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3.A.3.5.5
Cu+, Ag+-ATPase (efflux) (Fan and Rosen, 2002).  There are two metal binding domains (MBDs). The distal N-terminal MBD1 possesses a function analogous to the metallochaperones of related prokaryotic copper resistance systems and is involved in copper transfer to the membrane-integral ion binding sites of CopA. In contrast, the proximal domain MBD2 has a regulatory role by suppressing the catalytic activity of CopA in the absence of copper (Drees et al. 2015). The functions of Me2+ exporters are often supported by chaperone proteins, which scavenge the metal ions from the cytoplasm. A CopA chaperone is expressed in E. coli from the same gene that encodes the transporter (Meydan et al. 2017). Some ribosomes translating copA undergo programmed frameshifting, terminate translation in the -1 frame, and generate the 70 aa-long polypeptide CopA(Z), which helps cells survive toxic copper concentrations. The high efficiency of frameshifting is achieved by the combined stimulatory action of a "slippery" sequence, an mRNA pseudoknot, and the CopA nascent chain. Similar mRNA elements are not only found in the copA genes of other bacteria but are also present in ATP7B, the human homolog of copA, and direct ribosomal frameshifting in vivo (Meydan et al. 2017).

Accession Number:Q59385
Protein Name:ATCU aka CopA aka B0484
Length:834
Molecular Weight:87873.00
Species:Escherichia coli [83333]
Number of TMSs:8
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate Ag+, Cu+

Cross database links:

Genevestigator: Q59385
EchoBASE: EB3035
EcoGene: EG13246
eggNOG: COG2217
HEGENOM: HBG507745
RefSeq: AP_001133.1    NP_415017.1   
Entrez Gene ID: 946106   
Pfam: PF00122    PF00403    PF00702   
BioCyc: EcoCyc:G6260-MONOMER    ECOL168927:B0484-MONOMER   
KEGG: ecj:JW0473    eco:b0484   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005524 F:ATP binding
GO:0004008 F:copper-exporting ATPase activity
GO:0046872 F:metal ion binding
GO:0006754 P:ATP biosynthetic process
GO:0006825 P:copper ion transport
GO:0010273 P:detoxification of copper ion

References (8)

[1] “The complete genome sequence of Escherichia coli K-12.”  Blattner F.R.et.al.   9278503
[2] “Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.”  Hayashi K.et.al.   16738553
[3] “Small genes/gene-products in Escherichia coli K-12.”  Wasinger V.C.et.al.   9868784
[4] “CopA: an Escherichia coli Cu(I)-translocating P-type ATPase.”  Rensing C.et.al.   10639134
[5] “Control of copper homeostasis in Escherichia coli by a P-type ATPase, CopA, and a MerR-like transcriptional activator, CopR.”  Petersen C.et.al.   11167016
[6] “Escherichia coli CopA N-terminal Cys(X)(2)Cys motifs are not required for copper resistance or transport.”  Fan B.et.al.   11500054
[7] “Biochemical characterization of CopA, the Escherichia coli Cu(I)-translocating P-type ATPase.”  Fan B.et.al.   12351646
[8] “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.et.al.   12832075

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSQTIDLTLD GLSCGHCVKR VKESLEQRPD VEQADVSITE AHVTGTASAE QLIETIKQAG 
61:	YDASVSHPKA KPLAESSIPS EALTAVSEAL PAATADDDDS QQLLLSGMSC ASCVTRVQNA 
121:	LQSVPGVTQA RVNLAERTAL VMGSASPQDL VQAVEKAGYG AEAIEDDAKR RERQQETAVA 
181:	TMKRFRWQAI VALAVGIPVM VWGMIGDNMM VTADNRSLWL VIGLITLAVM VFAGGHFYRS 
241:	AWKSLLNGAA TMDTLVALGT GVAWLYSMSV NLWPQWFPME ARHLYYEASA MIIGLINLGH 
301:	MLEARARQRS SKALEKLLDL TPPTARLVTD EGEKSVPLAE VQPGMLLRLT TGDRVPVDGE 
361:	ITQGEAWLDE AMLTGEPIPQ QKGEGDSVHA GTVVQDGSVL FRASAVGSHT TLSRIIRMVR 
421:	QAQSSKPEIG QLADKISAVF VPVVVVIALV SAAIWYFFGP APQIVYTLVI ATTVLIIACP 
481:	CALGLATPMS IISGVGRAAE FGVLVRDADA LQRASTLDTV VFDKTGTLTE GKPQVVAVKT 
541:	FADVDEAQAL RLAAALEQGS SHPLARAILD KAGDMQLPQV NGFRTLRGLG VSGEAEGHAL 
601:	LLGNQALLNE QQVGTKAIEA EITAQASQGA TPVLLAVDGK AVALLAVRDP LRSDSVAALQ 
661:	RLHKAGYRLV MLTGDNPTTA NAIAKEAGID EVIAGVLPDG KAEAIKHLQS EGRQVAMVGD 
721:	GINDAPALAQ ADVGIAMGGG SDVAIETAAI TLMRHSLMGV ADALAISRAT LHNMKQNLLG 
781:	AFIYNSIGIP VAAGILWPFT GTLLNPVVAG AAMALSSITV VSNANRLLRF KPKE