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P38054

- CUSA_ECOLI

UniProt

P38054 - CUSA_ECOLI

Protein

Cation efflux system protein CusA

Gene

cusA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Part of a cation efflux system that mediates resistance to copper and silver.2 Publications

    GO - Molecular functioni

    1. copper ion binding Source: EcoCyc
    2. copper ion transmembrane transporter activity Source: EcoCyc
    3. silver ion transmembrane transporter activity Source: EcoCyc

    GO - Biological processi

    1. cellular copper ion homeostasis Source: EcoCyc
    2. copper ion export Source: EcoCyc
    3. detoxification of copper ion Source: EcoCyc
    4. plasma membrane copper ion transport Source: EcoCyc
    5. response to copper ion Source: EcoliWiki
    6. response to silver ion Source: EcoCyc
    7. silver ion transmembrane transport Source: GOC
    8. silver ion transport Source: EcoCyc

    Keywords - Biological processi

    Copper transport, Ion transport, Transport

    Keywords - Ligandi

    Copper

    Enzyme and pathway databases

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

    Protein family/group databases

    TCDBi2.A.6.1.4. the resistance-nodulation-cell division (rnd) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cation efflux system protein CusA
    Gene namesi
    Name:cusA
    Synonyms:ybdE
    Ordered Locus Names:b0575, JW0564
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG12367. cusA.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: EcoCyc
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi399 – 3991A → D: Strong decrease in copper resistance. 1 Publication
    Mutagenesisi405 – 4051D → N: Loss of copper resistance. 1 Publication
    Mutagenesisi412 – 4121E → D: Slight decrease in copper resistance. 1 Publication
    Mutagenesisi412 – 4121E → Q: Loss of copper resistance. 1 Publication
    Mutagenesisi573 – 5731M → I: Loss of copper resistance. 1 Publication
    Mutagenesisi623 – 6231M → I: Loss of copper resistance. 1 Publication
    Mutagenesisi640 – 6401M → I: No change in copper resistance. 1 Publication
    Mutagenesisi672 – 6721M → I: Loss of copper resistance. 1 Publication
    Mutagenesisi738 – 7381M → I: No change in copper resistance. 1 Publication
    Mutagenesisi755 – 7551M → I: Slight decrease in copper resistance. 1 Publication
    Mutagenesisi792 – 7921M → I: No change in copper resistance. 1 Publication
    Mutagenesisi812 – 8121M → I: Slight decrease in copper resistance. 1 Publication
    Mutagenesisi833 – 8331M → I: Slight decrease in copper resistance. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10471047Cation efflux system protein CusAPRO_0000161815Add
    BLAST

    Proteomic databases

    PaxDbiP38054.
    PRIDEiP38054.

    Expressioni

    Inductioni

    Transcriptionally regulated by CusR in response to copper and silver ions.1 Publication

    Gene expression databases

    GenevestigatoriP38054.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-9345N.
    IntActiP38054. 3 interactions.
    STRINGi511145.b0575.

