HPRK_STRSL
ID HPRK_STRSL Reviewed; 309 AA.
AC Q9ZA98;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 salivarius.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1304;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RC STRAIN=ATCC 25975;
RX PubMed=9922231; DOI=10.1128/jb.181.3.709-717.1999;
RA Brochu D., Vadeboncoeur C.;
RT "The HPr(Ser) kinase of Streptococcus salivarius: purification, properties,
RT and cloning of the hprK gene.";
RL J. Bacteriol. 181:709-717(1999).
RN [2]
RP CHARACTERIZATION, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 25975;
RX PubMed=12855169; DOI=10.1016/s0378-1097(03)00429-4;
RA Frey N., Nessler S., Fieulaine S., Vaillancourt K., Frenette M.,
RA Vadeboncoeur C.;
RT "The HPr(Ser) kinase of Streptococcus salivarius: a hexameric bifunctional
RT enzyme controlled by glycolytic intermediates and inorganic phosphate.";
RL FEMS Microbiol. Lett. 224:67-72(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 bifunctional HPr kinase/phosphorylase is a sensor enzyme that plays a
CC major role in the regulation of carbon metabolism and sugar transport:
CC it probably mediates carbon catabolite repression (CCR), and regulates
CC PTS-catalyzed carbohydrate 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 -!- ACTIVITY REGULATION: Kinase activity is slightly activated by fructose
CC 1,6-bisphosphate (FBP) at low ATP concentrations, and is inhibited by
CC inorganic phosphate (Pi). Moreover, FBP, phosphoenolpyruvate and 2-
CC phosphoglycerate, but not fructose 1-P, fructose 6-P, and ribulose 1,5-
CC bisphosphate protect kinase activity against inhibition by Pi.
CC Dephosphorylation of P-Ser-HPr by S.salivarius HPrK/P is strictly
CC dependent on the presence of Pi, and is inhibited by FBP. FBP seems to
CC modulate HPrK/P activities by enhancing affinity of the active site for
CC ATP and, conversely, lowering the affinity for Pi.
CC {ECO:0000269|PubMed:12855169}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 uM for HPr;
CC KM=5 uM for HPr(Ser-P);
CC KM=1 mM for ATP;
CC pH dependence:
CC Optimum pH is 7.5. Active from pH 5.5 to 9.5. At pH 5.5, exhibits
CC less than 15% of its optimal activity.;
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:12855169}.
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; AF069743; AAD12781.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9ZA98; -.
DR SMR; Q9ZA98; -.
DR STRING; 1304.HMPREF3219_0201753; -.
DR SABIO-RK; Q9ZA98; -.
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 Allosteric enzyme; ATP-binding; Carbohydrate metabolism;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..309
FT /note="HPr kinase/phosphorylase"
FT /id="PRO_0000059002"
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 309 AA; 34440 MW; B47C831F44563C64 CRC64;
MTVTVKMLVD KLKLKVIYGN EKLLSKPITT ADISRPGLEM TGYFDFYSPE RIQLVGMKEW
SYLKTLTDHN RYSVFSNMFK EETPAVIVAR GLDIPEEMYR AAKENGVAVL QGRNGTSSLS
GDMSWYLNAQ LAERTSVHGV LVDIYGMGVL IQGDSGIGKS ETGLELVKRG HRLVADDRVD
VYAKDEETLW GEPAEILHHL LEIRGVGIID VMSLYGASAV RNSSQVQLAI YLENFEDGKV
FDRLGNGNEE IELQGVKIPR VRIPVKTGRN VSVVIEAAAM NYRAKQMGFD ATKTFEERLT
NLISKNGED
