General information | DisProt: | DP00600 | Name: | 50S ribosomal protein L4 | Synonym(s): | RL4_ECOLI
| First appeared in release: | Release 5.5 (11/17/2010) | UniProt: | P60723 | UniGene: | | SwissProt: | RL4_ECOLI | TrEMBL: | | NCBI (GI): | 46397662 | Source organism: | Escherichia coli (strain K12) | Sequence length: | 201 | Percent disordered: | 31% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MELVLKDAQS ALTVSETTFG RDFNEALVHQ VVVAYAAGAR QGTRAQKTRA EVTGSGKKPW - 60 RQKGTGRARS GSIKSPIWRS GGVTFAARPQ DHSQKVNKKM YRGALKSILS ELVRQDRLIV - 120 VEKFSVEAPK TKLLAQKLKD MALEDVLIIT GELDENLFLA ARNLHKVDVR DATGIDPVSL - 180 IAFDKVVMTA DAVKQVEEML A
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Functional narrative |
One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. The inner loop of L13 is fully disordered.
Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the nusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103).
Forms part of the polypeptide exit tunnel.
Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro.
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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: | inner loop | Location: | 45 - 103 | Length: | 59 | Region sequence: |
AQKTRAEVTGSGKKPWRQKGTGRARSGSIKSPIWRSGGVTFAARPQDHSQKVNKKMYRG | Modification type: | Native
| PDB: | | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Protein-rRNA binding
| Detection methods: | References:
- Timsit Y, Acosta Z, Allemand F, Chiaruttini C, Springer M. "The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 s ribosomal subunit assembly." Int J Mol Sci. 2009; 10(3): 817-34. PubMed: 19399222
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Region 2 | Type: | Disordered | Name: | Inner Loop | Location: | 41 - 96 | Length: | 56 | Region sequence: |
QGTRAQKTRAEVTGSGKKPWRQKGTGRARSGSIKSPIWRSGGVTFAARPQDHSQKV | Modification type: | Native
| PDB: | 1DMG:A | Structural/functional type: | Function arises from the disordered state | Functional classes: | Molecular recognition effectors
| Functional subclasses: | Protein-rRNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (HEPES (buffer) 10 mM; Jasco J-715 (spectropolarimeter ); protein (sample) 0.1086 μg/ml)
| References:
- Timsit, Youri, Fréderic Allemand, Claude Chiaruttini, and Mathias Springer. "Coexistence of two protein folding states in the crystal structure of ribosomal protein L20." Embo J. 2006; 7(10): 1013-1018. PubMed: 1618378
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