CUSC_ECOL6
ID CUSC_ECOL6 Reviewed; 460 AA.
AC Q8CWA4;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cation efflux system protein CusC;
DE Flags: Precursor;
GN Name=cusC; OrderedLocusNames=c0658;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Component of the cus efflux system composed of
CC CusA, CusB, CusC and CusF (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Cell outer membrane {ECO:0000250};
CC Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- INDUCTION: Transcriptionally regulated by CusR in response to copper
CC and silver ions. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC family. {ECO:0000305}.
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DR EMBL; AE014075; AAN79133.1; -; Genomic_DNA.
DR RefSeq; WP_000074211.1; NC_004431.1.
DR AlphaFoldDB; Q8CWA4; -.
DR SMR; Q8CWA4; -.
DR STRING; 199310.c0658; -.
DR PRIDE; Q8CWA4; -.
DR EnsemblBacteria; AAN79133; AAN79133; c0658.
DR KEGG; ecc:c0658; -.
DR eggNOG; COG1538; Bacteria.
DR HOGENOM; CLU_012817_13_3_6; -.
DR OMA; AANQDYY; -.
DR BioCyc; ECOL199310:C0658-MON; -.
DR Proteomes; UP000001410; 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; ISS: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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
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 3: Inferred from homology;
KW Cell outer membrane; Ion transport; Lipoprotein; Membrane; Palmitate;
KW Porin; Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..460
FT /note="Cation efflux system protein CusC"
FT /id="PRO_0000030994"
FT LIPID 18
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 18
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 460 AA; 50709 MW; 4C1D618F06AD66B9 CRC64;
MSPCKLLPFC VALALTGCSL APDYQRPAMP VPQQFSLSQN GLVNAADNYQ NAGWRTFFVD
NQVKTLISEA LVNNRDLRMA ALKVQEARAQ YRLTDADRYP QLNGEGSGSW SGNLKGDSAT
TREFSTGLNA SFDLDFFGRL KNMSEAERQN YLATEEAQRA VHILLVSNVA QSYFNQQLAY
AQLQIAEETL RNYQQSYAFV EKQLLTGSSN VLALEQARGV IESTRSDIAK RQGELAQANN
ALQLLLGSYG KLPQAQTVNS DSLQSVKLPA GLPSQILLQR PDIMEAEHAL MAANANIGAA
RAAFFPSISL TSGISTASSD LSSLFNASSG MWNFIPKIEI PIFNAGRNQA NLDIAEIRQQ
QSVVNYEQKI QNAFKEVADA LALRQSLNDQ ISAQQRYLAS LQITLQRART LYQHGAVSYL
EVLDAERSLF ATRQTLLDLN YARQVNEISL YTALGGGWQQ