HPRK2_OCEIH
ID HPRK2_OCEIH Reviewed; 306 AA.
AC Q8EL04;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative HPr kinase/phosphorylase 2;
DE Short=HPrK/P 2;
DE EC=2.7.11.-;
DE EC=2.7.4.-;
DE AltName: Full=HPr(Ser) kinase/phosphorylase 2;
GN Name=hprK2; OrderedLocusNames=OB3428;
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}.
CC -!- CAUTION: In this second copy of HPRK/P in O.iheyensis, Ala-202 and Glu-
CC 243 are present instead of the conserved Glu and Arg which are
CC respectively expected to be part of the active site. {ECO:0000305}.
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DR EMBL; BA000028; BAC15384.1; -; Genomic_DNA.
DR RefSeq; WP_011067826.1; NC_004193.1.
DR AlphaFoldDB; Q8EL04; -.
DR SMR; Q8EL04; -.
DR STRING; 221109.22779117; -.
DR EnsemblBacteria; BAC15384; BAC15384; BAC15384.
DR KEGG; oih:OB3428; -.
DR eggNOG; COG1493; Bacteria.
DR HOGENOM; CLU_052030_0_1_9; -.
DR OMA; ANNWYLR; -.
DR OrthoDB; 391150at2; -.
DR PhylomeDB; Q8EL04; -.
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 InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
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..306
FT /note="Putative HPr kinase/phosphorylase 2"
FT /id="PRO_0000058979"
FT REGION 201..210
FT /note="Important for the catalytic mechanism of both
FT phosphorylation and dephosphorylation"
FT /evidence="ECO:0000250"
FT REGION 264..269
FT /note="Important for the catalytic mechanism of
FT dephosphorylation"
FT /evidence="ECO:0000250"
FT ACT_SITE 138
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /evidence="ECO:0000250"
FT ACT_SITE 177
FT /note="Proton acceptor; for phosphorylation activity.
FT Proton donor; for dephosphorylation activity"
FT /evidence="ECO:0000250"
FT BINDING 153..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 306 AA; 35049 MW; FE20D84914F9AEFD CRC64;
MKSIQVQQLV EEFNLEVLAG EDHRERTITK SRTHRPGLEF IGYFDFFPME RVQILGKKEI
NYLHQLNEQE RDIRIGNVVN YHPPCFIVTS DQDGLTYLKK YCHAEQIPLL RTKEATVDFM
AKVDHYLTRK LAPEIAVHGV CMNVLGIGIL IRGESGVGKS ELAHTLLGRG HRLVADDIVV
LKRLSHKTIL GTHNDKNKEF LALRSVGLLN VVRAYGSRAF QDETRISLDI KLSKWEKDSL
HNELEFETQY RDYMGVSVPS IEIQLQPGRD VAGLIEAAAN NWYLQQQGYS AAEDFMNRIE
WQDGDD
