CUSS_ECOLI
ID CUSS_ECOLI Reviewed; 480 AA.
AC P77485; Q9R7T9; Q9R7U0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Sensor histidine kinase CusS {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000305|PubMed:15522865};
GN Name=cusS; Synonyms=ybcZ; OrderedLocusNames=b0570, JW5082;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=11004187; DOI=10.1128/jb.182.20.5864-5871.2000;
RA Munson G.P., Lam D.L., Outten F.W., O'Halloran T.V.;
RT "Identification of a copper-responsive two-component system on the
RT chromosome of Escherichia coli K-12.";
RL J. Bacteriol. 182:5864-5871(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION IN COPPER HOMEOSTASIS.
RC STRAIN=K12;
RX PubMed=11399769; DOI=10.1074/jbc.m104122200;
RA Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V.;
RT "The independent cue and cus systems confer copper tolerance during aerobic
RT and anaerobic growth in Escherichia coli.";
RL J. Biol. Chem. 276:30670-30677(2001).
RN [7]
RP PROBABLE FUNCTION IN SILVER HOMEOSTASIS.
RC STRAIN=K38;
RX PubMed=11283292; DOI=10.1099/00221287-147-4-965;
RA Franke S., Grass G., Nies D.H.;
RT "The product of the ybdE gene of the Escherichia coli chromosome is
RT involved in detoxification of silver ions.";
RL Microbiology 147:965-972(2001).
RN [8]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15522865; DOI=10.1074/jbc.m410104200;
RA Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.;
RT "Functional characterization in vitro of all two-component signal
RT transduction systems from Escherichia coli.";
RL J. Biol. Chem. 280:1448-1456(2005).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22348296; DOI=10.1111/j.1574-6968.2012.02529.x;
RA Gudipaty S.A., Larsen A.S., Rensing C., McEvoy M.M.;
RT "Regulation of Cu(I)/Ag(I) efflux genes in Escherichia coli by the sensor
RT kinase CusS.";
RL FEMS Microbiol. Lett. 330:30-37(2012).
RN [11]
RP INTERPLAY BETWEEN HPRSR AND CUSSR.
RX PubMed=25568260; DOI=10.1099/mic.0.000026;
RA Urano H., Umezawa Y., Yamamoto K., Ishihama A., Ogasawara H.;
RT "Cooperative regulation of the common target genes between H(2)O(2)-sensing
RT YedVW and Cu2+-sensing CusSR in Escherichia coli.";
RL Microbiology 161:729-738(2015).
RN [12]
RP INTERPLAY BETWEEN HPRSR AND CUSSR.
RX PubMed=27983483; DOI=10.1099/mic.0.000410;
RA Urano H., Yoshida M., Ogawa A., Yamamoto K., Ishihama A., Ogasawara H.;
RT "Cross-regulation between two common ancestral response regulators, HprR
RT and CusR, in Escherichia coli.";
RL Microbiology 163:243-252(2017).
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:0000269|PubMed:11004187, ECO:0000269|PubMed:11283292,
CC ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:15522865,
CC ECO:0000269|PubMed:22348296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000305|PubMed:15522865};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15522865}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant has higher susceptibility to
CC silver and shows an increase in copper accumulation.
CC {ECO:0000269|PubMed:22348296}.
CC -!- MISCELLANEOUS: The cus system plays an important role in copper
CC tolerance under anaerobic growth and, under extreme copper stress, in
CC aerobic growth. {ECO:0000269|PubMed:11399769}.
CC -!- MISCELLANEOUS: HprSR and CusSR form a unique regulation system, where
CC both two-component systems recognize and regulate the same set of
CC genes, but under different environmental conditions. HprSR plays a role
CC in H(2)O(2) response regulation, while CusSR plays a role in Cu(2+)
CC response regulation. {ECO:0000269|PubMed:25568260,
CC ECO:0000269|PubMed:27983483}.
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DR EMBL; AF245661; AAF70176.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40768.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73671.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35204.2; -; Genomic_DNA.
DR PIR; H64789; H64789.
DR RefSeq; NP_415102.1; NC_000913.3.
DR RefSeq; WP_000253839.1; NZ_SSZK01000024.1.
DR PDB; 5KU5; X-ray; 2.15 A; A/B/C/D=39-187.
DR PDBsum; 5KU5; -.
DR AlphaFoldDB; P77485; -.
DR SMR; P77485; -.
DR BioGRID; 4259499; 18.
DR BioGRID; 850340; 1.
DR DIP; DIP-9349N; -.
DR IntAct; P77485; 2.
DR STRING; 511145.b0570; -.
DR PaxDb; P77485; -.
DR PRIDE; P77485; -.
DR EnsemblBacteria; AAC73671; AAC73671; b0570.
DR EnsemblBacteria; BAA35204; BAA35204; BAA35204.
DR GeneID; 945978; -.
DR KEGG; ecj:JW5082; -.
DR KEGG; eco:b0570; -.
DR PATRIC; fig|1411691.4.peg.1704; -.
DR EchoBASE; EB3406; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_6_6; -.
DR InParanoid; P77485; -.
DR OMA; MPAQQNE; -.
DR PhylomeDB; P77485; -.
DR BioCyc; EcoCyc:G6318-MON; -.
DR BioCyc; MetaCyc:G6318-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P77485; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; TAS:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IPI:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoliWiki.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0071280; P:cellular response to copper ion; IMP:EcoCyc.
DR GO; GO:0071292; P:cellular response to silver ion; IDA:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IDA:EcoliWiki.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Copper;
KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..480
FT /note="Sensor histidine kinase CusS"
FT /id="PRO_0000074724"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..186
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
FT DOMAIN 208..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"
FT HELIX 39..62
FT /evidence="ECO:0007829|PDB:5KU5"
FT HELIX 69..81
FT /evidence="ECO:0007829|PDB:5KU5"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:5KU5"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:5KU5"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:5KU5"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5KU5"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5KU5"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:5KU5"
FT STRAND 162..172
FT /evidence="ECO:0007829|PDB:5KU5"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:5KU5"
SQ SEQUENCE 480 AA; 53738 MW; B3D78C0810241519 CRC64;
MVSKPFQRPF SLATRLTFFI SLATIAAFFA FAWIMIHSVK VHFAEQDIND LKEISATLER
VLNHPDETQA RRLMTLEDIV SGYSNVLISL ADSQGKTVYH 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
RFVGDKCQVA GDPLMLRRAL SNLLSNALRY TPTGETIVVR CQTVDHLVQV IVENPGTPIA
PEHLPRLFDR FYRVDPSRQR KGEGSGIGLA IVKSIVVAHK GTVAVTSDAR GTRFVITLPA
