ID   CUSC_ECO57              Reviewed;         460 AA.
AC   Q8XBY3;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Cation efflux system protein CusC;
DE   Flags: Precursor;
GN   Name=cusC; OrderedLocusNames=Z0711, ECs0610;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG54905.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34033.1; -; Genomic_DNA.
DR   PIR; B90705; B90705.
DR   PIR; E85555; E85555.
DR   RefSeq; NP_308637.1; NC_002695.1.
DR   RefSeq; WP_000074204.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XBY3; -.
DR   SMR; Q8XBY3; -.
DR   STRING; 155864.EDL933_0636; -.
DR   EnsemblBacteria; AAG54905; AAG54905; Z0711.
DR   EnsemblBacteria; BAB34033; BAB34033; ECs_0610.
DR   GeneID; 916968; -.
DR   KEGG; ece:Z0711; -.
DR   KEGG; ecs:ECs_0610; -.
DR   PATRIC; fig|386585.9.peg.718; -.
DR   eggNOG; COG1538; Bacteria.
DR   HOGENOM; CLU_012817_13_3_6; -.
DR   OMA; AQYERTI; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome; Signal; Transmembrane;
KW   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_0000030993"
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;  50715 MW;  FE79EDB715ABC922 CRC64;
     MSPCKLLPFC VALALTGCSL APDYQRPAMP VPQQFSLSQN GLVNAADNYQ NAGWRTFFVD
     NQVKTLISEA LENNRDLRMA TLKVQEARAQ YRLTDADRYP QLNGEGSGSW SGNLKGDSAT
     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 ATRQTVLDLN YARQVNEISL YTALGGGWQQ