ID   GRAS_STAAC              Reviewed;         346 AA.
AC   Q5HI08;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Sensor histidine kinase GraS;
DE            EC=2.7.13.3;
DE   AltName: Full=Glycopeptide resistance-associated protein S;
GN   Name=graS; OrderedLocusNames=SACOL0717;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
RN   [2]
RP   FUNCTION IN CATIONIC ANTIMICROBIAL PEPTIDE RESISTANCE.
RX   PubMed=17502406; DOI=10.1128/aac.00209-07;
RA   Meehl M., Herbert S., Goetz F., Cheung A.;
RT   "Interaction of the graRS two-component system with the vraFG ABC
RT   transporter to support vancomycin-intermediate resistance in Staphylococcus
RT   aureus.";
RL   Antimicrob. Agents Chemother. 51:2679-2689(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; CP000046; AAW37781.1; -; Genomic_DNA.
DR   RefSeq; WP_001061252.1; NC_002951.2.
DR   AlphaFoldDB; Q5HI08; -.
DR   SMR; Q5HI08; -.
DR   EnsemblBacteria; AAW37781; AAW37781; SACOL0717.
DR   KEGG; sac:SACOL0717; -.
DR   HOGENOM; CLU_000445_13_1_9; -.
DR   OMA; YEWLRIH; -.
DR   Proteomes; UP000000530; 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   1: Evidence at protein level;
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 histidine kinase GraS"
FT                   /id="PRO_0000347914"
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;  50820220FB5FDEAF CRC64;
     MNNLKWVAYF LKSRMNWIFW ILFLNFLMLG ISLIDYDFPI DSLFYIVSLN LSLTMIFLLL
     TYFKEVKLYK HFDKDKEIEE IKHKDLAETP 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