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Cation efflux system protein CusC

 CUSC_ECOLI              Reviewed;         457 AA.
P77211; Q9L5Y3; Q9X444;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
28-MAR-2018, entry version 136.
RecName: Full=Cation efflux system protein CusC;
Flags: Precursor;
Name=cusC; Synonyms=ibeB, ylcB; OrderedLocusNames=b0572, JW0561;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K1 / RS218 / O18:K1:H7;
PubMed=10225861;
Huang S.-H., Chen Y.-H., Fu Q., Stins M., Wang Y., Wass C., Kim K.S.;
"Identification and characterization of an Escherichia coli invasion
gene locus, ibeB, required for penetration of brain microvascular
endothelial cells.";
Infect. Immun. 67:2103-2109(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-340.
STRAIN=K12 / DH5-alpha;
PubMed=11004187; DOI=10.1128/JB.182.20.5864-5871.2000;
Munson G.P., Lam D.L., Outten F.W., O'Halloran T.V.;
"Identification of a copper-responsive two-component system on the
chromosome of Escherichia coli K-12.";
J. Bacteriol. 182:5864-5871(2000).
[7]
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=B / BL21;
PubMed=10493123;
DOI=10.1002/(SICI)1522-2683(19990801)20:11<2181::AID-ELPS2181>3.0.CO;2-Q;
Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
"Enrichment of low abundance proteins of Escherichia coli by
hydroxyapatite chromatography.";
Electrophoresis 20:2181-2195(1999).
[8]
FUNCTION IN COPPER HOMEOSTASIS.
STRAIN=K12;
PubMed=11399769; DOI=10.1074/jbc.M104122200;
Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V.;
"The independent cue and cus systems confer copper tolerance during
aerobic and anaerobic growth in Escherichia coli.";
J. Biol. Chem. 276:30670-30677(2001).
[9]
INDUCTION.
STRAIN=K38;
PubMed=11283292;
Franke S., Grass G., Nies D.H.;
"The product of the ybdE gene of the Escherichia coli chromosome is
involved in detoxification of silver ions.";
Microbiology 147:965-972(2001).
[10]
FUNCTION.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=12813074; DOI=10.1128/JB.185.13.3804-3812.2003;
Franke S., Grass G., Rensing C., Nies D.H.;
"Molecular analysis of the copper-transporting efflux system CusCFBA
of Escherichia coli.";
J. Bacteriol. 185:3804-3812(2003).
[11]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 18-457, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-18, AND DIACYLGLYCEROL AT
CYS-18.
STRAIN=K12 / DH5-alpha;
PubMed=21249122; DOI=10.1371/journal.pone.0015610;
Kulathila R., Kulathila R., Indic M., van den Berg B.;
"Crystal structure of Escherichia coli CusC, the outer membrane
component of a heavy metal efflux pump.";
PLoS ONE 6:E15610-E15610(2011).
-!- FUNCTION: Forms pores that allow passive diffusion of cations
across the outer membrane. Part of a cation efflux system that
mediates resistance to copper and silver. In pathogenic strains it
allows the bacteria to invade brain microvascular endothelial
cells (BMEC) thus allowing it to cross the blood-brain barrier and
cause neonatal meningitis. {ECO:0000269|PubMed:11399769,
ECO:0000269|PubMed:12813074, ECO:0000269|PubMed:21249122}.
-!- SUBUNIT: Homotrimer. Component of the cus efflux system composed
of CusA, CusB, CusC and CusF. {ECO:0000269|PubMed:21249122}.
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000269|PubMed:21249122}; Multi-pass membrane protein
{ECO:0000269|PubMed:21249122}. Cell outer membrane
{ECO:0000269|PubMed:21249122}; Lipid-anchor {ECO:0000255|PROSITE-
ProRule:PRU00303, ECO:0000269|PubMed:21249122}.
-!- INDUCTION: Transcriptionally regulated by CusR in response to
copper and silver ions. {ECO:0000269|PubMed:11283292}.
-!- MISCELLANEOUS: The cus system plays an important role in copper
tolerance under anaerobic growth and, under extreme copper stress,
in aerobic growth.
-!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF094824; AAD30205.1; -; Genomic_DNA.
EMBL; U82598; AAB40770.1; -; Genomic_DNA.
EMBL; U00096; AAC73673.1; -; Genomic_DNA.
EMBL; AP009048; BAA35206.1; -; Genomic_DNA.
EMBL; AF245661; AAF70174.1; -; Genomic_DNA.
PIR; B64790; B64790.
RefSeq; NP_415104.1; NC_000913.3.
RefSeq; WP_000074234.1; NZ_LN832404.1.
PDB; 3PIK; X-ray; 2.30 A; A=18-457.
PDB; 4K34; X-ray; 2.69 A; A/B=18-457.
PDB; 4K7K; X-ray; 2.53 A; A/B=18-457.
PDB; 4K7R; X-ray; 2.09 A; A=18-457.
PDBsum; 3PIK; -.
PDBsum; 4K34; -.
PDBsum; 4K7K; -.
PDBsum; 4K7R; -.
ProteinModelPortal; P77211; -.
SMR; P77211; -.
BioGrid; 4262822; 262.
