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Protein

Cation efflux system protein CusA

Gene

cusA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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

  • copper ion binding Source: EcoCyc
  • copper ion transmembrane transporter activity Source: EcoCyc
  • silver ion transmembrane transporter activity Source: EcoCyc

GO - Biological processi

  • cellular copper ion homeostasis Source: EcoCyc
  • copper ion export Source: EcoCyc
  • detoxification of copper ion Source: EcoCyc
  • plasma membrane copper ion transport Source: EcoCyc
  • response to copper ion Source: EcoliWiki
  • response to silver ion Source: EcoCyc
  • 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.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12367. cusA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei14 – 34HelicalSequence analysisAdd BLAST21
Transmembranei338 – 358HelicalSequence analysisAdd BLAST21
Transmembranei363 – 383HelicalSequence analysisAdd BLAST21
Transmembranei391 – 411HelicalSequence analysisAdd BLAST21
Transmembranei446 – 466HelicalSequence analysisAdd BLAST21
Transmembranei485 – 505HelicalSequence analysisAdd BLAST21
Transmembranei532 – 552HelicalSequence analysisAdd BLAST21
Transmembranei871 – 891HelicalSequence analysisAdd BLAST21
Transmembranei898 – 918HelicalSequence analysisAdd BLAST21
Transmembranei928 – 948HelicalSequence analysisAdd BLAST21
Transmembranei985 – 1005HelicalSequence analysisAdd BLAST21
Transmembranei1012 – 1032HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

  • integral component of membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi399A → D: Strong decrease in copper resistance. 1 Publication1
Mutagenesisi405D → N: Loss of copper resistance. 1 Publication1
Mutagenesisi412E → D: Slight decrease in copper resistance. 1 Publication1
Mutagenesisi412E → Q: Loss of copper resistance. 1 Publication1
Mutagenesisi573M → I: Loss of copper resistance. 1 Publication1
Mutagenesisi623M → I: Loss of copper resistance. 1 Publication1
Mutagenesisi640M → I: No change in copper resistance. 1 Publication1
Mutagenesisi672M → I: Loss of copper resistance. 1 Publication1
Mutagenesisi738M → I: No change in copper resistance. 1 Publication1
Mutagenesisi755M → I: Slight decrease in copper resistance. 1 Publication1
Mutagenesisi792M → I: No change in copper resistance. 1 Publication1
Mutagenesisi812M → I: Slight decrease in copper resistance. 1 Publication1
Mutagenesisi833M → I: Slight decrease in copper resistance. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001618151 – 1047Cation efflux system protein CusAAdd BLAST1047

Proteomic databases

PaxDbiP38054.
PRIDEiP38054.

Expressioni

Inductioni

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi4260908. 265 interactors.
DIPiDIP-9345N.
IntActiP38054. 3 interactors.
STRINGi511145.b0575.

