ID   CUSS_ECOL6              Reviewed;         480 AA.
AC   Q8FK37;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Sensor histidine kinase CusS {ECO:0000250|UniProtKB:P77485};
DE            EC=2.7.13.3 {ECO:0000250|UniProtKB:P77485};
GN   Name=cusS; OrderedLocusNames=c0656;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Member of the two-component regulatory system CusS/CusR
CC       involved in response to copper and silver. Acts as a copper/silver ion
CC       sensor. Activates CusR by phosphorylation.
CC       {ECO:0000250|UniProtKB:P77485}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P77485};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P77485}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P77485}.
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DR   EMBL; AE014075; AAN79131.1; -; Genomic_DNA.
DR   RefSeq; WP_000253820.1; NC_004431.1.
DR   AlphaFoldDB; Q8FK37; -.
DR   SMR; Q8FK37; -.
DR   STRING; 199310.c0656; -.
DR   EnsemblBacteria; AAN79131; AAN79131; c0656.
DR   KEGG; ecc:c0656; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_6; -.
DR   OMA; MPAQQNE; -.
DR   BioCyc; ECOL199310:C0656-MON; -.
DR   BRENDA; 2.7.13.3; 2026.
DR   Proteomes; UP000001410; 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   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; Copper; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix; Two-component regulatory system.
FT   CHAIN           1..480
FT                   /note="Sensor histidine kinase CusS"
FT                   /id="PRO_0000074725"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P77485"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..186
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P77485"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..480
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P77485"
FT   DOMAIN          207..260
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          268..480
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         271
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   480 AA;  53776 MW;  34C2DA8ABA38F16E CRC64;
     MVSKPFQRPF SLATRLTFFI SLATIAAFFA FAWIMIHSVK VHFAEQDIND LKEISATLER
     VLNHPDETQA RRLMTLEDIV SGYSNVLISL ADSHGKTVYH SPGAPDIREF TRDAIPDKDA
     QGGEVYLLSG PTMMMPGHGH GHMEHSNWRM INLPVGPLVD GKPIYTLYIA LSIDFHLHYI
     NDLMNKLIMT ASVISILIVF IVLLAVHKGH APIRSVSRQI QNITSKDLDV RLDPQTVPIE
     LEQLVLSFNH MIERIEDVFT RQSNFSADIA HEIRTPITNL ITQTEIALSQ SRSQKELEDV
     LYSNLEELTR MAKMVSDMLF LAQADNNQLI PEKKMLNLAD EVGKVFDFFE ALAEDRGVEL
     RFVGDECQVA GDPLMLRRAL SNLLSNALRY TPTGETIVVR CQTVDHLVQV TVENPGTPIA
     PEHLPRLFDR FYRVDPSRQR KGEGSGIGLA IVKSIVVAHK GTVAVTSDVR GTRFVIILPA