(data stored in ACNUC7421 zone)

SWISSPROT: CUSS_ECO57

ID   CUSS_ECO57              Reviewed;         482 AA.
AC   Q8XBY4;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 109.
DE   RecName: Full=Sensor kinase CusS;
DE            EC=2.7.13.3;
GN   Name=cusS; OrderedLocusNames=Z0708, ECs0608;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system CusS/CusR.
CC       Copper ion sensor. Could also be a silver ion sensor. Activates
CC       CusR by phosphorylation (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250}.
DR   EMBL; AE005174; AAG54903.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34031.1; -; Genomic_DNA.
DR   PIR; C85555; C85555.
DR   PIR; H90704; H90704.
DR   RefSeq; NP_308635.1; NC_002695.1.
DR   RefSeq; WP_000253799.1; NZ_MWVM01000011.1.
DR   ProteinModelPortal; Q8XBY4; -.
DR   SMR; Q8XBY4; -.
DR   STRING; 155864.Z0708; -.
DR   EnsemblBacteria; AAG54903; AAG54903; Z0708.
DR   EnsemblBacteria; BAB34031; BAB34031; BAB34031.
DR   GeneID; 916966; -.
DR   KEGG; ece:Z0708; -.
DR   KEGG; ecs:ECs0608; -.
DR   PATRIC; fig|386585.9.peg.716; -.
DR   eggNOG; ENOG4105GR3; Bacteria.
DR   eggNOG; COG0642; LUCA.
DR   HOGENOM; HOG000126763; -.
DR   KO; K07644; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
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; cd06225; HAMP; 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; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
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;
DR   PRODOM; Q8XBY4.
DR   SWISS-2DPAGE; Q8XBY4.
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Copper; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN         1    482       Sensor kinase CusS.
FT                                /FTId=PRO_0000074726.
FT   TOPO_DOM      1     15       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     16     36       Helical. {ECO:0000255}.
FT   TOPO_DOM     37    186       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    187    207       Helical. {ECO:0000255}.
FT   TOPO_DOM    208    482       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      207    260       HAMP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00102}.
FT   DOMAIN      268    482       Histidine kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00107}.
FT   MOD_RES     271    271       Phosphohistidine; by autocatalysis.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00107}.
SQ   SEQUENCE   482 AA;  53909 MW;  E2AB98ACE676DA71 CRC64;
     MVSKPFQRPF SLATRLTFFI SLATIAAFFA FAWIMIHSVK VHFAEQDIND LKEISATLER
     VLNHPDETQA RRLMTLEDIV SGYSNVLISL ADSHGKTVYH SPGAPDIREF ARDAIPDKDA
     RGGEVFLLSG PTMMMPGHGH GHMEHSNWRM ISLPVGPLVD GKPIYTLYIA LSIDFHLHYI
     NDLMNKLIMT ASVISILIVF IVLLAVHKGH APIRSVSRQI QNITSKDLDV RLDPQTVPIE
     LEQLVLSFNH MIERIEDVFT RQSNFSADIA HEIRTPITNL ITQTEIALSQ SRSQKELEDV
     LYSNLEELTR MAKMVSDMLF LAQADNNQLI PEKKMLNLAD EVGKVFDFFE ALAEDRGVEL
     QFVGDECQVA GDPLMLRRAL SNLLSNALRY TPPGEAIVVR CQTVDHLVQV IVENPGTPIA
     PEHLPRLFDR FYRVDPSRQR KGEGSGIGLA IVKSIVVAHK GTVAVTSNAR GTRFVIVLPE
     RG
//

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