Protein Family Models

This N-terminal domain of various bacterial protein families is crucial for the targetting of periplasmic or extracellular proteins to specific regions of the bacterial envelope. AMIN is derived from the N-terminal domain of AmiC, an N-acetylmuramoyl-l-alanine amidase of Escherichia coli which localises to the septal ring during division and plays a key role in the separation of daughter cells. The AMIN domain is present in several protein families besides amidases suggesting that AMIN may represent a general targetting determinant involved in the localisation of periplasmic protein complexes [1]. [1]. 18723522. AMIN domains have a predicted role in localization of diverse periplasmic protein complexes. de Souza RF, Anantharaman V, de Souza SJ, Aravind L, Gueiros-Filho FJ;. Bioinformatics. 2008;24:2423-2426. (from Pfam)

Date:

2024-10-16

This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls. Characterisation of Swiss:P37134. [1]. 1495475. Genetic structure, isolation and characterization of a Bacillus licheniformis cell wall hydrolase. Kuroda A, Sugimoto Y, Funahashi T, Sekiguchi J;. Mol Gen Genet 1992;234:129-137. (from Pfam)

Date:

2024-10-16

The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation [1]. This domain may have a general peptidoglycan binding function. The structure of this domain is known [2]. [1]. 1352512. Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin. Joris B, Englebert S, Chu CP, Kariyama R, Daneo-Moore L, Shockman GD, Ghuysen JM;. FEMS Microbiol Lett 1992;70:257-264. [2]. 10843862. The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). Bateman A, Bycroft M;. J Mol Biol 2000;299:1113-1119. (from Pfam)

Date:

2024-10-29

protein containing domains AMIN, MurNAc-LAA, and LysM

Date:

2019-03-21