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This family consists of homologs (found only in Borrelia species) of the p13 gene product of Borrelia burgdorferi, which is posttranslationally processed at both ends and modified by an unknown mechanism. This protein is a 13 kDa integral outer membrane protein and exhibits a channel-forming activity. This channel is cation-selective and voltage-independent. The exact structural features of these proteins are not fully elucidated, since conflicting predictions reported P13 to be alpha helical. Single channel and selectivity measurements demonstrated that P13 had no preference for either cations or anions and showed no voltage-gating up to ±100 mV. The localization to the outer membrane and the porin activity leads to the assumption that the protein must form a ß barrel.
Characterization of multiprotein complexes of the Borrelia burgdorferi outer membrane vesicles
J Proteome Res. 2011 Oct 7;10(10):4556-66. doi: 10.1021/pr200395b. Epub 2011 Sep 13.
Specificity and role of the Borrelia burgdorferi CtpA protease in outer membrane protein processing
J Bacteriol. 2011 Oct;193(20):5759-65. doi: 10.1128/JB.05622-11. Epub 2011 Aug 19.
The BBA01 protein, a member of paralog family 48 from Borrelia burgdorferi, is potentially interchangeable with the channel-forming protein P13
J Bacteriol. 2006 Jun;188(12):4207-17. doi: 10.1128/JB.00302-06.
Molecular analysis of the channel-forming protein P13 and its paralogue family 48 from different Lyme disease Borrelia species
Microbiology (Reading). 2004 Mar;150(Pt 3):549-559. doi: 10.1099/mic.0.26728-0.
Elimination of channel-forming activity by insertional inactivation of the p13 gene in Borrelia burgdorferi
J Bacteriol. 2002 Dec;184(24):6811-9. doi: 10.1128/jb.184.24.6811-6819.2002.
P13, an integral membrane protein of Borrelia burgdorferi, is C-terminally processed and contains surface-exposed domains
Infect Immun. 2001 May;69(5):3323-34. doi: 10.1128/IAI.69.5.3323-3334.2001.