(data stored in ACNUC7421 zone)

SWISSPROT: CUSC_ECO57

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   05-JUL-2017, entry version 90.
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.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., 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.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and 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
CC       across the outer membrane. Part of a cation efflux system that
CC       mediates resistance to copper and silver (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. Component of the cus efflux system composed
CC       of CusA, CusB, CusC and CusF (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Cell outer membrane
CC       {ECO:0000250}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}.
CC   -!- INDUCTION: Transcriptionally regulated by CusR in response to
CC       copper and silver ions. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC       family. {ECO:0000305}.
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_MWVM01000011.1.
DR   ProteinModelPortal; Q8XBY3; -.
DR   SMR; Q8XBY3; -.
DR   STRING; 155864.Z0711; -.
DR   EnsemblBacteria; AAG54905; AAG54905; Z0711.
DR   EnsemblBacteria; BAB34033; BAB34033; BAB34033.
DR   GeneID; 916968; -.
DR   KEGG; ece:Z0711; -.
DR   KEGG; ecs:ECs0610; -.
DR   PATRIC; fig|386585.9.peg.718; -.
DR   eggNOG; ENOG4105ENJ; Bacteria.
DR   eggNOG; COG1538; LUCA.
DR   HOGENOM; HOG000111955; -.
DR   KO; K07796; -.
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: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;
DR   PRODOM; Q8XBY3.
DR   SWISS-2DPAGE; Q8XBY3.
KW   Cell outer membrane; Complete proteome; Ion transport; Lipoprotein;
KW   Membrane; Palmitate; Porin; Signal; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL        1     17       {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   CHAIN        18    460       Cation efflux system protein CusC.
FT                                /FTId=PRO_0000030993.
FT   LIPID        18     18       N-palmitoyl cysteine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00303}.
FT   LIPID        18     18       S-diacylglycerol cysteine.
FT                                {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
//

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