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

N-acetylmuramoyl-L-alanine amidase hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides

Date:

2022-06-08

Gene:

amiC

Date:

2022-02-18