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P27150

- RL1_THETH

UniProt

P27150 - RL1_THETH

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Protein

50S ribosomal protein L1

Gene
rplA, rpl1
Organism
Thermus thermophilus
Status
Reviewed - 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.UniRule annotation
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA By similarity.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 L1
Gene namesi
Name:rplA
Synonyms:rpl1
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 L1UniRule annotationPRO_0000125765Add
BLAST

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit.

Protein-protein interaction databases

STRINGi262724.TTC1739.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP27150.

Family & Domainsi

Sequence similaritiesi

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

MPKHGKRYRA LLEKVDPNKI YTIDEAAHLV KELATAKFDE TVEVHAKLGI    50
DPRRSDQNVR GTVSLPHGLG KQVRVLAIAK GEKIKEAEEA GADYVGGEEI 100
IQKILDGWMD FDAVVATPDV MGAVGSKLGR ILGPRGLLPN PKAGTVGFNI 150
GEIIREIKAG RIEFRNDKTG AIHAPVGKAS FPPEKLADNI RAFIRALEAH 200
KPEGAKGTFL RSVYVTTTMG PSVRINPHS 229
Length:229
Mass (Da):24,826
Last modified:January 23, 2007 - v3
Checksum:i38C14B2563718175
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21P → V AA sequence 1 Publication
Sequence conflicti4 – 52HG → TN AA sequence 1 Publication
Sequence conflicti14 – 141K → F AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X81375 Genomic DNA. Translation: CAA57139.1.
PIRiS66577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X81375 Genomic DNA. Translation: CAA57139.1 .
PIRi S66577.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AD2 X-ray 1.90 A 2-229 [» ]
1ZHO X-ray 2.60 A/C/E/G 2-229 [» ]
2HW8 X-ray 2.10 A 2-229 [» ]
2OUM X-ray 2.55 A 2-229 [» ]
2OV7 X-ray 2.30 A/B/C 2-229 [» ]
2VPL X-ray 2.30 A/C 2-229 [» ]
3U42 X-ray 1.35 A 1-229 [» ]
3U4M X-ray 2.00 A 1-229 [» ]
3U56 X-ray 2.10 A 1-229 [» ]
3UMY X-ray 1.90 A 2-229 [» ]
4F9T X-ray 1.46 A 1-229 [» ]
ProteinModelPortali P27150.
SMRi P27150. Positions 2-229.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 262724.TTC1739.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P27150.

Family and domain databases

Gene3Di 3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
HAMAPi MF_01318_B. Ribosomal_L1_B.
InterProi IPR005878. 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 ]
Pfami PF00687. Ribosomal_L1. 1 hit.
[Graphical view ]
PIRSFi PIRSF002155. Ribosomal_L1. 1 hit.
SUPFAMi SSF56808. SSF56808. 1 hit.
TIGRFAMsi TIGR01169. rplA_bact. 1 hit.
PROSITEi PS01199. RIBOSOMAL_L1. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 97 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

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