Document Detail


Long-chain N-acyl amino acid synthases are linked to the putative PEP-CTERM/exosortase protein-sorting system in Gram-negative bacteria.
MedLine Citation:
PMID:  21840974     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Jeffrey W Craig; Marisa A Cherry; Sean F Brady
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2011-08-12
Journal Detail:
Title:  Journal of bacteriology     Volume:  193     ISSN:  1098-5530     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2011 Oct 
Date Detail:
Created Date:  2011-09-28     Completed Date:  2011-11-15     Revised Date:  2012-04-02    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5707-15     Citation Subset:  IM    
Affiliation:
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.:
GENBANK/JF429404;  JF429405;  JF429406;  JF429407;  JF429408;  JF429409;  JF429410;  JF429411;  JF429412;  JF429413;  JF429414;  JF429415;  JF429416;  JF429417
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MeSH Terms
Descriptor/Qualifier:
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:
GM07739/GM/NIGMS NIH HHS; GM077516/GM/NIGMS NIH HHS; //Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Bacterial Proteins; EC 2.3.2.-/Aminoacyltransferases; EC 6.1.1.-/Amino Acyl-tRNA Synthetases

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