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P27150 (RL1_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L1
Gene names
Name:rplA
Synonyms:rpl1
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release By similarity. Binds directly to 23S rRNA. HAMAP-Rule MF_01318

Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA By similarity. HAMAP-Rule MF_01318

Subunit structure

Part of the 50S ribosomal subunit.

Sequence similarities

Belongs to the ribosomal protein L1P family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3
Chain2 – 22922850S ribosomal protein L1 HAMAP-Rule MF_01318
PRO_0000125765

Experimental info

Sequence conflict21P → V AA sequence Ref.3
Sequence conflict4 – 52HG → TN AA sequence Ref.3
Sequence conflict141K → F AA sequence Ref.3

Secondary structure

.............................................. 229
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27150 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 38C14B2563718175

FASTA22924,826
        10         20         30         40         50         60 
MPKHGKRYRA LLEKVDPNKI YTIDEAAHLV KELATAKFDE TVEVHAKLGI DPRRSDQNVR 

        70         80         90        100        110        120 
GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI IQKILDGWMD FDAVVATPDV 

       130        140        150        160        170        180 
MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI GEIIREIKAG RIEFRNDKTG AIHAPVGKAS 

       190        200        210        220 
FPPEKLADNI RAFIRALEAH KPEGAKGTFL RSVYVTTTMG PSVRINPHS 

« Hide

References

[1]"Cloning and overexpression of the ribosomal protein L1 gene from Thermus thermophilus VK1. Crystallization of the recombinant protein L1."
Ossina N., Eliseikina I.A., Garber M.B., Jonsson B.-H.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: VK1.
[2]"The complete primary structure of ribosomal protein L1 from Thermus thermophilus."
Amons R., Muranova T.A., Rykunova A.I., Eliseikina I.A., Sedelnikova S.E.
J. Protein Chem. 12:725-734(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-229.
[3]"Ribosomal proteins from Thermus thermophilus for structural investigations."
Garber M.B., Agalarov S.C., Eliseikina I.A., Fomenkova N.P., Nikonov S.V., Sedelnikova S.E., Shikaeva O.S., Vasiliev D., Zhdanov A.S., Liljas A., Svensson L.A.
Biochimie 74:327-336(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
Strain: VK1.
[4]"Interaction of ribosomal L1 proteins from mesophilic and thermophilic Archaea and Bacteria with specific L1-binding sites on 23S rRNA and mRNA."
Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W.
Eur. J. Biochem. 256:97-105(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO METHANOCOCCUS VANNIELII 23S RRNA AND TO M.VANNIELII L1 MRNA.
Strain: VK1.
[5]"Crystal structure of the RNA binding ribosomal protein L1 from Thermus thermophilus."
Nikonov S.V., Nevskaya N., Eliseikina I.A., Fomenkova N.P., Nikulin A., Ossina N., Garber M.B., Jonsson B.-H., Briand C., Al-Karadaghi S., Svensson L.A., Aevarsson A., Liljas A.
EMBO J. 15:1350-1359(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
Strain: VK1.
[6]"A mutant form of the ribosomal protein L1 reveals conformational flexibility."
Unge J., Al-Karadaghi S., Liljas A., Jonsson B.H., Eliseikina I., Ossina N., Nevskaya N., Fomenkova N., Garber M., Nikonov S.
FEBS Lett. 411:53-59(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT CYS-180.
[7]"New insights into the interaction of ribosomal protein L1 with RNA."
Nevskaya N., Tishchenko S., Volchkov S., Kljashtorny V., Nikonova E., Nikonov O., Nikulin A., Kohrer C., Piendl W., Zimmermann R., Stockley P., Garber M.B., Nikonov S.
J. Mol. Biol. 355:747-759(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH A M.VANNIELII L1 MRNA FRAGMENT.
Strain: VK1.
[8]"Solution structure of the E. coli 70S ribosome at 11.5 A resolution."
Gabashvili I.S., Agrawal R.K., Spahn C.M., Grassucci R.A., Svergun D.I., Frank J., Penczek P.
Cell 100:537-549(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81375 Genomic DNA. Translation: CAA57139.1.
PIRS66577.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AD2X-ray1.90A2-229[»]
1ZHOX-ray2.60A/C/E/G2-229[»]
2HW8X-ray2.10A2-229[»]
2OUMX-ray2.55A2-229[»]
2OV7X-ray2.30A/B/C2-229[»]
2VPLX-ray2.30A/C2-229[»]
3U42X-ray1.35A1-229[»]
3U4MX-ray2.00A1-229[»]
3U56X-ray2.10A1-229[»]
3UMYX-ray1.90A2-229[»]
4F9TX-ray1.46A1-229[»]
ProteinModelPortalP27150.
SMRP27150. Positions 2-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262724.TTC1739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPMF_01318_B. Ribosomal_L1_B.
InterProIPR005878. Ribosom_L1_bac-type.
IPR002143. Ribosomal_L1.
IPR023674. Ribosomal_L1-like.
IPR028364. Ribosomal_L1/biogenesis.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR023673. Ribosomal_L1_CS.
[Graphical view]
PfamPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMSSF56808. SSF56808. 1 hit.
TIGRFAMsTIGR01169. rplA_bact. 1 hit.
PROSITEPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27150.

Entry information

Entry nameRL1_THETH
AccessionPrimary (citable) accession number: P27150
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references