SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P38054

- CUSA_ECOLI

UniProt

P38054 - CUSA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cation efflux system protein CusA

Gene
cusA, ybdE, b0575, JW0564
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 – 3421Helical; Reviewed predictionAdd
BLAST
Transmembranei338 – 35821Helical; Reviewed predictionAdd
BLAST
Transmembranei363 – 38321Helical; Reviewed predictionAdd
BLAST
Transmembranei391 – 41121Helical; Reviewed predictionAdd
BLAST
Transmembranei446 – 46621Helical; Reviewed predictionAdd
BLAST
Transmembranei485 – 50521Helical; Reviewed predictionAdd
BLAST
Transmembranei532 – 55221Helical; Reviewed predictionAdd
BLAST
Transmembranei871 – 89121Helical; Reviewed predictionAdd
BLAST
Transmembranei898 – 91821Helical; Reviewed predictionAdd
BLAST
Transmembranei928 – 94821Helical; Reviewed predictionAdd
BLAST
Transmembranei985 – 100521Helical; Reviewed predictionAdd
BLAST
Transmembranei1012 – 103221Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

Miscellaneous databases

EvolutionaryTraceiP38054.

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti897 – 8982AL → SV in M58000. 1 Publication

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

« 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: July 9, 2014
This is version 121 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

Similar proteinsi