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Title: 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
 [1];  [2];  [3];  [3];  [1];  [4]
  1. Joint Center for Structural Genomics, San Diego, CA (United States); Sanford-Burnham Medical Research Inst., La Jolla, CA (United States)
  2. European Bioinformatics Inst., Cambridgeshire (United Kingdom). European Molecular Lab., Wellcome Trust Genome Campus
  3. Joint Center for Structural Genomics, San Diego, CA (United States); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
  4. 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
Citation Metrics:
Cited by: 5 works
Citation information provided by
Web of Science

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