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polysaccharide biosynthesis C-terminal domain-containing protein
This family represents the C-terminal integral membrane region of polysaccharide biosynthesis proteins. (from Pfam)
lipid II flippase MurJ
Peptidoglycan synthesis (PG) biosynthesis involves the formation of peptidoglycan precursor lipid II (undecaprenyl-pyrophosphate-linked N-acetyl glucosamine-N-acetyl muramic acid-pentapeptide) on the cytosolic face of the cell membrane. Lipid II is then translocated across the membrane and its glycopeptide moiety becomes incorporated into the growing cell wall mesh. MviN, renamed as MurJ, is a lipid II flippase essential for cell wall peptidoglycan synthesis [1, 2]. MurJ belongs to the MVF (mouse virulence factor) family of MOP superfamily transporters, which also includes the MATE (multidrug and toxic compound extrusion) transporter and eukaryotic OLF (oligosaccharidyl-lipid flippase) families. In addition to the canonical MOP transporter core consisting of 12 transmembrane helices (TMs), MurJ has two additional C-terminal TMs (13 and 14) of unknown function. Structural analysis indicates that the N lobe (TMs 1-6) and C lobe (TMs 7-14) are arranged in an inward-facing N-shape conformation, rather than the outward-facing V-shape conformation observed in all existing MATE transporter structures. Furthermore, a hydrophobic groove is formed by two C-terminal transmembrane helices, which leads into a large central cavity that is mostly cationic. Mutagenesis studies, revealed a solvent-exposed cavity that is essential for function. Mutation of conserved residues (Ser17, Arg18, Arg24, Arg52, and Arg255) at the proximal site failed to complement MurJ function, consistent with the idea that these residues are important for recognizing the diphosphate and/or sugar moieties of lipid II. It has also been suggested that the chloride i. TRUNCATED at 1650 bytes (from Pfam)
MATE family efflux transporter
MATE (Multi Antimicrobial Extrusion), 2.A.66.1 in Transporter Classification Database, is a widely distributed transporter family that includes both human proteins and bacterial antibiotic resistance efflux transporters.
oligosaccharide flippase family protein
Members of this family are integral membrane proteins [1]. Many members of the family are implicated in production of polysaccharide. The family includes RfbX part of the O antigen biosynthesis operon [2]. The family includes SpoVB from Bacillus subtilis Swiss:Q00758, which is involved in spore cortex biosynthesis [3]. [1]. 8118055. Analysis of the Rhizobium meliloti genes exoU, exoV, exoW, exoT, and exoI involved in exopolysaccharide biosynthesis and nodule invasion: exoU and exoW probably encode glucosyltransferases. Becker A, Kleickmann A, Kuster H, Keller M, Arnold W, Puhler A;. Mol Plant Microbe Interact. 1993;6:735-744. [2]. 7517390. Genetic analysis of the O-specific lipopolysaccharide biosynthesis region (rfb) of Escherichia coli K-12 W3110: identification of genes that confer group 6 specificity to Shigella flexneri serotypes Y and 4a. Yao Z, Valvano MA;. J Bacteriol 1994;176:4133-4143. [3]. 1744050. Cloning, characterization, and expression of the spoVB gene of Bacillus subtilis. Popham DL, Stragier P;. J Bacteriol 1991;173:7942-7949. (from Pfam)
polysaccharide biosynthesis protein
polysaccharide biosynthesis protein similar to Bacillus subtilis sporulation protein YkvU, Lipid II flippase MurJ, and uncharacterized membrane protein YabM, which are involved in cell wall metabolism; belongs to the multidrug and toxic compound extrusion (MATE)-like transporter superfamily
stage V sporulation protein B
SpoVB is the stage V sporulation protein B of the bacterial endopore formation program in Bacillus subtilis and various other Firmcutes. It is nearly universal among endospore-formers. Paralogs with rather high sequence similarity to SpoVB exist, including YkvU in B. subtilis and a number of proteins in the genus Clostridium. Member sequences for the seed alignment and cutoff scores for the resulting HMM were chosen to select those proteins, no more than one to a genome, closest to B. subtilis SpoVB in a neighbor joining tree.
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