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3.A.3.5.7
Cu+-Ag+-ATPase (efflux), CopA of 804 aas. Exhibits maximal activity at 75˚C (Cattoni et al., 2007). The 3-D structure of the ATP-binding domain has been solved (2HC8_A) (functions with the Cu+ chaperone, CopZ; 130aas) (González-Guerrero and Argüello, 2008). This protein has both N- and C- terminal metal binding domains (MBDs). The N-MBD exhibits a conserved ferredoxin-like fold, binds metals to CXXC, and regulates turnover. The C-MBD interacts with the ATP-binding (ATPB) domain and the actuator (A) domain (Agarwal et al., 2010). Cysteine is a non-essential activator of CopA, interacting with the cytoplasmic side of the enzyme in the E1 form (Yang et al. 2007).

Accession Number:O29777
Protein Name:CopA aka PaeS aka AF0473
Length:804
Molecular Weight:86432.00
Species:Archaeoglobus fulgidus [2234]
Number of TMSs:8
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate copper(1+), silver(1+)

Cross database links:

DIP: DIP-46021N
RefSeq: NP_069309.1   
Entrez Gene ID: 1483690   
Pfam: PF00122    PF00403    PF00702   
BioCyc: AFUL224325:AF_0473-MONOMER   
KEGG: afu:AF0473   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005524 F:ATP binding
GO:0005507 F:copper ion binding
GO:0004008 F:copper-exporting ATPase activity
GO:0006754 P:ATP biosynthetic process
GO:0006825 P:copper ion transport

References (7)

[1] “The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus.”  Klenk H.-P.et.al.   9389475
[2] “Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus.”  Mandal A.K.et.al.   11756450
[3] “Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus.”  Arguello J.M.et.al.   12763798
[4] “Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA.”  Mandal A.K.et.al.   12974640
[5] “Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites.”  Gonzalez-Guerrero M.et.al.   18417453
[6] “Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-ATPase.”  Sazinsky M.H.et.al.   16906753
[7] “Structure of the ATP binding domain from the Archaeoglobus fulgidus Cu+-ATPase.”  Sazinsky M.H.et.al.   16495228
Structure:
2B8E   2HC8   2VOY   3A1C   3A1D   3A1E   3FRY   3J08   3J09      [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MVKDTYISSA SKTPPMERTV RVTGMTCAMC VKSIETAVGS LEGVEEVRVN LATETAFIRF 
61:	DEKRIDFETI KRVIEDLGYG VVDEQAAVSA EVEHLSRMKR KLYVAAFAGV LLLFLAHFIS 
121:	LPYEDFVQLL IALPAIFYSG SSIFKAAFSA LRRRTLNMDV MYSMGVGAAF LASVLSTAGV 
181:	LPREYSFYET SVLLLAFLLL GRTLEARAKS RTGEAIKKLV GLQAKTAVVI RDGKEIAVPV 
241:	EEVAVGDIVI VRPGEKIPVD GVVVEGESYV DESMISGEPV PVLKSKGDEV FGATINNTGV 
301:	LKIRATRVGG ETLLAQIVKL VEDAMGSKPP IQRLADKVVA YFIPTVLLVA ISAFIYWYFI 
361:	AHAPLLFAFT TLIAVLVVAC PCAFGLATPT ALTVGMGKGA ELGILIKNAD ALEVAEKVTA 
421:	VIFDKTGTLT KGKPEVTDLV PLNGDERELL RLAAIAERRS EHPIAEAIVK KALEHGIELG 
481:	EPEKVEVIAG EGVVADGILV GNKRLMEDFG VAVSNEVELA LEKLEREAKT AVIVARNGRV 
541:	EGIIAVSDTL KESAKPAVQE LKRMGIKVGM ITGDNWRSAE AISRELNLDL VIAEVLPHQK 
601:	SEEVKKLQAK EVVAFVGDGI NDAPALAQAD LGIAVGSGSD VAVESGDIVL IRDDLRDVVA 
661:	AIQLSRKTMS KIKQNIFWAL IYNVILIPAA AGLLYPIFGV VFRPEFAGLA MAMSSVSVVA 
721:	NSLLLRNYVP PIRRGGDSVE KIVLELSGLS CHHCVARVKK ALEEAGAKVE KVDLNEAVVA 
781:	GNKEDVDKYI KAVEAAGYQA KLRS