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9.B.99 The MipA-interacting Protein (MipA) Family

The MipA family is a large family of outer membrane proteins called OmpV. MltA is designated as a lytic transglycosylase, and MipA may be a scaffolding protein in E. coli (Vollmer et al., 1999). Synthesis of the E. coli MipA is suppressed by glucose (Yang et al., 2011). It is related to the DUF2141 family. One member, YiaT of E. coli, has been considered to be a porin (Vinson et al., 2010). It may have ~10 TM β-strands.

References associated with 9.B.99 family:

Li, H., D.F. Zhang, X.M. Lin, and X.X. Peng. (2015). Outer membrane proteomics of kanamycin-resistant Escherichia coli identified MipA as a novel antibiotic resistance-related protein. FEMS Microbiol. Lett. 362:. 25940639
van Straaten, K.E., B.W. Dijkstra, W. Vollmer, and A.M. Thunnissen. (2005). Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold. J. Mol. Biol. 352: 1068-1080. 16139297
Vinson, H.M., A. Gautam, S. Olet, P.S. Gibbs, and R. Barigye. (2010). Molecular analysis of porin gene transcription in heterogenotypic multidrug-resistant Escherichia coli isolates from scouring calves. J Antimicrob Chemother 65: 1926-1935. 20639525
Vollmer, W., M. von Rechenberg, and J.V. Höltje. (1999). Demonstration of molecular interactions between the murein polymerase PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of Escherichia coli. J. Biol. Chem. 274: 6726-6734. 10037771
Yang, J.N., C. Wang, C. Guo, X.X. Peng, and H. Li. (2011). Outer membrane proteome and its regulation networks in response to glucose concentration changes in Escherichia coli. Mol Biosyst 7: 3087-3093. 21850335