| General information | | DisProt: | DP00197 | | Name: | Translation initiation factor IF-3 | | Synonym(s): | IF3_ECOLI
Translation initiation factor IF-3, N-terminally processed [cleavage product 1]
Translation initiation factor IF-3S [cleavage product 2]
| | First appeared in release: | Release 2.2 (04/14/2005) | | UniProt: | P0A707 | | UniGene: | | | SwissProt: | IF3_ECOLI | | TrEMBL: | | | NCBI (GI): | 67466073 | | Source organism: | Escherichia coli | | Sequence length: | 180 | | Percent disordered: | 7% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MKGGKRVQTA RPNRINGEIR AQEVRLTGLE GEQLGIVSLR EALEKAEEAG VDLVEISPNA - 60
EPPVCRIMDY GKFLYEKSKS SKEQKKKQKV IQVKEIKFRP GTDEGDYQVK LRSLIRFLEE - 120
GDKAKITLRF RGREMAHQQI GMEVLNRVKD DLQELAVVES FPTKIEGRQM IMVLAPKKKQ - 180
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| Functional narrative |
Translation initiation factor IF-3 is an essential component of the prokaryotic translation apparatus. When it binds to the 30S ribosomal subunit, it shifts the equilibrium between 70S ribosomes and their 50S and 30S subunits and makes the 30S subunits available for initiation of protein synthesis. Another function of translation initiation factor IF-3 is as a translational repressor protein. By binding to its mRNA, it can control the translation of its own gene.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | inter-domain linker | | Location: | 78 - 89 | | Length: | 12 | | Region sequence: |
SKSSKEQKKKQK | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- Nuclear magnetic resonance (NMR) (pH: 6.5; 20mM potassium phosphate)
| References:
- Moreau M, de Cock E, Fortier PL, Garcia C, Albaret C, Blanquet S, Lallemand JY, Dardel F. "Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution." J Mol Biol. 1997; 266(1): 15-22. PubMed: 9054966
| Comments:
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| Comments |
Disordered residues lie within the regions corresponding to cleavage products 1 and 2, however, there is no experimental evidence indicating that these products are disordered. The N-terminally processed cleavage product 1 differs from the full-length protein by removal of a single initiator methionine and cleavage product 2 has the first 6 residues removed.
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