Structure and sequence analyses of Bacteroides proteins BVU_4064 and BF1687 reveal presence of two novel predominantly-beta domains, predicted to be involved in lipid and cell surface interactions
Journal Article
·
· BMC Bioinformatics
- Joint Center for Structural Genomics, San Diego, CA (United States); Sanford-Burnham Medical Research Inst., La Jolla, CA (United States)
- European Bioinformatics Inst., Cambridgeshire (United Kingdom). European Molecular Lab., Wellcome Trust Genome Campus
- Joint Center for Structural Genomics, San Diego, CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
- National Library of Medicine, Bethesda, MD (United States)
N-terminal domains of BVU_4064 and BF1687 proteins from Bacteroides vulgatus and Bacteroides fragilis respectively are members of the Pfam family PF12985 (DUF3869). Proteins containing a domain from this family can be found in most Bacteroides species and, in large numbers, in all human gut microbiome samples. Both BVU_4064 and BF1687 proteins have a consensus lipobox motif implying they are anchored to the membrane, but their functions are otherwise unknown. The C-terminal half of BVU_4064 is assigned to protein family PF12986 (DUF3870); the equivalent part of BF1687 was unclassified.
- Research Organization:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- AC02-76SF00515
- OSTI ID:
- 1208934
- Journal Information:
- BMC Bioinformatics, Vol. 16, Issue 1; ISSN 1471-2105
- Publisher:
- BioMed CentralCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Cited by: 5 works
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