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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
 
 
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