ID   GRAS_STAES              Reviewed;         346 AA.
AC   Q8CTL4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=SE_0428;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Member of the two-component regulatory system GraR/GraS
CC       involved in resistance against cationic antimicrobial peptides (CAMPs).
CC       GraS probably functions as a sensor protein kinase which is
CC       autophosphorylated at a histidine residue and transfers its phosphate
CC       group to GraR (By similarity). {ECO:0000250}.
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; AE015929; AAO04025.1; -; Genomic_DNA.
DR   RefSeq; NP_763983.1; NC_004461.1.
DR   RefSeq; WP_002438833.1; NZ_WBME01000020.1.
DR   AlphaFoldDB; Q8CTL4; -.
DR   SMR; Q8CTL4; -.
DR   STRING; 176280.SE_0428; -.
DR   EnsemblBacteria; AAO04025; AAO04025; SE_0428.
DR   GeneID; 50019416; -.
DR   KEGG; sep:SE_0428; -.
DR   PATRIC; fig|176280.10.peg.402; -.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_13_1_9; -.
DR   OMA; YEWLRIH; -.
DR   Proteomes; UP000001411; 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:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
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; 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; 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; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system; Virulence.
FT   CHAIN           1..346
FT                   /note="Sensor histidine kinase GraS"
FT                   /id="PRO_0000347927"
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"
FT   MOD_RES         129
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   346 AA;  41149 MW;  3437C6652E01F4AD CRC64;
     MNNFRWFWFF IKSRINWILW ILFLNIILLG VAYIDYEISV ESVFYIVILN VGLSILFLLF
     TFVKEVRLSK HFYEDKEIEE IKHKDLAETP FQQQVIDYLY RHIAAQKEKV VEQQLQIKNH
     EQTITEFVHD IKTPVTAMKL LIDQENDDQR KRALLFEWSR INEMLDKQLY LTRLETHHRD
     MYFDYISLKR MVIDEIQVTR HISQAKGIGF ELDFKDEQKV YTDVKWCRMM IRQVLSNSLK
     YSDNSTINLS GYNIEGHVVL KIKDYGRGIS KRDLPRIFDR GFTSTTDRND TASSGMGLYL
     VQSVKEQLGI EVKVDSIVGK GTTFYFIFPQ QNEIIERMSK VTRLSF