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YcaO cyclodehydratase C-terminal domain
This is the proline-rich C-terminal domain found in ribosomal protein S12 methylthiotransferase accessory factor YcaO. It has been shown to be involved in both C protein recognition and cyclodehydration. The C-terminal domain resembles a tetratricopeptide repeat that mediates dimerization [1]. [1]. 25129028. Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis. Dunbar KL, Chekan JR, Cox CL, Burkhart BJ, Nair SK, Mitchell DA;. Nat Chem Biol. 2014;10:823-829. (from Pfam)
OsmC family protein
Osmotically inducible protein C (OsmC) (Swiss:P23929) is a stress -induced protein found in E. Coli. This family also contains a organic hydroperoxide detoxification protein (Swiss:O68390) that has a novel pattern of oxidative stress regulation [1]. [1]. 9573147. Identification and characterization of a new organic hydroperoxide resistance (ohr) gene with a novel pattern of oxidative stress regulation from Xanthomonas campestris pv. phaseoli. Mongkolsuk S, Praituan W, Loprasert S, Fuangthong M, Chamnongpol S;. J Bacteriol 1998;180:2636-2643. (from Pfam)
YcaO-like family protein
YcaO is an ATP- an Mg2+-binding protein involved in the peptidic biosynthesis of azoline. There three motifs involved in the binding are, in UniProtKB:P75838, 71-79: Sx3ExxER, 184-203: Sx6Ex3Qx3ExxER, and 286-290: RxxxE. Three slightly different functional families are represented in this family, proteins involved in TOMM (thiazole/oxazole-modified microcin) biogenesis, non-TOMM proteins such as UniProtKB:P75838, and TfuA-associated non-TOMM proteins involved in trifolitoxin biosynthesis. UniProtKB:P75838 hydrolyses ATP to AMP and pyrophosphate [1]. [1]. 25129028. Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis. Dunbar KL, Chekan JR, Cox CL, Burkhart BJ, Nair SK, Mitchell DA;. Nat Chem Biol. 2014;10:823-829. (from Pfam)
30S ribosomal protein S12 methylthiotransferase accessory factor YcaO
YcaO acts as a partner for RimO to achieve the modification of ribosomal protein S12. Homologs of YcaO are involved a wide variety of RiPP (ribosomally translated, post-translationally modified peptide) natural product biosynthesis pathways. Some members of this family have an additional N-terminal OsmC-like domain.
OsmC domain/YcaO domain-containing protein
OsmC domain/YcaO domain-containing protein may be involved in ATP-dependent peptide cyclodehydration
This family consists of remarkably well-conserved proteins from gamma and beta Proteobacteria, heavily skewed towards organisms of marine environments. Its gene neighborhood is not conserved. This family has an OsmC-like N-terminal domain. It shares a YcaO domain, frequently associated with ATP-dependent cyclodehydration for peptide modification. The function is unknown. Fifteen of the first sixteen members of this family are from selenouridine-positive genomes, but this correlation may not be meaningful.
YcaO-type kinase domain
This protein family includes YcaO and homologs that can phosphorylate a peptide amide backbone (rather than side chains), as during heterocycle-forming modifications during maturation of the TOMM class (Thiazole/Oxazole-Modified Microcins) of bacteriocins. However, YcaO domain proteins also occur in contexts that do not suggest peptide modification.
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