CUSR_ECOLI
ID CUSR_ECOLI Reviewed; 227 AA.
AC P0ACZ8; P77380;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transcriptional regulatory protein CusR {ECO:0000305};
GN Name=cusR; Synonyms=ylcA; OrderedLocusNames=b0571, JW0560;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-94.
RC STRAIN=HVC45;
RA Morel-Deville F., Ehrlich S.D., Morel P.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION.
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 [10]
RP FUNCTION, AND 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 [11]
RP FUNCTION, AND 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. Activates the expression of
CC cusCFBA, hiuH and plasmid pRJ1004 gene pcoE in response to increasing
CC levels of copper or silver ions. Can also increase the basal-level
CC expression of copper resistance gene operon pcoABCD.
CC {ECO:0000269|PubMed:11004187, ECO:0000269|PubMed:11283292,
CC ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:25568260,
CC ECO:0000269|PubMed:27983483}.
CC -!- INTERACTION:
CC P0ACZ8; P0ACZ8: cusR; NbExp=2; IntAct=EBI-1118807, EBI-1118807;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by CusS. {ECO:0000269|PubMed:15522865}.
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 (PubMed:25568260, PubMed:27983483). Under low
CC protein concentrations, the two regulators recognize and transcribe
CC both hiuH and cusC promoters, albeit at different efficiency,
CC apparently in a collaborative fashion (PubMed:27983483).
CC {ECO:0000269|PubMed:25568260, ECO:0000269|PubMed:27983483}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF245661; AAF70175.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40769.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73672.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35205.1; -; Genomic_DNA.
DR EMBL; U82579; AAB41754.1; -; Genomic_DNA.
DR PIR; A64790; A64790.
DR RefSeq; NP_415103.1; NC_000913.3.
DR RefSeq; WP_000770953.1; NZ_SSZK01000024.1.
DR AlphaFoldDB; P0ACZ8; -.
DR SMR; P0ACZ8; -.
DR BioGRID; 4259891; 18.
DR BioGRID; 849397; 2.
DR DIP; DIP-9348N; -.
DR IntAct; P0ACZ8; 9.
DR STRING; 511145.b0571; -.
DR jPOST; P0ACZ8; -.
DR PaxDb; P0ACZ8; -.
DR PRIDE; P0ACZ8; -.
DR EnsemblBacteria; AAC73672; AAC73672; b0571.
DR EnsemblBacteria; BAA35205; BAA35205; BAA35205.
DR GeneID; 58463696; -.
DR GeneID; 945003; -.
DR KEGG; ecj:JW0560; -.
DR KEGG; eco:b0571; -.
DR PATRIC; fig|1411691.4.peg.1703; -.
DR EchoBASE; EB3612; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_1_6; -.
DR InParanoid; P0ACZ8; -.
DR OMA; EFSILWV; -.
DR PhylomeDB; P0ACZ8; -.
DR BioCyc; EcoCyc:G6319-MON; -.
DR PRO; PR:P0ACZ8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IDA:EcoCyc.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0046688; P:response to copper ion; IDA:EcoCyc.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR006291; PcoR.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR TIGRFAMs; TIGR01387; cztR_silR_copR; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Copper; Cytoplasm; DNA-binding; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..227
FT /note="Transcriptional regulatory protein CusR"
FT /id="PRO_0000081063"
FT DOMAIN 2..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 125..223
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 227 AA; 25395 MW; 5CE129597FAE43C0 CRC64;
MKLLIVEDEK KTGEYLTKGL TEAGFVVDLA DNGLNGYHLA MTGDYDLIIL DIMLPDVNGW
DIVRMLRSAN KGMPILLLTA LGTIEHRVKG LELGADDYLV KPFAFAELLA RVRTLLRRGA
AVIIESQFQV ADLMVDLVSR KVTRSGTRIT LTSKEFTLLE FFLRHQGEVL PRSLIASQVW
DMNFDSDTNA IDVAVKRLRG KIDNDFEPKL IQTVRGVGYM LEVPDGQ
