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SILS_SALTM
ID   SILS_SALTM              Reviewed;         497 AA.
AC   Q9ZHD4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Probable sensor kinase SilS;
DE            EC=2.7.13.3;
GN   Name=silS;
OS   Salmonella typhimurium.
OG   Plasmid pMG101.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9930866; DOI=10.1038/5545;
RA   Gupta A., Matsui K., Lo J.-F., Silver S.;
RT   "Molecular basis for resistance to silver cations in Salmonella.";
RL   Nat. Med. 5:183-188(1999).
CC   -!- FUNCTION: Component of the sil cation-efflux system that confers
CC       resistance to silver. Probable member of a two-component regulatory
CC       system SilS/SilR. May activate SilR by phosphorylation.
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 inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
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DR   EMBL; AF067954; AAD11744.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZHD4; -.
DR   SMR; Q9ZHD4; -.
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   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR006290; CztS_silS_copS.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR01386; cztS_silS_copS; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Plasmid; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..497
FT                   /note="Probable sensor kinase SilS"
FT                   /id="PRO_0000074878"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..186
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..497
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          208..261
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          269..487
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         272
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   497 AA;  56247 MW;  C5F19D6DC11A0D96 CRC64;
     MHSKPSRLPF SLALRLTFFI SLSTILAFIA FTWFMLHSVE KHFAEQDVSD LQQISTTLSR
     ILQSPADPDE KKVSKIKESI ASYRNVALLL LNPRGEVLYS SAQGAALRPA VNSADFSEHS
     RARDVFLWTV EDTARAMDTG SGMKMETYRI IASSGQATFQ GKQQNYVMLT GLSINFHLHY
     LDALKKNLIA IAVVISLLIV LIIRIAVRQG HLPLRNVSNA IKNITSENLD ARLEPTRVPI
     ELEQLVISFN HMIGKIEDVF TRQANFSADI AHEIRTPITN LVTQTEIALS QDRTQKELED
     VLYSSLEEYN RMTKMVSDML FLAQADNNQL IPDRVRFDLQ SQNSLKVFRV FSEALGPKET
     PILLLKFNGM PCLVEGDPQM FRRAINNLLS NALRYTPEGQ AITVSIREQE SFFDLVIENP
     GKPIPEEHLS RLFDRFYRVD PSRQRKGEGS GIGLAIVKSI VEAHHGRVQV ESDVHSTRFI
     LSVPRLEKMI PDTQCWE
 
 
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