ID A0A0H3FRP5_KLEAK Unreviewed; 277 AA.
AC A0A0H3FRP5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Putative phosphoenolpyruvate synthase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
DE Short=PEP synthase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
DE Short=PSRP {ECO:0000256|HAMAP-Rule:MF_01062};
DE EC=2.7.11.33 {ECO:0000256|HAMAP-Rule:MF_01062};
DE EC=2.7.4.28 {ECO:0000256|HAMAP-Rule:MF_01062};
DE AltName: Full=Pyruvate, water dikinase regulatory protein {ECO:0000256|HAMAP-Rule:MF_01062};
GN OrderedLocusNames=EAE_17070 {ECO:0000313|EMBL:AEG98325.1};
OS Klebsiella aerogenes (strain ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235
OS / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56)
OS (Enterobacter aerogenes).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1028307 {ECO:0000313|EMBL:AEG98325.1, ECO:0000313|Proteomes:UP000008881};
RN [1] {ECO:0000313|Proteomes:UP000008881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 /
RC NCIMB 10102 / NCTC 10006 {ECO:0000313|Proteomes:UP000008881};
RA Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.;
RT "Complete sequence of Enterobacter aerogenes KCTC 2190.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG98325.1, ECO:0000313|Proteomes:UP000008881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 /
RC NCIMB 10102 / NCTC 10006 {ECO:0000313|Proteomes:UP000008881};
RX PubMed=22493190; DOI=10.1128/JB.00028-12;
RA Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA Yang K.S.;
RT "Complete genome sequence of Enterobacter aerogenes KCTC 2190.";
RL J. Bacteriol. 194:2373-2374(2012).
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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_01062};
CC -!- SIMILARITY: Belongs to the pyruvate, phosphate/water dikinase
CC regulatory protein family. PSRP subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01062}.
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DR EMBL; CP002824; AEG98325.1; -; Genomic_DNA.
DR RefSeq; WP_015367027.1; NC_015663.1.
DR RefSeq; YP_004593604.1; NC_015663.1.
DR AlphaFoldDB; A0A0H3FRP5; -.
DR GeneID; 66604278; -.
DR KEGG; eae:EAE_17070; -.
DR PATRIC; fig|1028307.3.peg.3415; -.
DR eggNOG; COG1806; Bacteria.
DR HOGENOM; CLU_046206_1_0_6; -.
DR OrthoDB; 9782201at2; -.
DR Proteomes; UP000008881; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_01062; PSRP; 1.
DR InterPro; IPR005177; Kinase-pyrophosphorylase.
DR InterPro; IPR026530; PSRP.
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_01062};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01062};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|HAMAP-Rule:MF_01062};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01062}.
FT BINDING 157..164
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01062"
SQ SEQUENCE 277 AA; 31101 MW; A2D13222E3230D0C CRC64;
MDSAVDRHVF YISDGTAITA EVLGHAVMSQ FPVAISSVTL PFVENVSRAR AVKEQIDAIF
QQTGIRPLVF YSIVIPEIRD IILQSEGFCQ DIVQALVAPL QQELHLDPTP VAHRTHGLNP
GNLIKYDARI AAIDYTLAHD DGISLRNLDQ AQVILLGVSR CGKTPTSLYL AMQYGIRAAN
YPFIADDMDN LVLPASLKPL QHKMFGLTIN PERLAAIREE RRENSRYASL RQCRMEVTEV
EALYRKNKIP CLNSTNYSVE EIATKIMDIM GLNRRMY
//
