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

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...

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Detalles Bibliográficos
Autores principales: de Souza, Robson Francisco, Anantharaman, Vivek, de Souza, Sandro José, Aravind, L., Gueiros-Filho, Frederico J.
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2008
Materias:
Discovery Notes
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2572700/
https://www.ncbi.nlm.nih.gov/pubmed/18723522
http://dx.doi.org/10.1093/bioinformatics/btn449
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author de Souza, Robson Francisco
Anantharaman, Vivek
de Souza, Sandro José
Aravind, L.
Gueiros-Filho, Frederico J.
author_facet de Souza, Robson Francisco
Anantharaman, Vivek
de Souza, Sandro José
Aravind, L.
Gueiros-Filho, Frederico J.
author_sort de Souza, Robson Francisco
collection PubMed
description 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@iq.usp.br Supplementary information: Supplementary data are available at Bioinformatics online.
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spelling pubmed-25727002008-10-26 AMIN domains have a predicted role in localization of diverse periplasmic protein complexes de Souza, Robson Francisco Anantharaman, Vivek de Souza, Sandro José Aravind, L. Gueiros-Filho, Frederico J. Bioinformatics Discovery Notes 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@iq.usp.br Supplementary information: Supplementary data are available at Bioinformatics online. Oxford University Press 2008-11-01 2008-09-04 /pmc/articles/PMC2572700/ /pubmed/18723522 http://dx.doi.org/10.1093/bioinformatics/btn449 Text en © 2008 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ 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.
spellingShingle Discovery Notes
de Souza, Robson Francisco
Anantharaman, Vivek
de Souza, Sandro José
Aravind, L.
Gueiros-Filho, Frederico J.
AMIN domains have a predicted role in localization of diverse periplasmic protein complexes
title AMIN domains have a predicted role in localization of diverse periplasmic protein complexes
title_full AMIN domains have a predicted role in localization of diverse periplasmic protein complexes
title_fullStr AMIN domains have a predicted role in localization of diverse periplasmic protein complexes
title_full_unstemmed AMIN domains have a predicted role in localization of diverse periplasmic protein complexes
title_short AMIN domains have a predicted role in localization of diverse periplasmic protein complexes
title_sort amin domains have a predicted role in localization of diverse periplasmic protein complexes
topic Discovery Notes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2572700/
https://www.ncbi.nlm.nih.gov/pubmed/18723522
http://dx.doi.org/10.1093/bioinformatics/btn449
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