(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BII0_GEOS0

ID   A0A0F6BII0_GEOS0        Unreviewed;       311 AA.
AC   A0A0F6BII0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 21.
DE   RecName: Full=HPr kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754002};
DE            Short=HPrK/P {ECO:0000256|HAMAP-Rule:MF_01249};
DE            EC=2.7.11.- {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754007};
DE            EC=2.7.4.- {ECO:0000256|HAMAP-Rule:MF_01249, ECO:0000256|SAAS:SAAS00754021};
DE   AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000256|HAMAP-Rule:MF_01249};
GN   Name=hprK {ECO:0000256|HAMAP-Rule:MF_01249};
GN   OrderedLocusNames=GY4MC1_0389 {ECO:0000313|EMBL:ADP73231.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73231.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73231.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73231.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-
CC       dependent phosphorylation of a specific serine residue in HPr, a
CC       phosphocarrier protein of the phosphoenolpyruvate-dependent sugar
CC       phosphotransferase system (PTS). HprK/P also catalyzes the
CC       pyrophosphate-producing, inorganic phosphate-dependent
CC       dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-
CC       Ser-HPr). The two antagonistic activities of HprK/P are regulated
CC       by several intracellular metabolites, which change their
CC       concentration in response to the absence or presence of rapidly
CC       metabolisable carbon sources (glucose, fructose, etc.) in the
CC       growth medium. Also phosphorylates/dephosphorylates the HPr-like
CC       catabolite repression protein crh on a specific serine residue.
CC       Therefore, by controlling the phosphorylation state of HPr and
CC       crh, HPrK/P is a sensor enzyme that plays a major role in the
CC       regulation of carbon metabolism and sugar transport: it mediates
CC       carbon catabolite repression (CCR), and regulates PTS-catalyzed
CC       carbohydrate uptake and inducer exclusion. {ECO:0000256|HAMAP-
CC       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:0000256|HAMAP-Rule:MF_01249,
CC         ECO:0000256|SAAS:SAAS01117191};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[HPr protein]-O-phospho-L-serine + H(+) + phosphate =
CC         [HPr protein]-L-serine + diphosphate; Xref=Rhea:RHEA:46604,
CC         Rhea:RHEA-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:0000256|HAMAP-Rule:MF_01249,
CC         ECO:0000256|SAAS:SAAS01117182};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01249, ECO:0000256|SAAS:SAAS00754019};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01249,
CC       ECO:0000256|SAAS:SAAS00754027}.
CC   -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
CC       {ECO:0000256|HAMAP-Rule:MF_01249}.
CC   -!- MISCELLANEOUS: Both phosphorylation and phosphorolysis are carried
CC       out by the same active site and suggest a common mechanism for
CC       both reactions. {ECO:0000256|HAMAP-Rule:MF_01249}.
CC   -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000256|HAMAP-
CC       Rule:MF_01249, ECO:0000256|SAAS:SAAS00754005}.
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DR   EMBL; CP002293; ADP73231.1; -; Genomic_DNA.
DR   RefSeq; WP_003248054.1; NC_014650.1.
DR   EnsemblBacteria; ADP73231; ADP73231; GY4MC1_0389.
DR   GeneID; 29236953; -.
DR   KEGG; gmc:GY4MC1_0389; -.
DR   KO; K06023; -.
DR   OMA; IQKPGLA; -.
DR   OrthoDB; 391150at2; -.
DR   BioCyc; GSP581103:G1GOQ-434-MONOMER; -.
DR   Proteomes; UP000002034; 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   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; 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;
DR   PRODOM; A0A0F6BII0.
DR   SWISS-2DPAGE; A0A0F6BII0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01249,
KW   ECO:0000256|SAAS:SAAS00754014};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01249};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01249,
KW   ECO:0000256|SAAS:SAAS00754009, ECO:0000313|EMBL:ADP73231.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01249,
KW   ECO:0000256|SAAS:SAAS00754024};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01249,
KW   ECO:0000256|SAAS:SAAS00754029};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01249,
KW   ECO:0000256|SAAS:SAAS00754025};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01249,
KW   ECO:0000256|SAAS:SAAS00754003};
KW   Serine/threonine-protein kinase {ECO:0000256|HAMAP-Rule:MF_01249,
KW   ECO:0000256|SAAS:SAAS00754023};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01249,
KW   ECO:0000256|SAAS:SAAS00754008}.
FT   DOMAIN        4    127       Hpr_kinase_N. {ECO:0000259|Pfam:PF02603}.
FT   DOMAIN      130    298       Hpr_kinase_C. {ECO:0000259|Pfam:PF07475}.
FT   NP_BIND     153    160       ATP. {ECO:0000256|HAMAP-Rule:MF_01249}.
FT   REGION      201    210       Important for the catalytic mechanism of
FT                                both phosphorylation and
FT                                dephosphorylation. {ECO:0000256|HAMAP-
FT                                Rule:MF_01249}.
FT   REGION      264    269       Important for the catalytic mechanism of
FT                                dephosphorylation. {ECO:0000256|HAMAP-
FT                                Rule:MF_01249}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_01249}.
FT   ACT_SITE    159    159       {ECO:0000256|HAMAP-Rule:MF_01249}.
FT   ACT_SITE    177    177       Proton acceptor; for phosphorylation
FT                                activity. Proton donor; for
FT                                dephosphorylation activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01249}.
FT   ACT_SITE    243    243       {ECO:0000256|HAMAP-Rule:MF_01249}.
FT   METAL       160    160       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01249}.
FT   METAL       202    202       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01249}.
SQ   SEQUENCE   311 AA;  34719 MW;  C9592882E0C5DE6E CRC64;
     MPKVRTKDII EKFQLELVSG AEGIYRPITT SDLSRPGIEM AGYFAYYPAE RIQLLGRTEL
     SFYETLSPEE KKIRMERLCT DITPGIIVSR GLEVPPELIE ASERQSVPVM RSTMKTTRLS
     SRLTNYLESK LAPTTAVHGV LVDVYGVGVL ITGKSGVGKS ETALELVKRG HRLVADDCVE
     IRQEDEGMLV GSAPELIEHL LEIRGLGIIN MMTLFGAGAV RTHKRISLVI DLELWDPNKQ
     YDRLGLEEEK VKILDTELPK LTIPVRPGRN LAVIVEVAAM NFRLKRMGVN AAEEFSARLT
     DAIEDGEHDY E
//

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