRC64;
     MSKIKVIVAS DSVGETGELV AKACLSQFNV DESDEVLIRY PYIESEENVD DVIDLAKSKN
     AIVVFTIITP ELRKYIKQEL QTENIASVDI MGPLMSILEG KAEEAPYYEP GRVHRLDEDY
     FKKIEAIEFA VKYDDGKDAS GLDKADIVLI GVSRTSKTPL SQYLAHKKYK VMNVPMVPEV
     TPPKELYNVD PNKCVGLKIN PTSLNKIRKE RLAQLGLKDT ASYANDQRIQ EELDYFNEVI
     GKIGCPVIDV SEKAIEETAN EILDYVEGRP DIKG
//
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