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Protein

50S ribosomal protein L7/L12

Gene

rplL

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation. It extends beyond the surface of the 70S ribosome. The stalk is preferentially stabilized in 70S versus 50S crystals.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-219-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L7/L12UniRule annotation
Gene namesi
Name:rplLUniRule annotation
Ordered Locus Names:TTHA0210
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12512450S ribosomal protein L7/L12PRO_0000157597Add
BLAST

Post-translational modificationi

The ion at m/z 13016 is probably phosphorylated; treatment with phosphatase in the presence of kinase inhibitors decreases it weight. This form is only detected on 70S ribosomes and not in isolated ribosomal stalk complexes.1 Publication
The ion at m/z 12978 is suggested to be the N-acetylated form of the protein (L7). The ion at m/z 12964 is suggested to be consistent with dimethylation or formylation and is present in very small quantities in the sample.

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homodimer. Part of the 50S ribosomal subunit; present in 6 copies per ribosome. Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine to which 3 L12 dimers bind in a sequential fashion. Contacts protein L11.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0210.

Structurei

Secondary structure

1
125
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 76Combined sources
Helixi9 – 135Combined sources
Turni14 – 163Combined sources
Helixi17 – 226Combined sources
Turni25 – 273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V42X-ray5.50DI/DJ32-125[»]
4V4PX-ray5.50I/J32-125[»]
4V51X-ray2.80L/M2-125[»]
4V6FX-ray3.10DI/DJ1-125[»]
ProteinModelPortaliQ8VVE2.
SMRiQ8VVE2. Positions 3-125.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VVE2.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L7/L12P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0222.
HOGENOMiHOG000248813.
KOiK02935.
OMAiFEEMTLI.
OrthoDBiEOG6WMJ69.
PhylomeDBiQ8VVE2.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PANTHERiPTHR11809. PTHR11809. 1 hit.
PfamiPF00542. Ribosomal_L12. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
TIGRFAMsiTIGR00855. L12. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q8VVE2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALDIERIKE ELSQATVLEL KQLIDALKEA WGVTAAAPVA VAAAPAAGAA
60 70 80 90 100
AAPAEEKTEF DVILKEAGAK KLEVIKELRA ITGLGLKEAK DLAEKGGPVK
110 120
EGVSKQEAEE IKKKLEAVGA VVELK
Length:125
Mass (Da):13,067
Last modified:January 23, 2007 - v4
Checksum:i3919CBF76605AC87
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 782EL → DV in CAD11987 (Ref. 1) Curated

Mass spectrometryi

Molecular mass is 96075±13 Da from positions 2 - 125. Determined by ESI. Isolated L10(L12)6.1 Publication
Molecular mass is 77670±9 Da from positions 2 - 125. Determined by ESI. Isolated (L12)6.1 Publication
Molecular mass is 13016±1.9 Da from positions 2 - 125. Determined by ESI. Probably phosphorylated, more strongly associated with the 50S ribosomal subunit.1 Publication
Molecular mass is 12936±0.5 Da from positions 2 - 125. Determined by ESI. Not phosphorylated.1 Publication
Molecular mass is 12937 Da from positions 2 - 125. Determined by MALDI. 1 Publication
Molecular mass is 12964 Da from positions 2 - 125. Determined by MALDI. May be N-acetylated.1 Publication
Molecular mass is 12978 Da from positions 2 - 125. Determined by MALDI. May be dimethylated or formylated.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ419825 Genomic DNA. Translation: CAD11987.1.
AP008226 Genomic DNA. Translation: BAD70033.1.
RefSeqiWP_008630582.1. NC_006461.1.
YP_143476.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70033; BAD70033; BAD70033.
GeneIDi3168576.
KEGGittj:TTHA0210.
PATRICi23955361. VBITheThe93045_0208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ419825 Genomic DNA. Translation: CAD11987.1.
AP008226 Genomic DNA. Translation: BAD70033.1.
RefSeqiWP_008630582.1. NC_006461.1.
YP_143476.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V42X-ray5.50DI/DJ32-125[»]
4V4PX-ray5.50I/J32-125[»]
4V51X-ray2.80L/M2-125[»]
4V6FX-ray3.10DI/DJ1-125[»]
ProteinModelPortaliQ8VVE2.
SMRiQ8VVE2. Positions 3-125.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70033; BAD70033; BAD70033.
GeneIDi3168576.
KEGGittj:TTHA0210.
PATRICi23955361. VBITheThe93045_0208.

Phylogenomic databases

eggNOGiCOG0222.
HOGENOMiHOG000248813.
KOiK02935.
OMAiFEEMTLI.
OrthoDBiEOG6WMJ69.
PhylomeDBiQ8VVE2.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-219-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ8VVE2.

Family and domain databases

Gene3Di3.30.1390.10. 1 hit.
HAMAPiMF_00368. Ribosomal_L7_L12.
InterProiIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PANTHERiPTHR11809. PTHR11809. 1 hit.
PfamiPF00542. Ribosomal_L12. 1 hit.
[Graphical view]
ProDomiPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
TIGRFAMsiTIGR00855. L12. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ribosomal protein L12 and L10 from Thermus thermophilus, dissertation."
    Huang Y., Sprinzl M.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus."
    Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T.
    Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-30.
  4. "Heptameric (L12)6/L10 rather than canonical pentameric complexes are found by tandem MS of intact ribosomes from thermophilic bacteria."
    Ilag L.L., Videler H., McKay A.R., Sobott F., Fucini P., Nierhaus K.H., Robinson C.V.
    Proc. Natl. Acad. Sci. U.S.A. 102:8192-8197(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, STOICHIOMETRY, PHOSPHORYLATION, MASS SPECTROMETRY.
  5. "Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry."
    Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A.
    Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  6. "The path of messenger RNA through the ribosome."
    Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F.
    Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.

Entry informationi

Entry nameiRL7_THET8
AccessioniPrimary (citable) accession number: Q8VVE2
Secondary accession number(s): Q5SLT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 92 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.