(data stored in ACNUC1104 zone)

SWISSPROT: PSRP_BORPA

ID   PSRP_BORPA              Reviewed;         275 AA.
AC   Q7WA44;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   05-DEC-2018, entry version 76.
DE   RecName: Full=Putative phosphoenolpyruvate synthase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062};
DE            Short=PEP synthase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062};
DE            Short=PSRP {ECO:0000255|HAMAP-Rule:MF_01062};
DE            EC=2.7.11.33 {ECO:0000255|HAMAP-Rule:MF_01062};
DE            EC=2.7.4.28 {ECO:0000255|HAMAP-Rule:MF_01062};
DE   AltName: Full=Pyruvate, water dikinase regulatory protein {ECO:0000255|HAMAP-Rule:MF_01062};
GN   OrderedLocusNames=BPP1543;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC       involved in the regulation of the phosphoenolpyruvate synthase
CC       (PEPS) by catalyzing its phosphorylation/dephosphorylation.
CC       {ECO:0000255|HAMAP-Rule:MF_01062}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[pyruvate, water dikinase] + ADP = [pyruvate, water
CC         dikinase]-phosphate + AMP + H(+); Xref=Rhea:RHEA:46020,
CC         Rhea:RHEA-COMP:11425, Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; EC=2.7.11.33; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01062};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[pyruvate, water dikinase]-phosphate + H(+) + phosphate =
CC         [pyruvate, water dikinase] + diphosphate; Xref=Rhea:RHEA:48580,
CC         Rhea:RHEA-COMP:11425, Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43176, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:68546; EC=2.7.4.28; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01062};
CC   -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC       regulatory protein family. PSRP subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01062}.
DR   EMBL; BX640427; CAE36845.1; -; Genomic_DNA.
DR   RefSeq; WP_003811765.1; NC_002928.3.
DR   SMR; Q7WA44; -.
DR   EnsemblBacteria; CAE36845; CAE36845; BPP1543.
DR   KEGG; bpa:BPP1543; -.
DR   HOGENOM; HOG000218053; -.
DR   KO; K09773; -.
DR   OMA; TSKTPTC; -.
DR   BioCyc; BPAR257311:G1GSY-1583-MONOMER; -.
DR   Proteomes; UP000001421; 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_01062; PSRP; 1.
DR   InterPro; IPR005177; Kinase-pyrophosphorylase.
DR   InterPro; IPR026530; PSRP.
DR   PANTHER; PTHR31756; PTHR31756; 1.
DR   Pfam; PF03618; Kinase-PPPase; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7WA44.
DR   SWISS-2DPAGE; Q7WA44.
KW   Complete proteome; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    275       Putative phosphoenolpyruvate synthase
FT                                regulatory protein.
FT                                /FTId=PRO_0000196636.
FT   NP_BIND     157    164       ADP. {ECO:0000255|HAMAP-Rule:MF_01062}.
SQ   SEQUENCE   275 AA;  30712 MW;  3B87B2C0BCD16301 CRC64;
     MTSTPIERAV YIVSDSTGIT AETFSHSVLS QFDEVNFKPV RLPFIDTLDK AREVVARINR
     NALEAGVPPI VFSTLVNPEI LALVRQSNGV FLDLFGTFVS HIEQALGLKS SHSIGRSHMA
     ANSEKYRNRI DAINFSLAHD DGQFVNQLDQ ADVILVGVSR CGKTPTSLYL AMQYAVKAAN
     FPLTPDDFER GALPKTIAPY RGKLFGLSIQ PERLAEVRNE RRPNSHYARL EQCRYEVAEA
     ERMMRREGIS WLSTTTKSIE EIATTVLQEV GLERV
//

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