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P38054 (CUSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cation efflux system protein CusA
Gene names
Name:cusA
Synonyms:ybdE
Ordered Locus Names:b0575, JW0564
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1047 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of a cation efflux system that mediates resistance to copper and silver. Ref.8 Ref.10

Subunit structure

The cus efflux system is composed of CusA, CusB, CusC and CusF.

Subcellular location

Cell inner membrane; Multi-pass membrane protein Potential.

Induction

Transcriptionally regulated by CusR in response to copper and silver ions. Ref.9

Miscellaneous

The cus system plays an important role in copper tolerance under anaerobic growth and, under extreme copper stress, in aerobic growth.

Sequence similarities

Belongs to the AcrB/AcrD/AcrF (TC 2.A.6) family. [View classification]

Sequence caution

The sequence M58000 differs from that shown. Reason: Frameshift at positions 897 and 933.

Ontologies

Keywords
   Biological processCopper transport
Ion transport
Transport
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandCopper
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular copper ion homeostasis

Inferred from genetic interaction PubMed 11222619. Source: EcoCyc

copper ion export

Inferred from genetic interaction PubMed 11222619Ref.10. Source: EcoCyc

detoxification of copper ion

Inferred from genetic interaction PubMed 11222619Ref.10. Source: EcoCyc

plasma membrane copper ion transport

Inferred from genetic interaction PubMed 11222619Ref.10. Source: EcoCyc

response to copper ion

Inferred from mutant phenotype Ref.10. Source: EcoliWiki

response to silver ion

Inferred from mutant phenotype Ref.9PubMed 11739772PubMed 18419149. Source: EcoCyc

silver ion transmembrane transport

Inferred from mutant phenotype PubMed 11739772. Source: GOC

silver ion transport

Inferred from mutant phenotype PubMed 11739772. Source: EcoCyc

   Cellular_componentintegral component of membrane

Inferred from direct assay PubMed 20865003. Source: EcoCyc

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopper ion binding

Inferred from genetic interaction Ref.10. Source: EcoCyc

copper ion transmembrane transporter activity

Inferred from genetic interaction PubMed 11222619Ref.10. Source: EcoCyc

silver ion transmembrane transporter activity

Inferred from mutant phenotype PubMed 11739772. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10471047Cation efflux system protein CusA
PRO_0000161815

Regions

Transmembrane14 – 3421Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane363 – 38321Helical; Potential
Transmembrane391 – 41121Helical; Potential
Transmembrane446 – 46621Helical; Potential
Transmembrane485 – 50521Helical; Potential
Transmembrane532 – 55221Helical; Potential
Transmembrane871 – 89121Helical; Potential
Transmembrane898 – 91821Helical; Potential
Transmembrane928 – 94821Helical; Potential
Transmembrane985 – 100521Helical; Potential
Transmembrane1012 – 103221Helical; Potential

Experimental info

Mutagenesis3991A → D: Strong decrease in copper resistance. Ref.10
Mutagenesis4051D → N: Loss of copper resistance. Ref.10
Mutagenesis4121E → D: Slight decrease in copper resistance. Ref.10
Mutagenesis4121E → Q: Loss of copper resistance. Ref.10
Mutagenesis5731M → I: Loss of copper resistance. Ref.10
Mutagenesis6231M → I: Loss of copper resistance. Ref.10
Mutagenesis6401M → I: No change in copper resistance. Ref.10
Mutagenesis6721M → I: Loss of copper resistance. Ref.10
Mutagenesis7381M → I: No change in copper resistance. Ref.10
Mutagenesis7551M → I: Slight decrease in copper resistance. Ref.10
Mutagenesis7921M → I: No change in copper resistance. Ref.10
Mutagenesis8121M → I: Slight decrease in copper resistance. Ref.10
Mutagenesis8331M → I: Slight decrease in copper resistance. Ref.10
Sequence conflict897 – 8982AL → SV in M58000. Ref.5

Secondary structure

...................................................................................................................................................................... 1047
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38054 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D20BAB10118D4C52

FASTA1,047114,707
        10         20         30         40         50         60 
MIEWIIRRSV ANRFLVLMGA LFLSIWGTWT IINTPVDALP DLSDVQVIIK TSYPGQAPQI 

        70         80         90        100        110        120 
VENQVTYPLT TTMLSVPGAK TVRGFSQFGD SYVYVIFEDG TDPYWARSRV LEYLNQVQGK 

       130        140        150        160        170        180 
LPAGVSAELG PDATGVGWIY EYALVDRSGK HDLADLRSLQ DWFLKYELKT IPDVAEVASV 

       190        200        210        220        230        240 
GGVVKEYQVV IDPQRLAQYG ISLAEVKSAL DASNQEAGGS SIELAEAEYM VRASGYLQTL 

       250        260        270        280        290        300 
DDFNHIVLKA SENGVPVYLR DVAKVQIGPE MRRGIAELNG EGEVAGGVVI LRSGKNAREV 

       310        320        330        340        350        360 
IAAVKDKLET LKSSLPEGVE IVTTYDRSQL IDRAIDNLSG KLLEEFIVVA VVCALFLWHV 

       370        380        390        400        410        420 
RSALVAIISL PLGLCIAFIV MHFQGLNANI MSLGGIAIAV GAMVDAAIVM IENAHKRLEE 

       430        440        450        460        470        480 
WQHQHPDATL DNKTRWQVIT DASVEVGPAL FISLLIITLS FIPIFTLEGQ EGRLFGPLAF 

       490        500        510        520        530        540 
TKTYAMAGAA LLAIVVIPIL MGYWIRGKIP PESSNPLNRF LIRVYHPLLL KVLHWPKTTL 

