HPRK_STRPN
ID HPRK_STRPN Reviewed; 312 AA.
AC Q97Q18;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=HPr kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249};
DE Short=HPrK/P {ECO:0000255|HAMAP-Rule:MF_01249};
DE EC=2.7.11.- {ECO:0000255|HAMAP-Rule:MF_01249};
DE EC=2.7.4.- {ECO:0000255|HAMAP-Rule:MF_01249};
DE AltName: Full=HPr(Ser) kinase/phosphorylase {ECO:0000255|HAMAP-Rule:MF_01249};
GN Name=hprK {ECO:0000255|HAMAP-Rule:MF_01249}; OrderedLocusNames=SP_1413;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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. Therefore, by controlling the phosphorylation state of
CC HPr, HPrK/P is a sensor enzyme that plays a major role in the
CC regulation of carbon metabolism and sugar transport: it mediates carbon
CC catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate
CC uptake and inducer exclusion. {ECO:0000255|HAMAP-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:0000255|HAMAP-Rule:MF_01249};
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; Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01249};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01249}.
CC -!- DOMAIN: The Walker A ATP-binding motif also binds Pi and PPi.
CC {ECO:0000255|HAMAP-Rule:MF_01249}.
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:0000255|HAMAP-Rule:MF_01249}.
CC -!- SIMILARITY: Belongs to the HPrK/P family. {ECO:0000255|HAMAP-
CC Rule:MF_01249}.
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DR EMBL; AE005672; AAK75511.1; -; Genomic_DNA.
DR PIR; F95164; F95164.
DR AlphaFoldDB; Q97Q18; -.
DR SMR; Q97Q18; -.
DR STRING; 170187.SP_1413; -.
DR EnsemblBacteria; AAK75511; AAK75511; SP_1413.
DR KEGG; spn:SP_1413; -.
DR eggNOG; COG1493; Bacteria.
DR OMA; AMNNRQK; -.
DR PhylomeDB; Q97Q18; -.
DR Proteomes; UP000000585; 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;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..312
FT /note="HPr kinase/phosphorylase"
FT /id="PRO_0000058996"
FT REGION 202..211
FT /note="Important for the catalytic mechanism of both
FT phosphorylation and dephosphorylation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT REGION 265..270
FT /note="Important for the catalytic mechanism of
FT dephosphorylation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT ACT_SITE 139
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT ACT_SITE 160
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT ACT_SITE 178
FT /note="Proton acceptor; for phosphorylation activity.
FT Proton donor; for dephosphorylation activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT ACT_SITE 244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
SQ SEQUENCE 312 AA; 34858 MW; 8DAF8D866C1D751E CRC64;
MMSVLVKEVI EKLRLDIVYG EPELLEKEIN TADITRPGLE MTGYFDYYTP ERIQLLGMKE
WSYLISMPSN SRYEVLKKMF LPETPAVIVA RGLVVPEEML KAARECKIAI LTSRAATSRL
SGELSSYLDS RLAERTSVHG VLMDIYGMGV LIQGDSGIGK SETGLELVKR GHRLVADDRV
DIFAKDEITL WGEPAEILKH LIEIRGVGII DVMSLYGASA VKDSSQVQLA VYLENYDTHK
TFDRLGNNAE ELEVSGVAIP RIRIPVKTGR NISVVIEAAA MNYRAKEMGF DATRLFDERL
TSLIARNEVQ NA
