Protein Family Models

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)

Date:

2024-10-16

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)

Date:

2024-10-16

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.

Gene:

ycaO

Date:

2022-02-17

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.

Date:

2024-08-07