ID   GRAS_STAAB              Reviewed;         346 AA.
AC   Q2YSS1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=SAB0609;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80297.1; -; Genomic_DNA.
DR   RefSeq; WP_001061258.1; NC_007622.1.
DR   AlphaFoldDB; Q2YSS1; -.
DR   SMR; Q2YSS1; -.
DR   KEGG; sab:SAB0609; -.
DR   HOGENOM; CLU_000445_13_1_9; -.
DR   OMA; YEWLRIH; -.
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_0000347913"
FT   TRANSMEM        15..35
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;  41079 MW;  56AA42F0635AADA8 CRC64;
     MNNLKWVAYF LKSRMNWIFW ILFLNLLMLG ISLIDYDFPI DSLFYIVSLN LSLTMIFLIL
     TYFKEVKLYK HFDKDKEIEE IKHKDFAETP FQRHTVDYLY RQISAHKEKV VEQQLQLNMH
     EQTITEFVHD IKTPVTAMKL LIDQEKNQER KQALLYEWSR INSMLDTQLY ITRLESQRKD
     MYFDYVSLKR MVIDEIQLTR HISQVKGIGF DVDFKVDDYV YTDIKWCRMI IRQILSNALK
     YSENFNIEIG TELNDQHVSL YIKDYGRGIS KKDMPRIFER GFTSTANRNE TTSSGMGLYL
     VNSVKDQLGI HLQVTSTVGK GTTVRLIFPL QNEIVERMSE VTNLSF