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HPRK_LISW6
ID   HPRK_LISW6              Reviewed;         312 AA.
AC   A0ALG7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=HPr kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249};
DE            Short=HPrK/P {ECO:0000255|HAMAP-Rule:MF_01249};
DE            EC=2.7.11.- {ECO:0000255|HAMAP-Rule:MF_01249};
DE            EC=2.7.4.- {ECO:0000255|HAMAP-Rule:MF_01249};
DE   AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249};
GN   Name=hprK {ECO:0000255|HAMAP-Rule:MF_01249}; OrderedLocusNames=lwe2431;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS   NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX   PubMed=16936040; DOI=10.1128/jb.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
CC   -!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent
CC       phosphorylation of a specific serine residue in HPr, a phosphocarrier
CC       protein of the phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS). HprK/P also catalyzes the pyrophosphate-producing,
CC       inorganic phosphate-dependent dephosphorylation (phosphorolysis) of
CC       seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities
CC       of HprK/P are regulated by several intracellular metabolites, which
CC       change their concentration in response to the absence or presence of
CC       rapidly metabolisable carbon sources (glucose, fructose, etc.) in the
CC       growth medium. Therefore, by controlling the phosphorylation state of
CC       HPr, HPrK/P is a sensor enzyme that plays a major role in the
CC       regulation of carbon metabolism and sugar transport: it mediates carbon
CC       catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate
CC       uptake and inducer exclusion. {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[HPr protein]-L-serine + ATP = [HPr protein]-O-phospho-L-
CC         serine + ADP + H(+); Xref=Rhea:RHEA:46600, Rhea:RHEA-COMP:11602,
CC         Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[HPr protein]-O-phospho-L-serine + H(+) + phosphate = [HPr
CC         protein]-L-serine + diphosphate; Xref=Rhea:RHEA:46604, Rhea:RHEA-
CC         COMP:11602, Rhea:RHEA-COMP:11603, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
CC       {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried out
CC       by the same active site and suggest a common mechanism for both
CC       reactions. {ECO:0000255|HAMAP-Rule:MF_01249}.
CC   -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000255|HAMAP-
CC       Rule:MF_01249}.
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DR   EMBL; AM263198; CAK21849.1; -; Genomic_DNA.
DR   RefSeq; WP_011703167.1; NC_008555.1.
DR   AlphaFoldDB; A0ALG7; -.
DR   SMR; A0ALG7; -.
DR   STRING; 386043.lwe2431; -.
DR   EnsemblBacteria; CAK21849; CAK21849; lwe2431.
DR   GeneID; 61190350; -.
DR   KEGG; lwe:lwe2431; -.
DR   eggNOG; COG1493; Bacteria.
DR   HOGENOM; CLU_052030_0_1_9; -.
DR   OMA; AMNNRQK; -.
DR   OrthoDB; 391150at2; -.
DR   Proteomes; UP000000779; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01918; HprK_C; 1.
DR   Gene3D; 3.40.1390.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01249; HPr_kinase; 1.
DR   InterPro; IPR003755; HPr(Ser)_kin/Pase.
DR   InterPro; IPR011104; Hpr_kin/Pase_C.
DR   InterPro; IPR011126; Hpr_kin/Pase_Hpr_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR028979; Ser_kin/Pase_Hpr-like_N_sf.
DR   PANTHER; PTHR30305:SF1; PTHR30305:SF1; 1.
DR   Pfam; PF07475; Hpr_kinase_C; 1.
DR   Pfam; PF02603; Hpr_kinase_N; 1.
DR   SUPFAM; SSF75138; SSF75138; 1.
DR   TIGRFAMs; TIGR00679; hpr-ser; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..312
FT                   /note="HPr kinase/phosphorylase"
FT                   /id="PRO_1000067159"
FT   REGION          202..211
FT                   /note="Important for the catalytic mechanism of both
FT                   phosphorylation and dephosphorylation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   REGION          265..270
FT                   /note="Important for the catalytic mechanism of
FT                   dephosphorylation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        178
FT                   /note="Proton acceptor; for phosphorylation activity.
FT                   Proton donor; for dephosphorylation activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
SQ   SEQUENCE   312 AA;  34958 MW;  5E2BD67029D9D53E CRC64;
     MTKSVTVKDL KERLNLELIC SETGLERPIL TSDLSRPGLE LTGFFSYYPE DRVQLFGMTE
     ISFSEGMEPE ERLKRYKQMC TKRTPAFVIS RNLEVPKELV AAAKEADIPV LRSRLKTTRL
     SVYITNYLES RLAPVISMHG VLVDIYGLGV LITGSSGVGK SETALELVKR GHRLVADDNV
     EIRQEDELTL IGSSPAIIEH LLEIRGLGII NVMTLFGAGA VRSSKKITIV VHLENWDPDK
     HYDRVGLDQE KTKIFDMDIP KITVPVRPGR NLSVIIEVAA MNFRLKNMGY NAAEQFTQDL
     NNLIGHNSSM ND
 
 
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