PSRP_SHIF8
ID PSRP_SHIF8 Reviewed; 277 AA.
AC Q0T4R2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=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 Name=ppsR {ECO:0000255|HAMAP-Rule:MF_01062}; OrderedLocusNames=SFV_1521;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
CC -!- FUNCTION: Bifunctional serine/threonine kinase and phosphorylase
CC involved in the regulation of the phosphoenolpyruvate synthase (PEPS)
CC by catalyzing its phosphorylation/dephosphorylation.
CC {ECO:0000255|HAMAP-Rule:MF_01062}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[pyruvate, water dikinase] + ADP = [pyruvate, water dikinase]-
CC phosphate + AMP + H(+); Xref=Rhea:RHEA:46020, Rhea:RHEA-COMP:11425,
CC Rhea:RHEA-COMP:11426, ChEBI:CHEBI:15378, ChEBI:CHEBI:43176,
CC ChEBI:CHEBI:68546, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.11.33; Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; CP000266; ABF03703.1; -; Genomic_DNA.
DR RefSeq; WP_000368046.1; NC_008258.1.
DR AlphaFoldDB; Q0T4R2; -.
DR SMR; Q0T4R2; -.
DR EnsemblBacteria; ABF03703; ABF03703; SFV_1521.
DR GeneID; 66674403; -.
DR KEGG; sfv:SFV_1521; -.
DR HOGENOM; CLU_046206_1_0_6; -.
DR OMA; YAQCEFE; -.
DR BioCyc; SFLE373384:SFV_RS08495-MON; -.
DR Proteomes; UP000000659; 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 GO; GO:0006468; P:protein phosphorylation; 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;
KW Kinase; Nucleotide-binding; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..277
FT /note="Phosphoenolpyruvate synthase regulatory protein"
FT /id="PRO_0000316742"
FT BINDING 157..164
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01062"
SQ SEQUENCE 277 AA; 31211 MW; 25508DEEC2E342CA CRC64;
MDNAVDRHVF YISDGTAITA EVLGHAVMSQ FPVTISSITL PFVENESRAR AVKDQIDAIY
HQTGVRPLVF YSIVLPEIRA IILQSEGFCQ DIVQALVAPL QQEMKLDPTP IAHRTHGLNP
NNLNKYDARI AAIDYTLAHD DGISLRNLDQ AQVILLGVSR CGKTPTSLYL AMQFGIRAAN
YPFIADDMDN LVLPASLKPL QHKLFGLTID PERLAAIREE RRENSRYASL RQCRMEVAEV
EALYRKNQIP WINSTNYSVE EIATKILDIM GLSRRMY