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9.B.98 The DUF95 (DUF95) Family

The DUF95 family consists of proteins that exhibit 4, 5 or 6 TMSs. They usually contain about 200 aas but can have N-terminal hydrophilic extensions of >100 aas. Members are found in archaea and bacteria. DUF95 domains are found in a few ABC transport systems such as 3.A.1.156.1 where the system may have an extra 4 TMS subunit.  Another ABC transport system having this domain is the 18 TMS protein (3.A.1.144.4) which has a 6 + 6 + 6 arrangement, and the last 6 TMSs correspond to the DUF95 domain.   It has been suggested that DUF95 proteins are auxilary subunits of bacteriocin ABC exporters (van Belkum et al., 2011). These proteins may be distantly related to TatC (2.A.64).

References associated with 9.B.98 family:

Chastanet, A. and R. Losick. (2007). Engulfment during sporulation in Bacillus subtilis is governed by a multi-protein complex containing tandemly acting autolysins. Mol. Microbiol. 64: 139-152. 17376078
Gutierrez, J., R. Smith, and K. Pogliano. (2010). SpoIID-mediated peptidoglycan degradation is required throughout engulfment during Bacillus subtilis sporulation. J. Bacteriol. 192: 3174-3186. 20382772
Kemperman, R., M. Jonker, A. Nauta, O.P. Kuipers, and J. Kok. (2003). Functional analysis of the gene cluster involved in production of the bacteriocin circularin A by Clostridium beijerinckii ATCC 25752. Appl. Environ. Microbiol. 69: 5839-5848. 14532033
Labay, V., R.M. Weichert, T. Makishima, and A.J. Griffith. (2010). Topology of transmembrane channel-like gene 1 protein. Biochemistry 49: 8592-8598. 20672865
van Belkum, M.J., L.A. Martin-Visscher, and J.C. Vederas. (2011). Structure and genetics of circular bacteriocins. Trends Microbiol. 19: 411-418. 21664137