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Protein

Cation efflux system protein CusB

Gene

cusB

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
  • transition metal ion binding 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
Complete GO annotation...

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

Copper

Enzyme and pathway databases

BioCyciEcoCyc:G6322-MONOMER.
ECOL316407:JW0563-MONOMER.
MetaCyc:G6322-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 CusB
Gene namesi
Name:cusB
Synonyms:ylcD
Ordered Locus Names:b0574, JW0563
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14235. cusB.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: InterPro
  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000001869029 – 407Cation efflux system protein CusBAdd BLAST379

Proteomic databases

PaxDbiP77239.
PRIDEiP77239.

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

BioGridi4262993. 129 interactors.
DIPiDIP-9346N.
IntActiP77239. 3 interactors.
STRINGi511145.b0574.

Structurei

Secondary structure

1407
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi96 – 98Combined sources3
Beta strandi100 – 102Combined sources3
Beta strandi105 – 124Combined sources20
Beta strandi130 – 135Combined sources6
Beta strandi143 – 145Combined sources3
Beta strandi149 – 154Combined sources6
Helixi159 – 170Combined sources12
Helixi175 – 187Combined sources13
Helixi192 – 201Combined sources10
Beta strandi207 – 211Combined sources5
Beta strandi213 – 220Combined sources8
Beta strandi231 – 233Combined sources3
Beta strandi235 – 251Combined sources17
Helixi252 – 254Combined sources3
Helixi255 – 258Combined sources4
Helixi261 – 263Combined sources3
Beta strandi264 – 268Combined sources5
Beta strandi271 – 278Combined sources8
Beta strandi282 – 288Combined sources7
Turni289 – 292Combined sources4
Beta strandi293 – 301Combined sources9
Beta strandi303 – 305Combined sources3
Beta strandi312 – 320Combined sources9
Beta strandi324 – 328Combined sources5
Helixi329 – 331Combined sources3
Beta strandi332 – 334Combined sources3
Beta strandi335 – 337Combined sources3
Beta strandi339 – 344Combined sources6
Beta strandi346 – 348Combined sources3
Beta strandi350 – 354Combined sources5
Beta strandi356 – 361Combined sources6
Beta strandi364 – 371Combined sources8
Beta strandi376 – 378Combined sources3
Turni386 – 388Combined sources3
Helixi391 – 396Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H94X-ray3.84A/B1-407[»]
3NE5X-ray2.90B/C1-407[»]
3OOCX-ray3.40A/B1-407[»]
3OPOX-ray3.85A/B1-407[»]
3OW7X-ray3.78A/B1-407[»]
3T51X-ray3.90B/C78-407[»]
3T53X-ray3.37B/C78-407[»]
3T56X-ray3.42B/C78-407[»]
4DNRX-ray3.68B/C1-407[»]
4DNTX-ray3.10B/C1-407[»]
4DOPX-ray4.20B/C1-407[»]
ProteinModelPortaliP77239.
SMRiP77239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP77239.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105EP1. Bacteria.
ENOG410XPHF. LUCA.
HOGENOMiHOG000126091.
InParanoidiP77239.
KOiK07798.
OMAiTISARQQ.
PhylomeDBiP77239.

Family and domain databases

InterProiIPR032317. HlyD_D23.
IPR006143. RND_pump_MFP.
[Graphical view]
PfamiPF00529. HlyD. 1 hit.
PF16576. HlyD_D23. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01730. RND_mfp. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P77239-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKIALIIGS MIAGGIISAA GFTWVAKAEP PAEKTSTAER KILFWYDPMY
60 70 80 90 100
PNTRFDKPGK SPFMDMDLVP KYADEESSAS GVRIDPTQTQ NLGVKTATVT
110 120 130 140 150
RGPLTFAQSF PANVSYNEYQ YAIVQARAAG FIDKVYPLTV GDKVQKGTPL
160 170 180 190 200
LDLTIPDWVE AQSEYLLLRE TGGTATQTEG ILERLRLAGM PEADIRRLIA
210 220 230 240 250
TQKIQTRFTL KAPIDGVITA FDLRAGMNIA KDNVVAKIQG MDPVWVTAAI
260 270 280 290 300
PESIAWLVKD ASQFTLTVPA RPDKTLTIRK WTLLPGVDAA TRTLQLRLEV
310 320 330 340 350
DNADEALKPG MNAWLQLNTA SEPMLLIPSQ ALIDTGSEQR VITVDADGRF
360 370 380 390 400
VPKRVAVFQA SQGVTALRSG LAEGEKVVSS GLFLIDSEAN ISGALERMRS

ESATHAH
Length:407
Mass (Da):44,305
Last modified:February 1, 1997 - v1
Checksum:iE949390000C61FC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40772.1.
U00096 Genomic DNA. Translation: AAC73675.1.
AP009048 Genomic DNA. Translation: BAA35208.1.
PIRiD64790.
RefSeqiNP_415106.1. NC_000913.3.
WP_000717157.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73675; AAC73675; b0574.
BAA35208; BAA35208; BAA35208.
GeneIDi945189.
KEGGiecj:JW0563.
eco:b0574.
PATRICi32116316. VBIEscCol129921_0598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40772.1.
U00096 Genomic DNA. Translation: AAC73675.1.
AP009048 Genomic DNA. Translation: BAA35208.1.
PIRiD64790.
RefSeqiNP_415106.1. NC_000913.3.
WP_000717157.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H94X-ray3.84A/B1-407[»]
3NE5X-ray2.90B/C1-407[»]
3OOCX-ray3.40A/B1-407[»]
3OPOX-ray3.85A/B1-407[»]
3OW7X-ray3.78A/B1-407[»]
3T51X-ray3.90B/C78-407[»]
3T53X-ray3.37B/C78-407[»]
3T56X-ray3.42B/C78-407[»]
4DNRX-ray3.68B/C1-407[»]
4DNTX-ray3.10B/C1-407[»]
4DOPX-ray4.20B/C1-407[»]
ProteinModelPortaliP77239.
SMRiP77239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262993. 129 interactors.
DIPiDIP-9346N.
IntActiP77239. 3 interactors.
STRINGi511145.b0574.

Protein family/group databases

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

Proteomic databases

PaxDbiP77239.
PRIDEiP77239.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73675; AAC73675; b0574.
BAA35208; BAA35208; BAA35208.
GeneIDi945189.
KEGGiecj:JW0563.
eco:b0574.
PATRICi32116316. VBIEscCol129921_0598.

Organism-specific databases

EchoBASEiEB3986.
EcoGeneiEG14235. cusB.

Phylogenomic databases

eggNOGiENOG4105EP1. Bacteria.
ENOG410XPHF. LUCA.
HOGENOMiHOG000126091.
InParanoidiP77239.
KOiK07798.
OMAiTISARQQ.
PhylomeDBiP77239.

Enzyme and pathway databases

BioCyciEcoCyc:G6322-MONOMER.
ECOL316407:JW0563-MONOMER.
MetaCyc:G6322-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP77239.
PROiP77239.

Family and domain databases

InterProiIPR032317. HlyD_D23.
IPR006143. RND_pump_MFP.
[Graphical view]
PfamiPF00529. HlyD. 1 hit.
PF16576. HlyD_D23. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01730. RND_mfp. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCUSB_ECOLI
AccessioniPrimary (citable) accession number: P77239
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 118 of the entry and version 1 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.