    Structurei

    Secondary structure

    1
    1047
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 117
    Helixi13 – 3220
    Beta strandi46 – 527
    Helixi58 – 647
    Helixi66 – 738
    Beta strandi79 – 879
    Beta strandi90 – 978
    Helixi103 – 11513
    Helixi118 – 1203
    Beta strandi127 – 1293
    Helixi135 – 1373
    Beta strandi138 – 15114
    Helixi153 – 16210
    Helixi164 – 1685
    Beta strandi174 – 1829
    Beta strandi185 – 1917
    Helixi193 – 1986
    Helixi203 – 2119
    Beta strandi217 – 2248
    Beta strandi227 – 2337
    Helixi240 – 2445
    Beta strandi247 – 2504
    Beta strandi256 – 2583
    Helixi259 – 2624
    Beta strandi263 – 2697
    Beta strandi273 – 2786
    Beta strandi285 – 2917
    Beta strandi293 – 2953
    Helixi297 – 31418
    Beta strandi319 – 3268
    Helixi328 – 35225
    Turni353 – 3553
    Helixi360 – 3678
    Turni368 – 3703
    Helixi371 – 38414
    Helixi390 – 41728
    Turni418 – 4203
    Helixi421 – 4244
    Helixi434 – 4407
    Turni441 – 4455
    Helixi446 – 45914
    Helixi462 – 4665
    Helixi469 – 49224
    Turni493 – 4964
    Helixi497 – 5037
    Helixi518 – 53215
    Helixi537 – 54913
    Helixi551 – 5544
    Beta strandi557 – 5593
    Beta strandi568 – 5725
    Helixi582 – 59716
    Beta strandi602 – 6109
    Beta strandi612 – 6143
    Beta strandi626 – 6305
    Turni633 – 6353
    Helixi642 – 65211
    Beta strandi658 – 6636
    Helixi665 – 67410
    Beta strandi678 – 6869
    Helixi690 – 70617
    Beta strandi707 – 7093
    Beta strandi711 – 7155
    Beta strandi721 – 7288
    Helixi730 – 7345
    Turni735 – 7373
    Helixi740 – 7489
    Turni749 – 7513
    Beta strandi755 – 7617
    Beta strandi764 – 7718
    Helixi774 – 7763
    Beta strandi777 – 7793
    Helixi780 – 7834
    Beta strandi787 – 7893
    Beta strandi795 – 7973
    Helixi798 – 8003
    Beta strandi802 – 8098
    Beta strandi813 – 8164
    Beta strandi819 – 8279
    Helixi833 – 84715
    Beta strandi855 – 8606
    Helixi861 – 87313
    Helixi875 – 89016
    Helixi894 – 9018
    Helixi905 – 91814
    Beta strandi921 – 9233
    Helixi924 – 95128
    Beta strandi953 – 9553
    Helixi956 – 9594
    Turni960 – 9623
    Helixi966 – 99934
    Helixi1006 – 10116
    Helixi1014 – 103017
    Helixi1032 – 10387
    Turni1039 – 10413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP38054.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38054.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei14 – 3421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei338 – 35821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei363 – 38321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei391 – 41121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei446 – 46621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei485 – 50521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei532 – 55221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei871 – 89121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei898 – 91821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei928 – 94821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei985 – 100521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1012 – 103221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3696.
    HOGENOMiHOG000126202.
    KOiK07787.
    OMAiTKTWSMA.
    OrthoDBiEOG6MPWR0.
    PhylomeDBiP38054.

