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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:O29901
Protein Name:Copper chaperone CopZ
Length:204
Molecular Weight:22588.00
Species:Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) [224325]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate Cu+, Ag+

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Structure:
2HU9     

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FASTA formatted sequence
1:	MMRCPECSTE GWRVLPLTVG AHVKEGLWSK IKGDFYFCSL ESCEVVYFNE QTVFRKGELK 
61:	TRVGVKEREE PKPVCYCNRV TEKMLLEAAE KFGKEKAVEI TGAGKGKWCV VTNPSGRCCH 
121:	WHLERLGFPV GGEKKAAKRV EIKLDGLTCM GCVSAVKAAL EEAGANVVEI GLDRAVVEVD 
181:	EEAELQKLVE AVEGAGYSAR LEKR