CUSC_ECOLI
ID CUSC_ECOLI Reviewed; 457 AA.
AC P77211; Q9L5Y3; Q9X444;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cation efflux system protein CusC;
DE Flags: Precursor;
GN Name=cusC; Synonyms=ibeB, ylcB; OrderedLocusNames=b0572, JW0561;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K1 / RS218 / O18:K1:H7;
RX PubMed=10225861; DOI=10.1128/iai.67.5.2103-2109.1999;
RA Huang S.-H., Chen Y.-H., Fu Q., Stins M., Wang Y., Wass C., Kim K.S.;
RT "Identification and characterization of an Escherichia coli invasion gene
RT locus, ibeB, required for penetration of brain microvascular endothelial
RT cells.";
RL Infect. Immun. 67:2103-2109(1999).
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 1-340.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [8]
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 [9]
RP INDUCTION.
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 [10]
RP FUNCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=12813074; DOI=10.1128/jb.185.13.3804-3812.2003;
RA Franke S., Grass G., Rensing C., Nies D.H.;
RT "Molecular analysis of the copper-transporting efflux system CusCFBA of
RT Escherichia coli.";
RL J. Bacteriol. 185:3804-3812(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 18-457, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-18, AND DIACYLGLYCEROL AT
RP CYS-18.
RC STRAIN=K12 / DH5-alpha;
RX PubMed=21249122; DOI=10.1371/journal.pone.0015610;
RA Kulathila R., Kulathila R., Indic M., van den Berg B.;
RT "Crystal structure of Escherichia coli CusC, the outer membrane component
RT of a heavy metal efflux pump.";
RL PLoS ONE 6:E15610-E15610(2011).
CC -!- FUNCTION: Forms pores that allow passive diffusion of cations across
CC the outer membrane. Part of a cation efflux system that mediates
CC resistance to copper and silver. In pathogenic strains it allows the
CC bacteria to invade brain microvascular endothelial cells (BMEC) thus
CC allowing it to cross the blood-brain barrier and cause neonatal
CC meningitis. {ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:12813074,
CC ECO:0000269|PubMed:21249122}.
CC -!- SUBUNIT: Homotrimer. Component of the cus efflux system composed of
CC CusA, CusB, CusC and CusF. {ECO:0000269|PubMed:21249122}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:21249122}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21249122}. Cell outer membrane
CC {ECO:0000269|PubMed:21249122}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:21249122}.
CC -!- INDUCTION: Transcriptionally regulated by CusR in response to copper
CC and silver ions. {ECO:0000269|PubMed:11283292}.
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.
CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC family. {ECO:0000305}.
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DR EMBL; AF094824; AAD30205.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40770.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73673.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35206.1; -; Genomic_DNA.
DR EMBL; AF245661; AAF70174.1; -; Genomic_DNA.
DR PIR; B64790; B64790.
DR RefSeq; NP_415104.1; NC_000913.3.
DR RefSeq; WP_000074234.1; NZ_SSZK01000024.1.
DR PDB; 3PIK; X-ray; 2.30 A; A=18-457.
DR PDB; 4K34; X-ray; 2.69 A; A/B=18-457.
DR PDB; 4K7K; X-ray; 2.53 A; A/B=18-457.
DR PDB; 4K7R; X-ray; 2.09 A; A=18-457.
DR PDBsum; 3PIK; -.
DR PDBsum; 4K34; -.
DR PDBsum; 4K7K; -.
DR PDBsum; 4K7R; -.
DR AlphaFoldDB; P77211; -.
DR SMR; P77211; -.
DR BioGRID; 4262822; 262.
DR ComplexPortal; CPX-2254; Cus cation efflux complex.
DR DIP; DIP-9347N; -.
DR IntAct; P77211; 1.
DR STRING; 511145.b0572; -.
DR TCDB; 1.B.17.3.5; the outer membrane factor (omf) family.
DR jPOST; P77211; -.
DR PaxDb; P77211; -.
DR PRIDE; P77211; -.
DR EnsemblBacteria; AAC73673; AAC73673; b0572.
DR EnsemblBacteria; BAA35206; BAA35206; BAA35206.
DR GeneID; 946288; -.
DR KEGG; ecj:JW0561; -.
DR KEGG; eco:b0572; -.
DR PATRIC; fig|1411691.4.peg.1702; -.
DR EchoBASE; EB3984; -.
