Abstract | BACKGROUND:
Peptidoglycan is hydrolyzed by a diverse set of enzymes during bacterial growth, development and cell division. The N1pC/P60 proteins define a family of cell-wall peptidases that are widely represented in various bacterial lineages. Currently characterized members are known to hydrolyze D-gamma-glutamyl-meso-diaminopimelate or N-acetylmuramate- L-alanine linkages. RESULTS: Detailed analysis of the N1pC/P60 peptidases showed that these proteins define a large superfamily encompassing several diverse groups of proteins. In addition to the well characterized P60-like proteins, this superfamily includes the AcmB/LytN and YaeF/YiiX families of bacterial proteins, the amidase domain of bacterial and kinetoplastid glutathionylspermidine synthases (GSPSs), and several proteins from eukaryotes, phages, poxviruses, positive-strand RNA viruses, and certain archaea. The eukaryotic members include lecithin retinol acyltransferase (LRAT), nematode developmental regulator Egl-26, and candidate tumor suppressor H-rev107. These eukaryotic proteins, along with the bacterial YaeF/poxviral G6R family, show a circular permutation of the catalytic domain. We identified three conserved residues, namely a cysteine, a histidine and a polar residue, that are involved in the catalytic activities of this superfamily. Evolutionary analysis of this superfamily shows that it comprises four major families, with diverse domain architectures in each of them. CONCLUSIONS:
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Authors | Vivek Anantharaman, L Aravind |
Journal | Genome biology
(Genome Biol)
Vol. 4
Issue 2
Pg. R11
( 2003)
ISSN: 1474-760X [Electronic] England |
PMID | 12620121
(Publication Type: Journal Article)
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Chemical References |
- Bacterial Proteins
- Peptide Hydrolases
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Topics |
- Amino Acid Sequence
- Bacterial Proteins
(genetics, metabolism)
- Evolution, Molecular
- Models, Molecular
- Molecular Sequence Data
- Multigene Family
(genetics)
- Peptide Hydrolases
(chemistry, genetics, metabolism)
- Phylogeny
- Sequence Alignment
- Sequence Homology, Amino Acid
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