HAMAP rule MF_01367
General rule information
[?]
Accession |
MF_01367 |
Dates |
20-NOV-2006 (Created) 1-JUN-2023 (Last updated, Version 21) |
Scope |
Bacteria
Archaea
Plastid |
case <OC:Bacteria> or <OC:Archaea> or <OG:Chloroplast>
end case
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Bacteria> and not <OC:Cyanobacteriota>
Protein name |
RecName:
|
Full=Large ribosomal subunit protein uL14;
|
|
else case <OC:Cyanobacteriota>
Protein name |
RecName:
|
Full=Large ribosomal subunit protein uL14;
|
|
else case <OC:Archaea>
Protein name |
RecName:
|
Full=Large ribosomal subunit protein uL14;
|
|
else case <OG:Chloroplast>
Protein name |
RecName:
|
Full=Large ribosomal subunit protein uL14c;
|
|
end case
case <OC:Bacteria>
Function |
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. |
Subunit |
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L19. In the 70S ribosome, L14 and L19 interact and together make contacts with the 16S rRNA in bridges B5 and B8. |
else case <OC:Archaea>
Function |
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. |
Subunit |
Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L24e, part of which may contact the 16S rRNA in 2 intersubunit bridges. |
else case <OG:Chloroplast>
Function |
Binds to 23S rRNA. |
Subunit |
Part of the 50S ribosomal subunit. |
Subcellular location |
Plastid, chloroplast. |
end case
Similarity |
Belongs to the universal ribosomal protein uL14 family. |
case <OG:Chloroplast>
end case
Additional information
[?]
Size range |
119-182 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
In E.coli interaction of L14 with ribosomal silencing factor RsfS has been shown block formation of bridge B8, preventing association of 2 ribosomal subunits and thus causes ribosomal silencing. The same interaction is suspected to have the same effect in human mitochondrial ribosomes and maybe maize chloroplasts as well. It has not yet been propagated to all ribosomal proteins while waiting further experimental confirmation. |