    Family and domain databases

    Gene3Di3.30.2090.10. 2 hits.
    InterProiIPR027463. AcrB_DN_DC_subdom.
    IPR001036. Acrflvin-R.
    IPR004763. CzcA/CusA/SilA/NccA/HelA/CnrA.
    [Graphical view]
    PfamiPF00873. ACR_tran. 1 hit.
    [Graphical view]
    PRINTSiPR00702. ACRIFLAVINRP.
    SUPFAMiSSF82714. SSF82714. 2 hits.
    TIGRFAMsiTIGR00914. 2A0601. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P38054-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIEWIIRRSV ANRFLVLMGA LFLSIWGTWT IINTPVDALP DLSDVQVIIK     50
    TSYPGQAPQI VENQVTYPLT TTMLSVPGAK TVRGFSQFGD SYVYVIFEDG 100
    TDPYWARSRV LEYLNQVQGK LPAGVSAELG PDATGVGWIY EYALVDRSGK 150
    HDLADLRSLQ DWFLKYELKT IPDVAEVASV GGVVKEYQVV IDPQRLAQYG 200
    ISLAEVKSAL DASNQEAGGS SIELAEAEYM VRASGYLQTL DDFNHIVLKA 250
    SENGVPVYLR DVAKVQIGPE MRRGIAELNG EGEVAGGVVI LRSGKNAREV 300
    IAAVKDKLET LKSSLPEGVE IVTTYDRSQL IDRAIDNLSG KLLEEFIVVA 350
    VVCALFLWHV RSALVAIISL PLGLCIAFIV MHFQGLNANI MSLGGIAIAV 400
    GAMVDAAIVM IENAHKRLEE WQHQHPDATL DNKTRWQVIT DASVEVGPAL 450
    FISLLIITLS FIPIFTLEGQ EGRLFGPLAF TKTYAMAGAA LLAIVVIPIL 500
    MGYWIRGKIP PESSNPLNRF LIRVYHPLLL KVLHWPKTTL LVAALSVLTV 550
    LWPLNKVGGE FLPQINEGDL LYMPSTLPGI SAAEAASMLQ KTDKLIMSVP 600
    EVARVFGKTG KAETATDSAP LEMVETTIQL KPQEQWRPGM TMDKIIEELD 650
    NTVRLPGLAN LWVPPIRNRI DMLSTGIKSP IGIKVSGTVL ADIDAMAEQI 700
    EEVARTVPGV ASALAERLEG GRYINVEINR EKAARYGMTV ADVQLFVTSA 750
    VGGAMVGETV EGIARYPINL RYPQSWRDSP QALRQLPILT PMKQQITLAD 800
    VADIKVSTGP SMLKTENARP TSWIYIDARD RDMVSVVHDL QKAIAEKVQL 850
    KPGTSVAFSG QFELLERANH KLKLMVPMTL MIIFVLLYLA FRRVGEALLI 900
    ISSVPFALVG GIWLLWWMGF HLSVATGTGF IALAGVAAEF GVVMLMYLRH 950
    AIEAVPSLNN PQTFSEQKLD EALYHGAVLR VRPKAMTVAV IIAGLLPILW 1000
    GTGAGSEVMS RIAAPMIGGM ITAPLLSLFI IPAAYKLMWL HRHRVRK 1047
    Length:1,047
    Mass (Da):114,707
    Last modified:November 1, 1997 - v2
    Checksum:iD20BAB10118D4C52
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti897 – 8982AL → SV in M58000. (PubMed:1711024)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82598 Genomic DNA. Translation: AAB40773.1.
    U00096 Genomic DNA. Translation: AAC73676.1.
    AP009048 Genomic DNA. Translation: BAA35215.1.
    M58000 Genomic DNA. No translation available.
    PIRiE64790.
    RefSeqiNP_415107.1. NC_000913.3.
    YP_488862.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73676; AAC73676; b0575.
    BAA35215; BAA35215; BAA35215.
    GeneIDi12931914.
    945191.
    KEGGiecj:Y75_p0562.
    eco:b0575.
    PATRICi32116318. VBIEscCol129921_0599.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82598 Genomic DNA. Translation: AAB40773.1 .
    U00096 Genomic DNA. Translation: AAC73676.1 .
    AP009048 Genomic DNA. Translation: BAA35215.1 .
    M58000 Genomic DNA. No translation available.
    PIRi E64790.
    RefSeqi NP_415107.1. NC_000913.3.
    YP_488862.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3K07 X-ray 3.52 A 1-1047 [» ]
    3K0I X-ray 4.12 A 1-1047 [» ]
    3KSO X-ray 4.37 A 1-1047 [» ]
    3KSS X-ray 3.88 A 1-1047 [» ]
    3NE5 X-ray 2.90 A 2-1047 [» ]
    3T51 X-ray 3.90 A 1-1047 [» ]
    3T53 X-ray 3.37 A 1-1047 [» ]
    3T56 X-ray 3.42 A 1-1047 [» ]
    4DNR X-ray 3.68 A 1-1047 [» ]
    4DNT X-ray 3.10 A 1-1047 [» ]
    4DOP X-ray 4.20 A 1-1047 [» ]
    ProteinModelPortali P38054.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9345N.
    IntActi P38054. 3 interactions.
    STRINGi 511145.b0575.

    Protein family/group databases

    TCDBi 2.A.6.1.4. the resistance-nodulation-cell division (rnd) superfamily.

    Proteomic databases

    PaxDbi P38054.
    PRIDEi P38054.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73676 ; AAC73676 ; b0575 .
    BAA35215 ; BAA35215 ; BAA35215 .
    GeneIDi 12931914.
    945191.
    KEGGi ecj:Y75_p0562.
    eco:b0575.
    PATRICi 32116318. VBIEscCol129921_0599.

    Organism-specific databases

    EchoBASEi EB2270.
    EcoGenei EG12367. cusA.

    Phylogenomic databases

    eggNOGi COG3696.
    HOGENOMi HOG000126202.
    KOi K07787.
    OMAi TKTWSMA.
    OrthoDBi EOG6MPWR0.
    PhylomeDBi P38054.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P38054.
    PROi P38054.

    Gene expression databases

    Genevestigatori P38054.

    Family and domain databases

    Gene3Di 3.30.2090.10. 2 hits.
    InterProi IPR027463. AcrB_DN_DC_subdom.
    IPR001036. Acrflvin-R.
    IPR004763. CzcA/CusA/SilA/NccA/HelA/CnrA.
    [Graphical view ]
    Pfami PF00873. ACR_tran. 1 hit.
    [Graphical view ]
    PRINTSi PR00702. ACRIFLAVINRP.
    SUPFAMi SSF82714. SSF82714. 2 hits.
    TIGRFAMsi TIGR00914. 2A0601. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. 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. 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.

    Entry informationi

    Entry nameiCUSA_ECOLI
    AccessioniPrimary (citable) accession number: P38054
    Secondary accession number(s): P77767
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3