HPRK_STREI
ID HPRK_STREI Reviewed; 310 AA.
AC Q9WXK7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=HPr kinase/phosphorylase;
DE Short=HPrK/P;
DE EC=2.7.11.-;
DE EC=2.7.4.-;
DE AltName: Full=HPr(Ser) kinase/phosphorylase;
GN Name=hprK;
OS Streptococcus equinus (Streptococcus bovis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1335;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 700410 / JB1;
RX PubMed=12610726; DOI=10.1007/s00203-003-0516-9;
RA Asanuma N., Hino T.;
RT "Molecular characterization of HPr and related enzymes, and regulation of
RT HPr phosphorylation in the ruminal bacterium Streptococcus bovis.";
RL Arch. Microbiol. 179:205-213(2003).
CC -!- FUNCTION: Catalyzes the ATP- as well as probably the pyrophosphate-
CC dependent phosphorylation of 'Ser-46' in HPr, a phosphocarrier protein
CC of the phosphoenolpyruvate-dependent sugar phosphotransferase system
CC (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic
CC phosphate-dependent dephosphorylation (phosphorolysis) of seryl-
CC phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of
CC HprK/P are regulated by several intracellular metabolites, which change
CC their concentration in response to the absence or presence of rapidly
CC metabolisable carbon sources (glucose, fructose, etc.) in the growth
CC medium. Therefore, by controlling the phosphorylation state of HPr, the
CC HPrK/P is a sensor enzyme that plays a major role in the regulation of
CC carbon metabolism and sugar transport: it probably mediates carbon
CC catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate
CC uptake and inducer exclusion.
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;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- ACTIVITY REGULATION: Kinase activity is inhibited by inorganic
CC phosphate (Pi). In contrast to many other bacteria, neither kinase
CC activity nor phosphorylase activity is affected by fructose 1,6-
CC bisphosphate (FBP).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0 for both kinase and phosphorylase reactions.
CC Activity decreases to less than 10% of the maximal activity at pH
CC 5.5.;
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- INDUCTION: Constitutively expressed. Transcription of S.bovis hprK is
CC not significantly altered by growth rate or energy source.
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: PubMed:12610726 presented the dephosphorylation reaction
CC catalyzed by HPrK/P as a phosphatase activity, but it is most likely a
CC phosphorylase activity as shown in B.subtilis. {ECO:0000305}.
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DR EMBL; AB027460; BAA77782.1; -; Genomic_DNA.
DR RefSeq; WP_020917207.1; NZ_LPVR01000001.1.
DR AlphaFoldDB; Q9WXK7; -.
DR SMR; Q9WXK7; -.
DR GeneID; 58528586; -.
DR GeneID; 66896116; -.
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 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..310
FT /note="HPr kinase/phosphorylase"
FT /id="PRO_0000058994"
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 ACT_SITE 243
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"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
SQ SEQUENCE 310 AA; 34686 MW; 6D24300CA7D443D2 CRC64;
MSVTVKMLVD KVKLDVIYGD DDLLSKEITT SDISRPGLEM TGYFDYYSPE RLQLLGMKEW
SYLTKMTSHN RRHVLREMIK PETPAIIVAR NLAIPEEMIS AAKEKGIAIL QSHVPTSRLS
GEMSWYLDSC LAERTSVHGV LMDIYGMGVL IQGDSGIGKS ETGLELVKRG HRLVADDRVD
VFAKDEETLW GEPAEILRHL LEIRGVGIID VMSLYGASAV KDSSQVQLAI YLENYESGKV
FDRLGNGNEE LELSGVKIPR LRIPVQTGRN MSVVIEAAAM NYRAKQMGFD ATKTFEERLT
QLITKNEGNQ