DIP; DIP-9347N; -.
STRING; 316385.ECDH10B_0638; -.
TCDB; 1.B.17.3.5; the outer membrane factor (omf) family.
PaxDb; P77211; -.
PRIDE; P77211; -.
EnsemblBacteria; AAC73673; AAC73673; b0572.
EnsemblBacteria; BAA35206; BAA35206; BAA35206.
GeneID; 946288; -.
KEGG; ecj:JW0561; -.
KEGG; eco:b0572; -.
PATRIC; fig|1411691.4.peg.1702; -.
EchoBASE; EB3984; -.
EcoGene; EG14233; cusC.
eggNOG; ENOG4105ENJ; Bacteria.
eggNOG; COG1538; LUCA.
HOGENOM; HOG000111955; -.
InParanoid; P77211; -.
KO; K07796; -.
OMA; MIESTRA; -.
PhylomeDB; P77211; -.
BioCyc; EcoCyc:G6320-MONOMER; -.
BioCyc; MetaCyc:G6320-MONOMER; -.
EvolutionaryTrace; P77211; -.
PRO; PR:P77211; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
GO; GO:0005507; F:copper ion binding; IGI:EcoCyc.
GO; GO:0005375; F:copper ion transmembrane transporter activity; IGI:EcoCyc.
GO; GO:0019992; F:diacylglycerol binding; IDA:UniProtKB.
GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
GO; GO:0006878; P:cellular copper ion homeostasis; IGI:EcoCyc.
GO; GO:0060003; P:copper ion export; IGI:EcoCyc.
GO; GO:0010273; P:detoxification of copper ion; IGI:EcoCyc.
GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
GO; GO:0046688; P:response to copper ion; IMP:EcoliWiki.
GO; GO:0010272; P:response to silver ion; IMP:EcoCyc.
InterPro; IPR003423; OMP_efflux.
InterPro; IPR010131; RND_efflux_OM_lipoprot_NodT.
Pfam; PF02321; OEP; 2.
TIGRFAMs; TIGR01845; outer_NodT; 1.
PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
1: Evidence at protein level;
3D-structure; Cell outer membrane; Complete proteome; Ion transport;
Lipoprotein; Membrane; Palmitate; Porin; Reference proteome; Signal;
Transmembrane; Transmembrane beta strand; Transport.
SIGNAL 1 17 {ECO:0000255|PROSITE-ProRule:PRU00303}.
CHAIN 18 457 Cation efflux system protein CusC.
/FTId=PRO_0000030992.
LIPID 18 18 N-palmitoyl cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000269|PubMed:21249122}.
LIPID 18 18 S-diacylglycerol cysteine.
{ECO:0000255|PROSITE-ProRule:PRU00303,
ECO:0000269|PubMed:21249122}.
VARIANT 6 6 L -> I (in strain: K1 / RS218).
VARIANT 20 20 L -> M (in strain: K1 / RS218).
VARIANT 27 27 P -> S (in strain: K1 / RS218).
VARIANT 33 33 Q -> H (in strain: K1 / RS218).
VARIANT 50 51 QN -> RS (in strain: K1 / RS218).
VARIANT 81 81 T -> A (in strain: K1 / RS218).
VARIANT 102 102 L -> F (in strain: K1 / RS218).
VARIANT 106 106 G -> D (in strain: K1 / RS218).
VARIANT 117 118 NT -> DS (in strain: K1 / RS218).
VARIANT 167 167 S -> F (in strain: K1 / RS218).
VARIANT 191 191 R -> G (in strain: K1 / RS218).
VARIANT 232 232 Q -> R (in strain: K1 / RS218).
VARIANT 273 273 S -> P (in strain: K1 / RS218).
VARIANT 457 457 G -> GWQQ (in strain: K1 / RS218).
STRAND 33 35 {ECO:0000244|PDB:4K7R}.
HELIX 54 57 {ECO:0000244|PDB:4K7R}.
HELIX 61 73 {ECO:0000244|PDB:4K7R}.
HELIX 75 96 {ECO:0000244|PDB:4K7R}.
STRAND 101 111 {ECO:0000244|PDB:4K7R}.
STRAND 114 117 {ECO:0000244|PDB:4K7R}.
STRAND 121 133 {ECO:0000244|PDB:4K7R}.
HELIX 139 204 {ECO:0000244|PDB:4K7R}.
TURN 205 207 {ECO:0000244|PDB:4K7R}.
HELIX 211 246 {ECO:0000244|PDB:4K7R}.
HELIX 260 262 {ECO:0000244|PDB:4K7R}.
HELIX 274 279 {ECO:0000244|PDB:4K7R}.
HELIX 281 302 {ECO:0000244|PDB:4K7R}.
STRAND 307 320 {ECO:0000244|PDB:4K7R}.
HELIX 321 323 {ECO:0000244|PDB:4K7R}.
HELIX 327 329 {ECO:0000244|PDB:4K7R}.
STRAND 330 339 {ECO:0000244|PDB:4K7R}.
HELIX 347 413 {ECO:0000244|PDB:4K7R}.
HELIX 419 453 {ECO:0000244|PDB:4K7R}.
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


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