GRAS_STAHJ
ID GRAS_STAHJ Reviewed; 344 AA.
AC Q4L482;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 25-MAY-2022, entry version 125.
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=SH2234;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE05543.1; -; Genomic_DNA.
DR RefSeq; WP_011276494.1; NC_007168.1.
DR AlphaFoldDB; Q4L482; -.
DR SMR; Q4L482; -.
DR STRING; 279808.SH2234; -.
DR EnsemblBacteria; BAE05543; BAE05543; SH2234.
DR KEGG; sha:SH2234; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_13_1_9; -.
DR OMA; YEWLRIH; -.
DR OrthoDB; 1827824at2; -.
DR Proteomes; UP000000543; 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; Phosphoprotein; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system; Virulence.
FT CHAIN 1..344
FT /note="Sensor histidine kinase GraS"
FT /id="PRO_0000347929"
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"
FT MOD_RES 129
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 344 AA; 40436 MW; 1F9D47203BC85A65 CRC64;
MSNLKWFWLF LKTRSNWIFW IVFLHLILLG MAYIDYDISI ESIGFIVTLN LGLTAMFLIF
TFLKEVKLYQ HLYNNKEIEE IKHKDLAEDP FQKEVVNYLY RKLTSQKERV VEQQLHIQST
EQSLTEFVHD IKTPVTAMKL LIDQEEEGKR KKSLLYEWAR INELLDKQLY LTRLESKNRD
MYFEETSLKR LVIDEVQLTR HISQAKGIGY DLDLETNLDV YTDVKWCRMM IRQILSNSLK
YSQGQDIIIR SYTNDGHVTL EIKDFGRGIS HKDLPRIFER GFTSTVNRNE TTSSGIGLYL
VNSVKDQLGI NVRVESTVGQ GTTFVLTFPK QNELMARMTQ VTTM