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HPRK_STAS1
ID   HPRK_STAS1              Reviewed;         313 AA.
AC   Q49VV8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=SSP1957;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE19102.1; -; Genomic_DNA.
DR   RefSeq; WP_011303626.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49VV8; -.
DR   SMR; Q49VV8; -.
DR   STRING; 342451.SSP1957; -.
DR   EnsemblBacteria; BAE19102; BAE19102; SSP1957.
DR   KEGG; ssp:SSP1957; -.
DR   PATRIC; fig|342451.11.peg.1950; -.
DR   eggNOG; COG1493; Bacteria.
DR   HOGENOM; CLU_052030_0_1_9; -.
DR   OMA; AMNNRQK; -.
DR   OrthoDB; 391150at2; -.
DR   Proteomes; UP000006371; 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..313
FT                   /note="HPr kinase/phosphorylase"
FT                   /id="PRO_0000058990"
FT   REGION          199..208
FT                   /note="Important for the catalytic mechanism of both
FT                   phosphorylation and dephosphorylation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   REGION          262..267
FT                   /note="Important for the catalytic mechanism of
FT                   dephosphorylation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        175
FT                   /note="Proton acceptor; for phosphorylation activity.
FT                   Proton donor; for dephosphorylation activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         151..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         158
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
FT   BINDING         200
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01249"
SQ   SEQUENCE   313 AA;  35197 MW;  5A8DE218DEBAA986 CRC64;
     MLTTQSLVER FKLEVITGEA GLNKQIKNTD ISRPGLEMAG YFSHYASDRI QLLGTTELSF
     YNLLPDEERK GRMRKLCRPE TPAIIVTRDL EPPEELIEAA KENETPLITS TIATTQLMSR
     LTTFLEHELA RTTSLHGVLV DVYGVGVLIT GDSGIGKSET ALELIKRGHR LVADDNVEIR
     EISKDELTGR APKLIEHLLE IRGLGIINVM TLFGAGSILT EKRLRLNIHL ENWHKEKLYD
     RVGLNEETLR ILDTEITKKT IPVRPGRNVA VIIEVAAMNY RLNIMGINTA EEFNERLNAE
     ILRNGNHSEG NNQ
 
 
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