Structurei

Secondary structure

11047
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 11Combined sources7
Helixi13 – 32Combined sources20
Beta strandi46 – 52Combined sources7
Helixi58 – 64Combined sources7
Helixi66 – 73Combined sources8
Beta strandi79 – 87Combined sources9
Beta strandi90 – 97Combined sources8
Helixi103 – 115Combined sources13
Helixi118 – 120Combined sources3
Beta strandi127 – 129Combined sources3
Helixi135 – 137Combined sources3
Beta strandi138 – 151Combined sources14
Helixi153 – 162Combined sources10
Helixi164 – 168Combined sources5
Beta strandi174 – 182Combined sources9
Beta strandi185 – 191Combined sources7
Helixi193 – 198Combined sources6
Helixi203 – 211Combined sources9
Beta strandi217 – 224Combined sources8
Beta strandi227 – 233Combined sources7
Helixi240 – 244Combined sources5
Beta strandi247 – 250Combined sources4
Beta strandi256 – 258Combined sources3
Helixi259 – 262Combined sources4
Beta strandi263 – 269Combined sources7
Beta strandi273 – 278Combined sources6
Beta strandi285 – 291Combined sources7
Beta strandi293 – 295Combined sources3
Helixi297 – 314Combined sources18
Beta strandi319 – 326Combined sources8
Helixi328 – 352Combined sources25
Turni353 – 355Combined sources3
Helixi360 – 367Combined sources8
Turni368 – 370Combined sources3
Helixi371 – 384Combined sources14
Helixi390 – 417Combined sources28
Turni418 – 420Combined sources3
Helixi421 – 424Combined sources4
Helixi434 – 440Combined sources7
Turni441 – 445Combined sources5
Helixi446 – 459Combined sources14
Helixi462 – 466Combined sources5
Helixi469 – 492Combined sources24
Turni493 – 496Combined sources4
Helixi497 – 503Combined sources7
Helixi518 – 532Combined sources15
Helixi537 – 549Combined sources13
Helixi551 – 554Combined sources4
Beta strandi557 – 559Combined sources3
Beta strandi568 – 572Combined sources5
Helixi582 – 597Combined sources16
Beta strandi602 – 610Combined sources9
Beta strandi612 – 614Combined sources3
Beta strandi626 – 630Combined sources5
Turni633 – 635Combined sources3
Helixi642 – 652Combined sources11
Beta strandi658 – 663Combined sources6
Helixi665 – 674Combined sources10
Beta strandi678 – 686Combined sources9
Helixi690 – 706Combined sources17
Beta strandi707 – 709Combined sources3
Beta strandi711 – 715Combined sources5
Beta strandi721 – 728Combined sources8
Helixi730 – 734Combined sources5
Turni735 – 737Combined sources3
Helixi740 – 748Combined sources9
Turni749 – 751Combined sources3
Beta strandi755 – 761Combined sources7
Beta strandi764 – 771Combined sources8
Helixi774 – 776Combined sources3
Beta strandi777 – 779Combined sources3
Helixi780 – 783Combined sources4
Beta strandi787 – 789Combined sources3
Beta strandi795 – 797Combined sources3
Helixi798 – 800Combined sources3
Beta strandi802 – 809Combined sources8
Beta strandi813 – 816Combined sources4
Beta strandi819 – 827Combined sources9
Helixi833 – 847Combined sources15
Beta strandi855 – 860Combined sources6
Helixi861 – 873Combined sources13
Helixi875 – 890Combined sources16
Helixi894 – 901Combined sources8
Helixi905 – 918Combined sources14
Beta strandi921 – 923Combined sources3
Helixi924 – 951Combined sources28
Beta strandi953 – 955Combined sources3
Helixi956 – 959Combined sources4
Turni960 – 962Combined sources3
Helixi966 – 999Combined sources34
Helixi1006 – 1011Combined sources6
Helixi1014 – 1030Combined sources17
Helixi1032 – 1038Combined sources7
Turni1039 – 1041Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP38054.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38054.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4108IJF. Bacteria.
COG3696. LUCA.
HOGENOMiHOG000126202.
InParanoidiP38054.
KOiK07787.
OMAiFLIRIYH.
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)DescriptionActionsGraphical viewLength
Sequence conflicti897 – 898AL → SV in M58000 (PubMed:1711024).Curated2

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.
WP_000573945.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73676; AAC73676; b0575.
BAA35215; BAA35215; BAA35215.
GeneIDi945191.
KEGGiecj:JW0564.
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.
PIRiE64790.
RefSeqiNP_415107.1. NC_000913.3.
WP_000573945.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP38054.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260908. 265 interactors.
DIPiDIP-9345N.
IntActiP38054. 3 interactors.
STRINGi511145.b0575.

Protein family/group databases

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

Proteomic databases

PaxDbiP38054.
PRIDEiP38054.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73676; AAC73676; b0575.
BAA35215; BAA35215; BAA35215.
GeneIDi945191.
KEGGiecj:JW0564.
eco:b0575.
PATRICi32116318. VBIEscCol129921_0599.

Organism-specific databases

EchoBASEiEB2270.
EcoGeneiEG12367. cusA.

Phylogenomic databases

eggNOGiENOG4108IJF. Bacteria.
COG3696. LUCA.
HOGENOMiHOG000126202.
InParanoidiP38054.
KOiK07787.
OMAiFLIRIYH.
PhylomeDBiP38054.

Enzyme and pathway databases

BioCyciEcoCyc:YBDE-MONOMER.
ECOL316407:JW0564-MONOMER.
MetaCyc:YBDE-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38054.
PROiP38054.

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.
ProtoNetiSearch...

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 2, 2016
This is version 137 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.