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P38054

- CUSA_ECOLI

UniProt

P38054 - CUSA_ECOLI

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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

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
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

  1. integral component of membrane Source: EcoCyc
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3696.
HOGENOMiHOG000126202.
InParanoidiP38054.
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

        10         20         30         40         50
MIEWIIRRSV ANRFLVLMGA LFLSIWGTWT IINTPVDALP DLSDVQVIIK
60 70 80 90 100
TSYPGQAPQI VENQVTYPLT TTMLSVPGAK TVRGFSQFGD SYVYVIFEDG
110 120 130 140 150
TDPYWARSRV LEYLNQVQGK LPAGVSAELG PDATGVGWIY EYALVDRSGK
160 170 180 190 200
HDLADLRSLQ DWFLKYELKT IPDVAEVASV GGVVKEYQVV IDPQRLAQYG
210 220 230 240 250
ISLAEVKSAL DASNQEAGGS SIELAEAEYM VRASGYLQTL DDFNHIVLKA
260 270 280 290 300
SENGVPVYLR DVAKVQIGPE MRRGIAELNG EGEVAGGVVI LRSGKNAREV
310 320 330 340 350
IAAVKDKLET LKSSLPEGVE IVTTYDRSQL IDRAIDNLSG KLLEEFIVVA
360 370 380 390 400
VVCALFLWHV RSALVAIISL PLGLCIAFIV MHFQGLNANI MSLGGIAIAV
410 420 430 440 450
GAMVDAAIVM IENAHKRLEE WQHQHPDATL DNKTRWQVIT DASVEVGPAL
460 470 480 490 500
FISLLIITLS FIPIFTLEGQ EGRLFGPLAF TKTYAMAGAA LLAIVVIPIL
510 520 530 540 550
MGYWIRGKIP PESSNPLNRF LIRVYHPLLL KVLHWPKTTL LVAALSVLTV
560 570 580 590 600
LWPLNKVGGE FLPQINEGDL LYMPSTLPGI SAAEAASMLQ KTDKLIMSVP
610 620 630 640 650
EVARVFGKTG KAETATDSAP LEMVETTIQL KPQEQWRPGM TMDKIIEELD
660 670 680 690 700
NTVRLPGLAN LWVPPIRNRI DMLSTGIKSP IGIKVSGTVL ADIDAMAEQI
710 720 730 740 750
EEVARTVPGV ASALAERLEG GRYINVEINR EKAARYGMTV ADVQLFVTSA
760 770 780 790 800
VGGAMVGETV EGIARYPINL RYPQSWRDSP QALRQLPILT PMKQQITLAD
810 820 830 840 850
VADIKVSTGP SMLKTENARP TSWIYIDARD RDMVSVVHDL QKAIAEKVQL
860 870 880 890 900
KPGTSVAFSG QFELLERANH KLKLMVPMTL MIIFVLLYLA FRRVGEALLI
910 920 930 940 950
ISSVPFALVG GIWLLWWMGF HLSVATGTGF IALAGVAAEF GVVMLMYLRH
960 970 980 990 1000
AIEAVPSLNN PQTFSEQKLD EALYHGAVLR VRPKAMTVAV IIAGLLPILW
1010 1020 1030 1040
GTGAGSEVMS RIAAPMIGGM ITAPLLSLFI IPAAYKLMWL HRHRVRK
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. Curated

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P38054.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 124 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