| Long-chain N-acyl amino acid synthases are linked to the putative PEP-CTERM/exosortase protein-sorting system in Gram-negative bacteria. | |
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MedLine Citation:
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PMID: 21840974 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Clones that encode the biosynthesis of long-chain N-acyl amino acids are frequently recovered from activity-based screens of soil metagenomic libraries. Members of a diverse set of enzymes referred to as N-acyl amino acid synthases are responsible for the production of all metagenome-derived N-acyl amino acids characterized to date. Based on the frequency at which N-acyl amino acid synthase genes have been identified from metagenomic samples, related genes are expected to be common throughout the global bacterial metagenome. Homologs of metagenome-derived N-acyl amino acid synthase genes are scarce, however, within the sequenced genomes of cultured bacterial species. Toward the goal of understanding the role(s) played by N-acyl amino acids in environmental bacteria, we looked for conserved genetic features that are positionally linked to metagenome-derived N-acyl amino acid synthase genes. This analysis revealed that N-acyl amino acid synthase genes are frequently found adjacent to genes predicted to encode PEP-CTERM motif-containing proteins and, in some cases, other conserved elements of the PEP-CTERM/exosortase system. Although relatively little is known about the PEP-CTERM/exosortase system, its core components are believed to represent the putative Gram-negative equivalent of the LPXTG/sortase protein-sorting system of Gram-positive bacteria. During the course of this investigation, we were able to provide evidence that an uncharacterized family of hypothetical acyltransferases, which had previously been linked to the PEP-CTERM/exosortase system by bioinformatics, is a new family of N-acyl amino acid synthases that is widely distributed among the PEP-CTERM/exosortase system-containing Proteobacteria. |
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Authors:
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Jeffrey W Craig; Marisa A Cherry; Sean F Brady |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2011-08-12 |
Journal Detail:
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Title: Journal of bacteriology Volume: 193 ISSN: 1098-5530 ISO Abbreviation: J. Bacteriol. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-09-28 Completed Date: 2011-11-15 Revised Date: 2012-04-02 |
Medline Journal Info:
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Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: United States |
Other Details:
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Languages: eng Pagination: 5707-15 Citation Subset: IM |
Affiliation:
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Laboratory of Genetically Encoded Small Molecules, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/JF429404; JF429405; JF429406; JF429407; JF429408; JF429409; JF429410; JF429411; JF429412; JF429413; JF429414; JF429415; JF429416; JF429417 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Motifs Amino Acid Sequence Amino Acids / biosynthesis*, chemistry Amino Acyl-tRNA Synthetases / chemistry, genetics, metabolism* Aminoacyltransferases / chemistry, genetics, metabolism* Bacterial Proteins / chemistry*, genetics, metabolism* Gram-Negative Bacteria / chemistry, classification, enzymology*, genetics Metagenome Molecular Sequence Data Phylogeny Protein Transport Soil Microbiology* |
| Grant Support | |
ID/Acronym/Agency:
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GM07739/GM/NIGMS NIH HHS; GM077516/GM/NIGMS NIH HHS; //Howard Hughes Medical Institute |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Bacterial Proteins; EC 2.3.2.-/Aminoacyltransferases; EC 6.1.1.-/Amino Acyl-tRNA Synthetases |
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