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Protein

Divalent-cation tolerance protein CutA

Gene

cutA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in resistance toward heavy metals.1 Publication

Cofactori

Cu cation1 PublicationNote: Binds 1 copper ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161CopperCurated
Metal bindingi83 – 831CopperCurated
Metal bindingi84 – 841CopperCurated

GO - Molecular functioni

  • copper ion binding Source: UniProtKB-HAMAP
  • metal ion binding Source: EcoCyc

GO - Biological processi

  • protein homooligomerization Source: UniProtKB
  • response to copper ion Source: EcoCyc
Complete GO annotation...

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG12177-MONOMER.
ECOL316407:JW4097-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Divalent-cation tolerance protein CutA
Alternative name(s):
C-type cytochrome biogenesis protein CycY
Gene namesi
Name:cutA
Synonyms:cutA1, cycY
Ordered Locus Names:b4137, JW4097
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12177. cutA.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Divalent-cation tolerance protein CutAPRO_0000157118Add
BLAST

Proteomic databases

EPDiP69488.
PaxDbiP69488.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi4262693. 8 interactions.
DIPiDIP-47984N.
IntActiP69488. 9 interactions.
STRINGi511145.b4137.

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Beta strandi11 – 2010Combined sources
Helixi21 – 3313Combined sources
Beta strandi38 – 5215Combined sources
Beta strandi55 – 6915Combined sources
Helixi70 – 723Combined sources
Helixi73 – 8311Combined sources
Beta strandi85 – 884Combined sources
Beta strandi91 – 955Combined sources
Helixi101 – 11010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NAQX-ray1.70A/B/C/D/E/F1-112[»]
3AA8X-ray2.30A/B/C1-112[»]
3AA9X-ray2.30A/B/C1-112[»]
3AH6X-ray2.40A/B/C/D/E/F1-112[»]
3X3UX-ray2.09A/B/C/D/E/F1-112[»]
4Y65X-ray1.70A/B/C1-112[»]
4Y6IX-ray1.70A/B/C/D/E/F5-112[»]
ProteinModelPortaliP69488.
SMRiP69488. Positions 7-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP69488.

Family & Domainsi

Sequence similaritiesi

Belongs to the CutA family.Curated

Phylogenomic databases

eggNOGiENOG4105VF7. Bacteria.
COG1324. LUCA.
HOGENOMiHOG000222826.
InParanoidiP69488.
KOiK03926.
OMAiPGMQSVY.
OrthoDBiEOG6KWZ1P.
PhylomeDBiP69488.

Family and domain databases

HAMAPiMF_01160. CutA.
InterProiIPR023700. CutA_bact.
IPR004323. Ion_tolerance_CutA.
IPR011322. N-reg_PII-like_a/b.
[Graphical view]
PANTHERiPTHR23419. PTHR23419. 1 hit.
PfamiPF03091. CutA1. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.

Sequencei

Sequence statusi: Complete.

P69488-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLDEKSSNTA SVVVLCTAPD EATAQDLAAK VLAEKLAACA TLIPGATSLY
60 70 80 90 100
YWEGKLEQEY EVQMILKTTV SHQQALLECL KSHHPYQTPE LLVLPVTHGD
110
TDYLSWLNAS LR
Length:112
Mass (Da):12,331
Last modified:March 15, 2005 - v1
Checksum:i802145EF012DDB69
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241A → R (PubMed:7623667).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77707 Genomic DNA. Translation: CAA54780.1.
Z36905 Genomic DNA. Translation: CAA85374.1.
U14003 Genomic DNA. Translation: AAA97036.1.
U00096 Genomic DNA. Translation: AAC77097.1.
AP009048 Genomic DNA. Translation: BAE78139.1.
PIRiI41027.
RefSeqiNP_418560.1. NC_000913.3.
WP_000883400.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77097; AAC77097; b4137.
BAE78139; BAE78139; BAE78139.
GeneIDi948660.
KEGGiecj:JW4097.
eco:b4137.
PATRICi32123841. VBIEscCol129921_4268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X77707 Genomic DNA. Translation: CAA54780.1.
Z36905 Genomic DNA. Translation: CAA85374.1.
U14003 Genomic DNA. Translation: AAA97036.1.
U00096 Genomic DNA. Translation: AAC77097.1.
AP009048 Genomic DNA. Translation: BAE78139.1.
PIRiI41027.
RefSeqiNP_418560.1. NC_000913.3.
WP_000883400.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NAQX-ray1.70A/B/C/D/E/F1-112[»]
3AA8X-ray2.30A/B/C1-112[»]
3AA9X-ray2.30A/B/C1-112[»]
3AH6X-ray2.40A/B/C/D/E/F1-112[»]
3X3UX-ray2.09A/B/C/D/E/F1-112[»]
4Y65X-ray1.70A/B/C1-112[»]
4Y6IX-ray1.70A/B/C/D/E/F5-112[»]
ProteinModelPortaliP69488.
SMRiP69488. Positions 7-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262693. 8 interactions.
DIPiDIP-47984N.
IntActiP69488. 9 interactions.
STRINGi511145.b4137.

Proteomic databases

EPDiP69488.
PaxDbiP69488.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77097; AAC77097; b4137.
BAE78139; BAE78139; BAE78139.
GeneIDi948660.
KEGGiecj:JW4097.
eco:b4137.
PATRICi32123841. VBIEscCol129921_4268.

Organism-specific databases

EchoBASEiEB2094.
EcoGeneiEG12177. cutA.

Phylogenomic databases

eggNOGiENOG4105VF7. Bacteria.
COG1324. LUCA.
HOGENOMiHOG000222826.
InParanoidiP69488.
KOiK03926.
OMAiPGMQSVY.
OrthoDBiEOG6KWZ1P.
PhylomeDBiP69488.

Enzyme and pathway databases

BioCyciEcoCyc:EG12177-MONOMER.
ECOL316407:JW4097-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP69488.
PROiP69488.

Family and domain databases

HAMAPiMF_01160. CutA.
InterProiIPR023700. CutA_bact.
IPR004323. Ion_tolerance_CutA.
IPR011322. N-reg_PII-like_a/b.
[Graphical view]
PANTHERiPTHR23419. PTHR23419. 1 hit.
PfamiPF03091. CutA1. 1 hit.
[Graphical view]
SUPFAMiSSF54913. SSF54913. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The biogenesis of c-type cytochromes in Escherichia coli requires a membrane-bound protein, DipZ, with a protein disulphide isomerase-like domain."
    Crooke H.R., Cole J.A.
    Mol. Microbiol. 15:1139-1150(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Molecular genetics of a chromosomal locus involved in copper tolerance in Escherichia coli K-12."
    Fong S.-T., Camakaris J., Lee B.T.O.
    Mol. Microbiol. 15:1127-1137(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
    Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transduction."
    Arnesano F., Banci L., Benvenuti M., Bertini I., Calderone V., Mangani S., Viezzoli M.S.
    J. Biol. Chem. 278:45999-46006(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), COFACTOR, SUBUNIT.
    Strain: LE392.

Entry informationi

Entry nameiCUTA_ECOLI
AccessioniPrimary (citable) accession number: P69488
Secondary accession number(s): P36654, Q2M6G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: March 16, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.