AMIN domains have a predicted role in localization of diverse periplasmic protein complexes.

Bioinformatics
Robson Francisco de SouzaFrederico J Gueiros-Filho

Abstract

We describe AMIN (Amidase N-terminal domain), a novel protein domain found specifically in bacterial periplasmic proteins. AMIN domains are widely distributed among peptidoglycan hydrolases and transporter protein families. Based on experimental data, contextual information and phyletic profiles, we suggest that AMIN domains mediate the targeting of periplasmic or extracellular proteins to specific regions of the bacterial envelope.

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Citations

Mar 27, 2015·Environmental Microbiology·Tiffany L LeightonLori L Burrows
Oct 24, 2020·Proceedings of the National Academy of Sciences of the United States of America·Romain MercierTâm Mignot

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Software Mentioned

BLAST
JPRED
KALIGN
HMMER2
hmm
Phyre
BLASTCLUST
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PSI

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Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.

Bacterial Cell Wall Structure

Bacterial cell walls are made of peptidoglycan (also called murein), which is made from polysaccharide chains cross-linked by unusual peptides containing D-amino acids. Here is the latest research on bacterial cell wall structures.