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2.A.4.7.10
Cobalt/zinc resistance protein B, CzrB, of 291 aas and 6 TMSs.  It has a cytosolic extramembranal C-terminus. This 92-residue fragment may function independently of the full-length integral membrane protein. X-ray analyses of this fragment to 2.2 A resolution with and 1.7 A without zinc ions have been solved. The former has at least two zinc ions bound per monomer (Höfer et al. 2007).  Full-length variants of CzrB in the apo and zinc-loaded states were generated by homology modeling with the Zn2+/H+ antiporter YiiP. The model suggests a way in which zinc binding to the cytoplasmic fragment creates a docking site to which a metallochaperone can bind for delivery and transport of zinc. A proposal was advanced that it functions as a metallochaperone and regulates the zinc-transporting activity of the full-length protein. The latter requires that zinc binding becomes uncoupled from the creation of a metallochaperone-docking site on CzrB (Cherezov et al. 2008).

Accession Number:Q8VLX7
Protein Name:CzrB protein
Length:291
Molecular Weight:31234.00
Species:Thermus thermophilus [274]
Number of TMSs:6
Substrate Co2+, Zn2+

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FASTA formatted sequence
1:	MAEGAARLSL VVALLVLGLK AFAYLLTGSV ALLSDALESL VNVAAALAAL LALRVARKPP 
61:	DQNHPFGHTK AEYVSAVLEG VLVVLAALWI AREALPRLLH PVPLEGLGLG LGVSLLASLL 
121:	NGLLAYHLLK EGRRHRSPAL TADGYHVLSD VLTSLGVVLG VGLAGLTGLW VLDPLLALAV 
181:	AGQILFLGYR IVRESVGGLM DEGLPPEEVE RIRAFLQERI RGRALEVHDL KTRRAGPRSF 
241:	LEFHLVVRGD TPVEEAHRLC DELERALAQA FPGLQATIHV EPEGERKRTN P