Protein Family Models

This domain is found in the UvrB protein where it interacts with the UvrA protein [2]. [1]. 18158267. Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding. Pakotiprapha D, Inuzuka Y, Bowman BR, Moolenaar GF, Goosen N, Jeruzalmi D, Verdine GL;. Mol Cell. 2008;29:122-133. [2]. 19287003. A structural model for the damage-sensing complex in bacterial nucleotide excision repair. Pakotiprapha D, Liu Y, Verdine GL, Jeruzalmi D;. J Biol Chem. 2009;284:12837-12844. (from Pfam)

Date:

2024-10-16

This is the N-terminal, transmembrane, domain of the transglycosylases ()penicillin-binding proteins), the multi-domain membrane proteins essential for cell wall synthesis that are targeted by penicillin antibiotics. The TM domain is a single helix, several of whose residues lie in close proximity to hydrophobic residues in the TGT domain. The TM helix seems to be necessary for stabilizing the protein-membrane interaction, and the resulting orientation limits the interaction between PBPb1 and lipid II in the membrane in a 2D lateral diffusion fashion [1]. [1]. 19458048. Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli. Sung MT, Lai YT, Huang CY, Chou LY, Shih HW, Cheng WC, Wong CH, Ma C;. Proc Natl Acad Sci U S A. 2009;106:8824-8829. (from Pfam)

Date:

2024-10-16

UB2H is the second domain of the transglycosylases, or penicillin-binding proteins PBP1bs)), the multi-domain membrane proteins essential for cell wall synthesis that are targeted by penicillin antibiotics. The exact function of the UB2H domain is uncertain, but it may act as the binding component of PBP1b with different binding partners, or it may participate in the regulation between DNA repair and/or synthesis and cell wall formation during the bacterial cell cycle [1]. [1]. 19458048. Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli. Sung MT, Lai YT, Huang CY, Chou LY, Shih HW, Cheng WC, Wong CH, Ma C;. Proc Natl Acad Sci U S A. 2009;106:8824-8829. (from Pfam)

Date:

2024-10-16

The penicillin-binding proteins are bifunctional proteins consisting of transglycosylase and transpeptidase in the N- and C-terminus respectively [1]. The transglycosylase domain catalyses the polymerisation of murein glycan chains ([4]). [1]. 9244263. Topographical and functional investigation of Escherichia coli penicillin-binding protein 1b by alanine stretch scanning mutagenesis. F. Lefevre, M. H. Remy & J. M. Masson;. J Bacteriol 1997;179:4761-4767. [2]. 9614972. X-ray studies of enzymes that interact with penicillins. Kelly JA, Kuzin AP, Charlier P, Fonze E;. Cell Mol Life Sci 1998;54:353-358. [3]. 8830253. Monofunctional biosynthetic peptidoglycan transglycosylases. Spratt BG, Zhou J, Taylor M, Merrick MJ;. Mol Microbiol 1996;19:639-640. [4]. 12867450. The glycosyltransferase domain of penicillin-binding protein 2a from Streptococcus pneumoniae catalyzes the polymerization of murein glycan chains. Di Guilmi AM, Dessen A, Dideberg O, Vernet T;. J Bacteriol 2003;185:4418-4423. (from Pfam)

Date:

2024-10-16

The active site serine (residue 337 in Swiss:P14677) is conserved in all members of this family. [1]. 8605631. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Pares S, Mouz N, Petillot Y, Hakenbeck R, Dideberg O. Nat Struct Biol 1996;3:284-289. (from Pfam)

Date:

2024-10-16

Bacterial that synthesize a cell wall of peptidoglycan (murein) generally have several transglycosylases and transpeptidases for the task. This family consists of a particular bifunctional transglycosylase/transpeptidase in E. coli and other Proteobacteria, designated penicillin-binding protein 1B.

Gene:

mrcB

Date:

2021-08-23

penicillin-binding protein 1B is a bifunctional transpeptidases/transglycosylase that catalyzes synthesis of cross-linked peptidoglycan from the lipid intermediates in cell wall formation

Date:

2017-05-18

Gene:

mrcB

Date:

2024-06-27