(data stored in SCRATCH3701 zone)

SWISSPROT: PDRP_RICTY

ID   PDRP_RICTY              Reviewed;         273 AA.
AC   Q68Y01;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 76.
DE   RecName: Full=Putative pyruvate, phosphate dikinase regulatory protein {ECO:0000255|HAMAP-Rule:MF_00921};
DE            Short=PPDK regulatory protein {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=RT0001;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU03491.1; -; Genomic_DNA.
DR   RefSeq; WP_011190478.1; NC_006142.1.
DR   SMR; Q68Y01; -.
DR   STRING; 257363.RT0001; -.
DR   EnsemblBacteria; AAU03491; AAU03491; RT0001.
DR   KEGG; rty:RT0001; -.
DR   eggNOG; ENOG4105CF9; Bacteria.
DR   eggNOG; COG1806; LUCA.
DR   HOGENOM; HOG000218052; -.
DR   KO; K09773; -.
DR   OMA; TSKTPTC; -.
DR   OrthoDB; 980472at2; -.
DR   BioCyc; RTYP257363:G1G0L-1-MONOMER; -.
DR   Proteomes; UP000000604; 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   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;
DR   PRODOM; Q68Y01.
DR   SWISS-2DPAGE; Q68Y01.
KW   Kinase; Nucleotide-binding; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..273
FT                   /note="Putative pyruvate, phosphate dikinase regulatory
FT                   protein"
FT                   /id="PRO_0000196704"
FT   NP_BIND         149..156
FT                   /note="ADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
SQ   SEQUENCE   273 AA;  31656 MW;  8A8E116D0757994E CRC64;
     MTKLIIHLVS DSSVQTVKHA ANSALAQFTS IKQKLYHWPM IRNLELLNEV LSKIESKHGI
     VLYTIADQEL RKALTKFCYE LKIPCISVIG KIIKEMSVFS GIEIEKEQNY NYKFDKTYFD
     TLNAIDYAIR HDDGQMINEL SESDIILIGP SRTSKTPTSV FLAYNGLKAA NIPYVYNCPF
     PDFIEKNIDQ LVVGLVINPN RLIEIREARL NLLQINENKS YTDFNIVQRE CIEVRKICNQ
     RNWPVIDVST RSIEETAALI MRIYYNRKNK YHK
//

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