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Bioinformatics Advance Access originally published online on August 21, 2008
Bioinformatics 2008 24(21):2423-2426; doi:10.1093/bioinformatics/btn449
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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

Robson Francisco de Souza 1,2,{dagger}, Vivek Anantharaman 3,{dagger}, Sandro José de Souza 2, L. Aravind 3 and Frederico J. Gueiros-Filho 1,*

1Departamento de Bioquímica, Universidade de São Paulo, São Paulo, Brazil, 2Ludwig Institute for Cancer Research, Sío Paulo Branch, Sío Paulo, Brazil and 3National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA

*To whom correspondence should be addressed.


  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.

Contact: fgueiros{at}iq.usp.br

Supplementary information: Supplementary data are available at Bioinformatics online.

{dagger}The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.

Associate Editor: Dmitrij Frishman

Received on March 29, 2008; revised on August 8, 2008; accepted on August 19, 2008

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