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AMIN domain-containing protein
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)
secretin and TonB N-terminal domain-containing protein
This is a short domain found at the N-terminus of the Secretins of the bacterial type II/III secretory system as well as the TonB-dependent receptor proteins. These proteins are involved in TonB-dependent active uptake of selective substrates. (from Pfam)
secretin N-terminal domain-containing protein
This is a short, often repeated, domain found in bacterial type II/III secretory system proteins. All previous NolW-like domains fall into this family. (from Pfam)
Bacterial type II and III secretion system protein
type IV pilus secretin PilQ family protein
type IV pilus secretin PilQ family protein such as Francisella tularensis PilQ, which could function as a pore for exit of the pilus but also as a channel for entry of heme and antimicrobial agents and uptake of transforming DNA, and Haemophilus influenzae competence protein E (ComE), which is a DNA transformation protein
type IV pilus secretin PilQ
PilQ is a secretin (an outer membrane complex formation protein required for secretion) of type 4 pilus assembly. The family also includes proteins of competence system for transformation by exogenous DNA, where the competence system may transport machinery may derive from an incomplete type 4 pilus system. The system also includes HofQ from Escherichia coli, part of an apparent incomplete competence system in which DNA is imported as a carbon source rather than for transformation. PilQ shows homology to secretins of type 2 and type 3 secretion.
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