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 03-AUG-2022, entry version 128.
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=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., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT 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 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; 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_SWKA01000005.1.
DR AlphaFoldDB; Q8XBY4; -.
DR SMR; Q8XBY4; -.
DR STRING; 155864.EDL933_0633; -.
DR EnsemblBacteria; AAG54903; AAG54903; Z0708.
DR EnsemblBacteria; BAB34031; BAB34031; ECs_0608.
DR GeneID; 916966; -.
DR KEGG; ece:Z0708; -.
DR KEGG; ecs:ECs_0608; -.
DR PATRIC; fig|386585.9.peg.716; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_6; -.
DR OMA; MPAQQNE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..482
FT /note="Sensor histidine kinase CusS"
FT /id="PRO_0000074726"
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..482
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..482
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 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