DR eggNOG; COG1538; Bacteria.
DR HOGENOM; CLU_012817_13_3_6; -.
DR InParanoid; P77211; -.
DR OMA; AANQDYY; -.
DR PhylomeDB; P77211; -.
DR BioCyc; EcoCyc:G6320-MON; -.
DR BioCyc; MetaCyc:G6320-MON; -.
DR EvolutionaryTrace; P77211; -.
DR PRO; PR:P77211; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0019992; F:diacylglycerol binding; IDA:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0060003; P:copper ion export; IEP:EcoCyc.
DR GO; GO:0035434; P:copper ion transmembrane transport; IC:ComplexPortal.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0046688; P:response to copper ion; IMP:EcoliWiki.
DR GO; GO:0010272; P:response to silver ion; IMP:EcoCyc.
DR GO; GO:0009636; P:response to toxic substance; IC:ComplexPortal.
DR GO; GO:1902601; P:silver ion transmembrane transport; IC:ComplexPortal.
DR InterPro; IPR003423; OMP_efflux.
DR InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT.
DR Pfam; PF02321; OEP; 2.
DR TIGRFAMs; TIGR01845; outer_NodT; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Ion transport; Lipoprotein; Membrane;
KW Palmitate; Porin; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..457
FT /note="Cation efflux system protein CusC"
FT /id="PRO_0000030992"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:21249122"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:21249122"
FT VARIANT 6
FT /note="L -> I (in strain: K1 / RS218)"
FT VARIANT 20
FT /note="L -> M (in strain: K1 / RS218)"
FT VARIANT 27
FT /note="P -> S (in strain: K1 / RS218)"
FT VARIANT 33
FT /note="Q -> H (in strain: K1 / RS218)"
FT VARIANT 50..51
FT /note="QN -> RS (in strain: K1 / RS218)"
FT VARIANT 81
FT /note="T -> A (in strain: K1 / RS218)"
FT VARIANT 102
FT /note="L -> F (in strain: K1 / RS218)"
FT VARIANT 106
FT /note="G -> D (in strain: K1 / RS218)"
FT VARIANT 117..118
FT /note="NT -> DS (in strain: K1 / RS218)"
FT VARIANT 167
FT /note="S -> F (in strain: K1 / RS218)"
FT VARIANT 191
FT /note="R -> G (in strain: K1 / RS218)"
FT VARIANT 232
FT /note="Q -> R (in strain: K1 / RS218)"
FT VARIANT 273
FT /note="S -> P (in strain: K1 / RS218)"
FT VARIANT 457
FT /note="G -> GWQQ (in strain: K1 / RS218)"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 75..96
FT /evidence="ECO:0007829|PDB:4K7R"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:4K7R"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:4K7R"
FT STRAND 121..133
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 139..204
FT /evidence="ECO:0007829|PDB:4K7R"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 211..246
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 281..302
FT /evidence="ECO:0007829|PDB:4K7R"
FT STRAND 307..320
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:4K7R"
FT STRAND 330..339
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 347..413
FT /evidence="ECO:0007829|PDB:4K7R"
FT HELIX 419..453
FT /evidence="ECO:0007829|PDB:4K7R"
SQ SEQUENCE 457 AA; 50270 MW; B85B2B6B6719F7A1 CRC64;
MSPCKLLPFC VALALTGCSL APDYQRPAMP VPQQFSLSQN GLVNAADNYQ NAGWRTFFVD
NQVKTLISEA LVNNRDLRMA TLKVQEARAQ YRLTDADRYP QLNGEGSGSW SGNLKGNTAT
TREFSTGLNA SFDLDFFGRL KNMSEAERQN YLATEEAQRA VHILLVSNVA QSYFNQQLAY
AQLQIAEETL RNYQQSYAFV EKQLLTGSSN VLALEQARGV IESTRSDIAK RQGELAQANN
ALQLLLGSYG KLPQAQTVNS DSLQSVKLPA GLSSQILLQR PDIMEAEHAL MAANANIGAA
RAAFFPSISL TSGISTASSD LSSLFNASSG MWNFIPKIEI PIFNAGRNQA NLDIAEIRQQ
QSVVNYEQKI QNAFKEVADA LALRQSLNDQ ISAQQRYLAS LQITLQRARA LYQHGAVSYL
EVLDAERSLF ATRQTLLDLN YARQVNEISL YTALGGG
