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Q59385 (COPA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Copper-exporting P-type ATPase A
EC=3.6.3.n1
Gene names
Name:copA
Synonyms:ybaR
Ordered Locus Names:b0484, JW0473
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length834 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in copper export. May also be involved in silver export. Ref.10

Catalytic activity

ATP + H2O + Cu+(In) = ADP + phosphate + Cu+(Out).

Enzyme regulation

Phosphorylation is inhibited by vanadate and sensitive to KOH and hydroxylamine. Phosphorylation is Cu+-dependent. Ref.9

Subcellular location

Cell membrane; Multi-pass membrane protein Probable.

Induction

Transcriptionally regulated by CueR in response to Cu+ or Ag+ ions. Ref.9

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 2 HMA domains.

Biophysicochemical properties

Kinetic parameters:

KM=1.5 µM for copper Ref.9

KM=0.5 mM for ATP

Vmax=0.19 µmol/min/mg enzyme (in the presence of Cu+)

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 834833Copper-exporting P-type ATPase A
PRO_0000046320

Regions

Transmembrane187 – 20721Helical; Potential
Transmembrane218 – 23821Helical; Potential
Transmembrane254 – 27421Helical; Potential
Transmembrane284 – 30421Helical; Potential
Transmembrane438 – 45821Helical; Potential
Transmembrane464 – 48421Helical; Potential
Transmembrane779 – 79921Helical; Potential
Transmembrane801 – 82121Helical; Potential
Domain4 – 6562HMA 1
Domain100 – 16364HMA 2

Sites

Active site52314-aspartylphosphate intermediate Probable
Metal binding141Copper Potential
Metal binding171Copper Potential
Metal binding1101Copper Potential
Metal binding1131Copper Potential
Metal binding7201Magnesium By similarity
Metal binding7241Magnesium By similarity

Experimental info

Mutagenesis8 – 150143Missing: Loss of activity.
Mutagenesis141C → A: No effect. Ref.8
Mutagenesis171C → A: No effect. Ref.8
Mutagenesis1101C → A: No effect. Ref.8
Mutagenesis1131C → A: No effect. Ref.8
Mutagenesis4791C → A: Loss of copper resistance, transport and phosphoenzyme formation. Ref.9
Mutagenesis4811C → A or H: Loss of copper resistance, transport and phosphoenzyme formation. Ref.9
Sequence conflict162 – 18120EAIED…TAVAT → KRLKMTLNAASASKKPPSLA in AAB02268. Ref.1
Sequence conflict5081A → R in AAB02268. Ref.1
Sequence conflict5761Q → R in AAB02268. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59385 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: CF84A18FE208E6F6

FASTA83487,873
        10         20         30         40         50         60 
MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG 

        70         80         90        100        110        120 
YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA 

       130        140        150        160        170        180 
LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA 

       190        200        210        220        230        240 
TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS 

       250        260        270        280        290        300 
AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH 

       310        320        330        340        350        360 
MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE 

       370        380        390        400        410        420 
ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR 

       430        440        450        460        470        480 
QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP 

       490        500        510        520        530        540 
CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT 

       550        560        570        580        590        600 
FADVDEAQAL RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL 

       610        620        630        640        650        660 
LLGNQALLNE QQVGTKAIEA EITAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ 

       670        680        690        700        710        720 
RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKHLQS EGRQVAMVGD 

       730        740        750        760        770        780 
GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LHNMKQNLLG 

       790        800        810        820        830 
AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE

« Hide

References

« Hide 'large scale' references
[1]Das S., Chuang E., Vulpe C., Goldman J., Gitschier J.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Small genes/gene-products in Escherichia coli K-12."
Wasinger V.C., Humphery-Smith I.
FEMS Microbiol. Lett. 169:375-382(1998) [PubMed: 9868784] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Strain: K12.
[6]"CopA: an Escherichia coli Cu(I)-translocating P-type ATPase."
Rensing C., Fan B., Sharma R., Mitra B., Rosen B.P.
Proc. Natl. Acad. Sci. U.S.A. 97:652-656(2000) [PubMed: 10639134] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Control of copper homeostasis in Escherichia coli by a P-type ATPase, CopA, and a MerR-like transcriptional activator, CopR."
Petersen C., Moeller L.B.
Gene 261:289-298(2000) [PubMed: 11167016] [Abstract]
Cited for: CHARACTERIZATION.
Strain: K12.
[8]"Escherichia coli CopA N-terminal Cys(X)(2)Cys motifs are not required for copper resistance or transport."
Fan B., Grass G., Rensing C., Rosen B.P.
Biochem. Biophys. Res. Commun. 286:414-418(2001) [PubMed: 11500054] [Abstract]
Cited for: MUTAGENESIS OF CYS-14; CYS-17; CYS-110 AND CYS-113.
[9]"Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase."
Fan B., Rosen B.P.
J. Biol. Chem. 277:46987-46992(2002) [PubMed: 12351646] [Abstract]
Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, PHOSPHORYLATION, MUTAGENESIS OF CYS-479 AND CYS-481.
Strain: K12.
[10]"Measurement of cytoplasmic copper, silver, and gold with a lux biosensor shows copper and silver, but not gold, efflux by the CopA ATPase of Escherichia coli."
Stoyanov J.V., Magnani D., Solioz M.
FEBS Lett. 546:391-394(2003) [PubMed: 12832075] [Abstract]
Cited for: FUNCTION IN SILVER EXPORT.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U58330 Genomic DNA. Translation: AAB02268.1.
U82664 Genomic DNA. Translation: AAB40238.1.
U00096 Genomic DNA. Translation: AAC73586.1.
AP009048 Genomic DNA. Translation: BAE76263.1.
PIRC64779.
RefSeqNP_415017.1. NC_000913.2.

3D structure databases

ProteinModelPortalQ59385.
SMRQ59385. Positions 1-833.
ModBaseSearch...

Protein-protein interaction databases

IntActQ59385. 6 interactions.

Protein family/group databases

TCDB3.A.3.5.5. P-type ATPase (P-ATPase) superfamily.

Proteomic databases

PRIDEQ59385.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000001759; EBESCP00000001759; EBESCG00000001449.
EBESCT00000015944; EBESCP00000015235; EBESCG00000015004.
GeneID946106.
GenomeReviewsGene locus JW0473 in contig AP009048_GR.
Gene locus b0484 in contig U00096_GR.
KEGGecj:JW0473.
eco:b0484.
PATRIC32116127. VBIEscCol129921_0505.

Organism-specific databases

EchoBASEEB3035.
EcoGeneEG13246. copA.

Phylogenomic databases

eggNOGCOG2217.
GeneTreeEBGT00050000009754.
HOGENOMHBG507745.
OMAINGMSCA.
PhylomeDBQ59385.
ProtClustDBPRK10671.

Enzyme and pathway databases

BioCycEcoCyc:G6260-MONOMER.

Gene expression databases

GenevestigatorQ59385.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR000695. ATPase_P-typ_H-transp.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
IPR000150. Hypothet_cof.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK01533.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 2 hits.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 2 hits.
TIGRFAMsTIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOPA_ECOLI
AccessionPrimary (citable) accession number: Q59385
Secondary accession number(s): P78245, Q2MBU3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 113 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents