(data stored in SCRATCH zone)

SWISSPROT: PDRP_BACSU

ID   PDRP_BACSU              Reviewed;         270 AA.
AC   P54470;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 115.
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   Name=yqfL; OrderedLocusNames=BSU25240;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-270.
RX   PubMed=3086839; DOI=10.1093/nar/14.10.4293;
RA   Wang L.F., Doi R.H.;
RT   "Nucleotide sequence and organization of Bacillus subtilis RNA polymerase
RT   major sigma (sigma 43) operon.";
RL   Nucleic Acids Res. 14:4293-4307(1986).
RN   [4]
RP   FUNCTION IN GLUCONEOGENESIS REGULATION, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15720552; DOI=10.1111/j.1365-2958.2005.04473.x;
RA   Servant P., Le Coq D., Aymerich S.;
RT   "CcpN (YqzB), a novel regulator for CcpA-independent catabolite repression
RT   of Bacillus subtilis gluconeogenic genes.";
RL   Mol. Microbiol. 55:1435-1451(2005).
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, ECO:0000269|PubMed:15720552}.
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   -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:15720552}.
CC   -!- DISRUPTION PHENOTYPE: Lowers the level of gapB and pckA transcription
CC       threefold under both glycolytic and gluconeogenic conditions.
CC       {ECO:0000269|PubMed:15720552}.
CC   -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC       regulatory protein family. PDRP subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00921}.
DR   EMBL; D84432; BAA12486.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14453.1; -; Genomic_DNA.
DR   EMBL; X03897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; G69953; G69953.
DR   RefSeq; NP_390402.1; NC_000964.3.
DR   RefSeq; WP_003230064.1; NZ_JNCM01000036.1.
DR   SMR; P54470; -.
DR   STRING; 224308.BSU25240; -.
DR   jPOST; P54470; -.
DR   PaxDb; P54470; -.
DR   PRIDE; P54470; -.
DR   EnsemblBacteria; CAB14453; CAB14453; BSU25240.
DR   GeneID; 937889; -.
DR   KEGG; bsu:BSU25240; -.
DR   PATRIC; fig|224308.179.peg.2743; -.
DR   eggNOG; ENOG4105CF9; Bacteria.
DR   eggNOG; COG1806; LUCA.
DR   HOGENOM; HOG000218052; -.
DR   InParanoid; P54470; -.
DR   KO; K09773; -.
DR   OMA; TSKTPTC; -.
DR   PhylomeDB; P54470; -.
DR   BioCyc; BSUB:BSU25240-MONOMER; -.
DR   Proteomes; UP000001570; 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   1: Evidence at protein level;
DR   PRODOM; P54470.
DR   SWISS-2DPAGE; P54470.
KW   Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..270
FT                   /note="Putative pyruvate, phosphate dikinase regulatory
FT                   protein"
FT                   /id="PRO_0000196630"
FT   NP_BIND         151..158
FT                   /note="ADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00921"
FT   CONFLICT        40..41
FT                   /note="IP -> NS (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   270 AA;  30349 MW;  55461D5B2C3BF252 CRC64;
     MNNRIIYVVS DSVGETAELV VKAALSQFNG SADDTHVRRI PYVEDIGTIN EVISLAKADG
     GIICFTLVVP EIREYLIAEA EKANVLYYDI IGPLIDKMET AYGLTAKYEP GRVRQLDEDY
     FKKVEAIEFA VKYDDGRDPR GILKADIVLI GVSRTSKTPL SQYLAHKRLK VANVPIVPEV
     DPPEELFNVD PKKCIGLKIS PDKLNHIRKE RLKSLGLNDK AIYANINRIK EELEYFEKIV
     DRIGCQVVDV SNKAVEETAN IIHHLKTKNI
//

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