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Protein

50S ribosomal protein L1

Gene

rplA

Organism
Thermus thermophilus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). Binds directly to 23S rRNA.By similarity
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.UniRule annotation

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro
  3. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. regulation of translation Source: UniProtKB-KW
  2. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Repressor, Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L1UniRule annotation
Gene namesi
Name:rplAUniRule annotation
Synonyms:rpl1UniRule annotation
OrganismiThermus thermophilus
Taxonomic identifieri274 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Subcellular locationi

GO - Cellular componenti

  1. large ribosomal subunit Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 22922850S ribosomal protein L1PRO_0000125765Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.1 PublicationUniRule annotation

Protein-protein interaction databases

STRINGi262724.TTC1739.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Helixi23 – 3311Combined sources
Beta strandi36 – 383Combined sources
Beta strandi41 – 5010Combined sources
Helixi55 – 573Combined sources
Beta strandi60 – 645Combined sources
Beta strandi66 – 683Combined sources
Beta strandi75 – 784Combined sources
Helixi82 – 898Combined sources
Beta strandi93 – 964Combined sources
Helixi100 – 1056Combined sources
Beta strandi112 – 1165Combined sources
Helixi118 – 1203Combined sources
Helixi121 – 13515Combined sources
Helixi141 – 1433Combined sources
Beta strandi146 – 1483Combined sources
Helixi150 – 1589Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi170 – 1789Combined sources
Helixi183 – 19917Combined sources
Beta strandi209 – 2168Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2253Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP27150.
SMRiP27150. Positions 2-229.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27150.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.UniRule annotation

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B.
InterProiIPR005878. 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]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27150-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPKHGKRYRA LLEKVDPNKI YTIDEAAHLV KELATAKFDE TVEVHAKLGI
60 70 80 90 100
DPRRSDQNVR GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI
110 120 130 140 150
IQKILDGWMD FDAVVATPDV MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI
160 170 180 190 200
GEIIREIKAG RIEFRNDKTG AIHAPVGKAS FPPEKLADNI RAFIRALEAH
210 220
KPEGAKGTFL RSVYVTTTMG PSVRINPHS
Length:229
Mass (Da):24,826
Last modified:January 23, 2007 - v3
Checksum:i38C14B2563718175
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21P → V AA sequence (PubMed:1637860)Curated
Sequence conflicti4 – 52HG → TN AA sequence (PubMed:1637860)Curated
Sequence conflicti14 – 141K → F AA sequence (PubMed:1637860)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81375 Genomic DNA. Translation: CAA57139.1.
PIRiS66577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81375 Genomic DNA. Translation: CAA57139.1.
PIRiS66577.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP27150.
SMRiP27150. Positions 2-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi262724.TTC1739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP27150.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPiMF_01318_B. Ribosomal_L1_B.
InterProiIPR005878. 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]
PfamiPF00687. Ribosomal_L1. 1 hit.
[Graphical view]
PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. 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. 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).

Entry informationi

Entry nameiRL1_THETH
AccessioniPrimary (citable) accession number: P27150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.