ID   HPTS_STAAR              Reviewed;         518 AA.
AC   Q6GK92;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Sensor protein kinase HptS;
DE            EC=2.7.13.3;
GN   Name=hptS; OrderedLocusNames=SAR0215;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Member of the two-component regulatory system HptS/HptR that
CC       regulates genes involved in hexose phosphate transport system in
CC       response to changes in extracellular phosphate sources. May act as a
CC       sensor protein kinase which is autophosphorylated at a histidine
CC       residue and transfers its phosphate group to the conserved aspartic
CC       acid residue in the regulatory domain of HptS. In turn, HptS
CC       antagonizes CcpA-dependent transcription of a subset of CcpA-regulated
CC       genes involved in antibiotic susceptibility.
CC       {ECO:0000250|UniProtKB:Q2G1E0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR   EMBL; BX571856; CAG39242.1; -; Genomic_DNA.
DR   RefSeq; WP_000127979.1; NC_002952.2.
DR   AlphaFoldDB; Q6GK92; -.
DR   SMR; Q6GK92; -.
DR   KEGG; sar:SAR0215; -.
DR   HOGENOM; CLU_525720_0_0_9; -.
DR   OMA; YIWVEHR; -.
DR   OrthoDB; 1031920at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR   Pfam; PF06580; His_kinase; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..518
FT                   /note="Sensor protein kinase HptS"
FT                   /id="PRO_0000299121"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          297..513
FT                   /note="Histidine kinase"
FT   MOD_RES         325
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   518 AA;  61002 MW;  9FC99B0C24D07850 CRC64;
     MTAYKPYRHQ LRRSLFASTI FPVFLVIIIG LVSFYAIYIW IEHRTIHQHV DESQSSLHHT
     EKQIQTFITQ HNNSFQELDL TNHHDVTATK RELLKLIHQQ PATLYYELSG PNQFITNNYE
     HLNTKNMYLF STHQLKFKNS TYMLKIYIAN TPRLSEIKKD SRQFALIVDQ YDNILYANDD
     RFTIGEKYRP QQFGFMNESV KLNHADHRLI IYKDIHENIE DGITLLIVMA VVLVLLVIFG
     FISADNMAKR QTKDIETIIQ KIYYAKNRHL GTYTPLKNNS ELEEINNYIY DLFESNEQLI
     HSIEHTERRL RDIQLKEIER QFQPHFLFNT MQTIQYLITL SPKLAQTVVQ QLSQMLRYSL
     RTNSHTVELN EELNYIEQYV AIQNIRFDDM IKLHIESSEE ARHQTIGKMM LQPLIENAIK
     HGRDTESLDI TIRLTLARQN LHVLVCDNGI GMSSSRLQYV RQSLNNDVFD TKHLGLNHLH
     NKAMIQYGSH ARLHIFSKRN QGTLICYKIP LSRGNVDV