       550        560        570        580        590        600 
LVAALSVLTV LWPLNKVGGE FLPQINEGDL LYMPSTLPGI SAAEAASMLQ KTDKLIMSVP 

       610        620        630        640        650        660 
EVARVFGKTG KAETATDSAP LEMVETTIQL KPQEQWRPGM TMDKIIEELD NTVRLPGLAN 

       670        680        690        700        710        720 
LWVPPIRNRI DMLSTGIKSP IGIKVSGTVL ADIDAMAEQI EEVARTVPGV ASALAERLEG 

       730        740        750        760        770        780 
GRYINVEINR EKAARYGMTV ADVQLFVTSA VGGAMVGETV EGIARYPINL RYPQSWRDSP 

       790        800        810        820        830        840 
QALRQLPILT PMKQQITLAD VADIKVSTGP SMLKTENARP TSWIYIDARD RDMVSVVHDL 

       850        860        870        880        890        900 
QKAIAEKVQL KPGTSVAFSG QFELLERANH KLKLMVPMTL MIIFVLLYLA FRRVGEALLI 

       910        920        930        940        950        960 
ISSVPFALVG GIWLLWWMGF HLSVATGTGF IALAGVAAEF GVVMLMYLRH AIEAVPSLNN 

       970        980        990       1000       1010       1020 
PQTFSEQKLD EALYHGAVLR VRPKAMTVAV IIAGLLPILW GTGAGSEVMS RIAAPMIGGM 

      1030       1040 
ITAPLLSLFI IPAAYKLMWL HRHRVRK 

« Hide

References

« Hide 'large scale' references
[1]"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."
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. expand/collapse author list , 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.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"Sequence of minutes 4-25 of Escherichia coli."
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.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Cloning and sequencing of the pheP gene, which encodes the phenylalanine-specific transport system of Escherichia coli."
Pi J., Wookey P.J., Pittard A.J.
J. Bacteriol. 173:3622-3629(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 871-1047.
Strain: K12.
[6]"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
Borodovsky M., Rudd K.E., Koonin E.V.
Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]"Identification of a copper-responsive two-component system on the chromosome of Escherichia coli K-12."
Munson G.P., Lam D.L., Outten F.W., O'Halloran T.V.
J. Bacteriol. 182:5864-5871(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE NAME.
Strain: K12 / DH5-alpha.
[8]"The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli."
Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V.
J. Biol. Chem. 276:30670-30677(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN COPPER HOMEOSTASIS.
Strain: K12.
[9]"The product of the ybdE gene of the Escherichia coli chromosome is involved in detoxification of silver ions."
Franke S., Grass G., Nies D.H.
Microbiology 147:965-972(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: K38.
[10]"Molecular analysis of the copper-transporting efflux system CusCFBA of Escherichia coli."
Franke S., Grass G., Rensing C., Nies D.H.
J. Bacteriol. 185:3804-3812(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ALA-399; ASP-405; GLU-412; MET-573; MET-623; MET-640; MET-672; MET-738; MET-755; MET-792; MET-812 AND MET-833.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82598 Genomic DNA. Translation: AAB40773.1.
U00096 Genomic DNA. Translation: AAC73676.1.
AP009048 Genomic DNA. Translation: BAA35215.1.
M58000 Genomic DNA. No translation available.
PIRE64790.
RefSeqNP_415107.1. NC_000913.3.
YP_488862.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3K07X-ray3.52A1-1047[»]
3K0IX-ray4.12A1-1047[»]
3KSOX-ray4.37A1-1047[»]
3KSSX-ray3.88A1-1047[»]
3NE5X-ray2.90A2-1047[»]
3T51X-ray3.90A1-1047[»]
3T53X-ray3.37A1-1047[»]
3T56X-ray3.42A1-1047[»]
4DNRX-ray3.68A1-1047[»]
4DNTX-ray3.10A1-1047[»]
4DOPX-ray4.20A1-1047[»]
ProteinModelPortalP38054.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9345N.
IntActP38054. 3 interactions.
STRING511145.b0575.

Protein family/group databases

TCDB2.A.6.1.4. the resistance-nodulation-cell division (rnd) superfamily.

Proteomic databases

PaxDbP38054.
PRIDEP38054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73676; AAC73676; b0575.
BAA35215; BAA35215; BAA35215.
GeneID12931914.
945191.
KEGGecj:Y75_p0562.
eco:b0575.
PATRIC32116318. VBIEscCol129921_0599.

Organism-specific databases

EchoBASEEB2270.
EcoGeneEG12367. cusA.

Phylogenomic databases

eggNOGCOG3696.
HOGENOMHOG000126202.
KOK07787.
OMATKTWSMA.
OrthoDBEOG6MPWR0.
PhylomeDBP38054.

Enzyme and pathway databases

BioCycEcoCyc:YBDE-MONOMER.
ECOL316407:JW0564-MONOMER.
MetaCyc:YBDE-MONOMER.
RETL1328306-WGS:GSTH-2533-MONOMER.

Gene expression databases

GenevestigatorP38054.

Family and domain databases

Gene3D3.30.2090.10. 2 hits.
InterProIPR027463. AcrB_DN_DC_subdom.
IPR001036. Acrflvin-R.
IPR004763. CzcA/CusA/SilA/NccA/HelA/CnrA.
[Graphical view]
PfamPF00873. ACR_tran. 1 hit.
[Graphical view]
PRINTSPR00702. ACRIFLAVINRP.
SUPFAMSSF82714. SSF82714. 2 hits.
TIGRFAMsTIGR00914. 2A0601. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP38054.
PROP38054.

Entry information

Entry nameCUSA_ECOLI
AccessionPrimary (citable) accession number: P38054
Secondary accession number(s): P77767
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene