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HPRK1_OCEIH
ID   HPRK1_OCEIH             Reviewed;         310 AA.
AC   Q8ENK1;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=HPr kinase/phosphorylase 1;
DE            Short=HPrK/P 1;
DE            EC=2.7.11.-;
DE            EC=2.7.4.-;
DE   AltName: Full=HPr(Ser) kinase/phosphorylase 1;
GN   Name=hprK1; OrderedLocusNames=OB2482;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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. 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 crh,
CC       HPrK/P is a sensor enzyme that plays a major role in the regulation of
CC       carbon metabolism and sugar transport: it mediates carbon catabolite
CC       repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and
CC       inducer exclusion (By similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
CC       {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000305}.
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DR   EMBL; BA000028; BAC14438.1; -; Genomic_DNA.
DR   RefSeq; WP_011066875.1; NC_004193.1.
DR   AlphaFoldDB; Q8ENK1; -.
DR   SMR; Q8ENK1; -.
DR   STRING; 221109.22778168; -.
DR   PRIDE; Q8ENK1; -.
DR   EnsemblBacteria; BAC14438; BAC14438; BAC14438.
DR   KEGG; oih:OB2482; -.
DR   eggNOG; COG1493; Bacteria.
DR   HOGENOM; CLU_052030_0_1_9; -.
DR   OMA; AMNNRQK; -.
DR   OrthoDB; 391150at2; -.
DR   PhylomeDB; Q8ENK1; -.
DR   Proteomes; UP000000822; 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; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..310
FT                   /note="HPr kinase/phosphorylase 1"
FT                   /id="PRO_0000058978"
FT   REGION          202..211
FT                   /note="Important for the catalytic mechanism of both
FT                   phosphorylation and dephosphorylation"
FT                   /evidence="ECO:0000250"
FT   REGION          265..270
FT                   /note="Important for the catalytic mechanism of
FT                   dephosphorylation"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        139
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /note="Proton acceptor; for phosphorylation activity.
FT                   Proton donor; for dephosphorylation activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        244
FT                   /evidence="ECO:0000250"
FT   BINDING         154..161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   310 AA;  34831 MW;  84114BA62212B633 CRC64;
     MVAVVRTQDL LDNFNLTLVS GEDGIQREII TSDISRPGIE MTGYFRYYPK ERLQLIGKTE
     MAYFLDLSSE QRRDRAERLC TDITPGIVVS RGMDIPEELK EASEKSGVPI LQSPRKTTRV
     ISRLTNYLES KFAPFTAIHG VLVDIYGVGV LIIGQSGVGK SETALELVKR GHRLVADDNV
     EIRQEDYDSL IGNAPPLIEH LLEIRGLGII NVMTLFGAGS VRSKKRISLV INLENWDEKK
     QYDRLGLDED MMKVMDVHLP KATVPVRPGR NLAVIIEVAA MNFRLKRMGV NTAEEFSERL
     STMIEKGELE
 
 
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