CUSA_ECOL6
ID CUSA_ECOL6 Reviewed; 1047 AA.
AC Q8FK36;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cation efflux system protein CusA;
GN Name=cusA; OrderedLocusNames=c0661;
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: Part of a cation efflux system that mediates resistance to
CC copper and silver. {ECO:0000250}.
CC -!- SUBUNIT: The cus efflux system is composed of CusA, CusB, CusC and
CC CusF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Transcriptionally regulated by CusR in response to copper
CC and silver ions. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. {ECO:0000305}.
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DR EMBL; AE014075; AAN79136.1; -; Genomic_DNA.
DR RefSeq; WP_000573985.1; NC_004431.1.
DR STRING; 199310.c0661; -.
DR EnsemblBacteria; AAN79136; AAN79136; c0661.
DR KEGG; ecc:c0661; -.
DR eggNOG; COG3696; Bacteria.
DR HOGENOM; CLU_002755_1_2_6; -.
DR OMA; NSWTYPI; -.
DR BioCyc; ECOL199310:C0661-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2090.10; -; 2.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR004763; CzcA/CusA/SilA/NccA/HelA/CnrA.
DR PANTHER; PTHR32063; PTHR32063; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82714; SSF82714; 2.
DR TIGRFAMs; TIGR00914; 2A0601; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Copper; Copper transport;
KW Ion transport; Membrane; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1047
FT /note="Cation efflux system protein CusA"
FT /id="PRO_0000161817"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 871..891
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 898..918
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 928..948
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1005
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1012..1032
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1047 AA; 114723 MW; 53F21ECED055930C CRC64;
MIEWIIRRSV ANRFLVLMGA LFLSIWGTWT IINTPVDALP DLSDVQVIIK TSYPGQAPQI
VENQVTYPLT TTMLSVPGAK TVRGFSQFGD SYVYVIFEDG TDPYWARSRV LEYLNQVQGK
LPAGVSAELG PDATGVGWIY EYALVDRSGK HDLADLRSLQ DWFLKYELKT IPDVAEVASV
GGVVKEYQVV IDPQRLAQYG ISLAEVKSAL DASNQEAGGS SIELAEAEYM VRASGYLQTL
DDFNHIVLKA SENGVPVYLR DVAKVQVGPE MRRGIAELNG EGEVAGGVVI LRSGKNAREV
IAAVKDKLET LKSSLPEGVE IVTTYDRSQL IDRAIDNLSG KLLEEFIVVA VVCALFLWHV
RSALVAIISL PLGLCIAFIV MHFQGLNANI MSLGGIAIAV GAMVDAAIVM IENAHKRLEE
WQHQHPDATL DNKTRWQVIT DASVEVGPAL FISLLIITLS FIPIFTLEGQ EGRLFGPLAF
TKTYAMAGAA LLAIVVIPIL MGYWIRGKIP PESSNPLNRF LIRVYHPLLL KVLHWPKTTL
LVAALSVLTV LWPXNKVGGE FLPQINEGDL LYMPSTLPGI SAAEAASMLQ KTDKLIMSVP
EVARVFGKTG KAETATDSAP LEMVETTIQL KPQDQWRPGM TMDKIIEELD NTVRLPGLAN
LWVPPIRNRI DMLSTGIKSP IGIKVSGTVL ADIDTMAEQI EEVARTVPGV ASALAERLEG
GRYINVEINR EKAARYGMTV ADVQLFVTSA VGGAMVGETV EGIARYPINL RYPQSWRDSP
QALRQLPILT PMKQQITLAD VADVKVSTGP SMLKTENARP TSWIYIDARD RDMVSVVHDL
QKAIAEKVQL KPGTSVAFSG QFELLERANH KLKLMVPMTL MIIFVLLYLA FRRVGEALLI
ISSVPFALVG GIWLLWWMGF HLSVATGTGF IALAGVAAEF GVVMLMYLRH AIEAEPSLNN
PQTFSEQKLD EALYHGAVLR VRPKAMTVAV IIAGLLPILW GTGAGSEVMS RIAAPMIGGM
ITAPLLSLFI IPAAYKLMWL HRHRVRK