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This family consists of several bacterial copper resistance proteins. Copper is essential as it serves as co-factor for a variety of enzymes. However, excess of copper is toxic and leads to radical formation and oxidation of biomolecules. CopB serves to extrude copper when it approaches toxic levels. The protein CopB is located in the outer membrane, and seems to form a ß-barrel. The relatively small N-terminal domain is predicted to be periplasmic, suggesting a structural resemblance with TonB dependent receptors, however no sequence homology is apparent.
Tetrathiomolybdate inhibition of the Enterococcus hirae CopB copper ATPase
FEBS Lett. 2001 Nov 2;507(3):367-70. doi: 10.1016/s0014-5793(01)03009-5.
Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins
Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):8915-9. doi: 10.1073/pnas.88.20.8915.
Characterization of chromosomal homologs of the plasmid-borne copper resistance operon of Pseudomonas syringae
J Bacteriol. 1993 Jul;175(14):4492-8. doi: 10.1128/jb.175.14.4492-4498.1993.
Molecular characterization of copper resistance genes from Xanthomonas citri subsp. citri and Xanthomonas alfalfae subsp. citrumelonis
Appl Environ Microbiol. 2011 Jun;77(12):4089-96. doi: 10.1128/AEM.03043-10. Epub 2011 Apr 22.