ID   GRAS_STAAR              Reviewed;         346 AA.
AC   Q6GJ10;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Sensor protein kinase GraS;
DE            EC=2.7.13.3;
DE   AltName: Full=Glycopeptide resistance-associated protein S;
GN   Name=graS; OrderedLocusNames=SAR0670;
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 GraR/GraS
CC       involved in resistance against cationic antimicrobial peptides (CAMPs).
CC       Functions as a sensor protein kinase which phosphorylates GraR through
CC       the auxiliary protein GraX. In turn, GraR up-regulates many genes such
CC       as adhesins, exoproteins, transporters, toxins, and proteins involved
CC       in cell wall synthesis. Down-regulates the expression of many genes
CC       involved in RNA and amino acid synthesis or glycolysis.
CC       {ECO:0000250|UniProtKB:Q2G0D9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBUNIT: Interacts with GraX. {ECO:0000250|UniProtKB:Q2G0D9}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; BX571856; CAG39687.1; -; Genomic_DNA.
DR   RefSeq; WP_001061270.1; NC_002952.2.
DR   AlphaFoldDB; Q6GJ10; -.
DR   SMR; Q6GJ10; -.
DR   KEGG; sar:SAR0670; -.
DR   HOGENOM; CLU_000445_13_1_9; -.
DR   OMA; YEWLRIH; -.
DR   OrthoDB; 1827824at2; -.
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   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; ATP-binding; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system; Virulence.
FT   CHAIN           1..346
FT                   /note="Sensor protein kinase GraS"
FT                   /id="PRO_0000347917"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          126..332
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   346 AA;  40934 MW;  30B3250B54708E53 CRC64;
     MNNLKWVVYF LKSRKNWIFW ILFLNILMLG ISLIDYDFPI DSLFYIVSLN LSLTLIFLIL
     TFFKEVKLYR HFEKDKEIEE IKHKDLAETP FQRHTVDYLY RQILAHKDKV VDQQLQLNMH
     EQTITEFVHD IKTPVTAMKL LIDQEENQER KQALLFEWSR INSMLDTQLY ITRLESQRKD
     MFFDYVSLKR MVIDEIQLTR HISQVKGIGF DIDFKVDNHV YTDIKWCRMI IRQILSNALK
     YSENYNVDIS TELIDQHVAL IIKDHGRGIS KKDMPRIFER GFTSTANRNE TTSSGMGLYL
     VDSVKDQLGI QLQVTSTIGK GTTVKLIFPL QNEIVERMSE VTNLSF