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Q8VVE2 (RL7_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. 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 L7/L12
Gene names
Name:rplL
Ordered Locus Names:TTHA0210
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length125 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00368

Subunit structure

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. Ref.4

Post-translational modification

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. Ref.4

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. HAMAP-Rule MF_00368

Sequence similarities

Belongs to the ribosomal protein L7/L12P family.

Mass spectrometry

Molecular mass is 96075±13 Da from positions 2 - 125. Determined by ESI. Isolated L10(L12)6. Ref.4

Molecular mass is 77670±9 Da from positions 2 - 125. Determined by ESI. Isolated (L12)6. Ref.4

Molecular mass is 13016±1.9 Da from positions 2 - 125. Determined by ESI. Probably phosphorylated, more strongly associated with the 50S ribosomal subunit. Ref.4

Molecular mass is 12936±0.5 Da from positions 2 - 125. Determined by ESI. Not phosphorylated. Ref.4

Molecular mass is 12937 Da from positions 2 - 125. Determined by MALDI. Ref.5

Molecular mass is 12964 Da from positions 2 - 125. Determined by MALDI. May be N-acetylated. Ref.5

Molecular mass is 12978 Da from positions 2 - 125. Determined by MALDI. May be dimethylated or formylated. Ref.5

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionstructural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 12512450S ribosomal protein L7/L12 HAMAP-Rule MF_00368
PRO_0000157597

Experimental info

Sequence conflict77 – 782EL → DV in CAD11987. Ref.1

Secondary structure

......... 125
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8VVE2 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 3919CBF76605AC87

FASTA12513,067
        10         20         30         40         50         60 
MALDIERIKE ELSQATVLEL KQLIDALKEA WGVTAAAPVA VAAAPAAGAA AAPAEEKTEF 

        70         80         90        100        110        120 
DVILKEAGAK KLEVIKELRA ITGLGLKEAK DLAEKGGPVK EGVSKQEAEE IKKKLEAVGA 


VVELK 

« Hide

References

« Hide 'large scale' references
[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]"Crystal structure of the ribosome at 5.5 A resolution."
Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., Cate J.H.D., Noller H.F.
Science 292:883-896(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ419825 Genomic DNA. Translation: CAD11987.1.
AP008226 Genomic DNA. Translation: BAD70033.1.
RefSeqYP_143476.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIYX-ray5.50I/J32-125[»]
1YL3X-ray5.50I/J32-125[»]
2J01X-ray2.80L/M2-124[»]
2J03X-ray2.80L/M2-124[»]
3I8IX-ray3.10I/J1-125[»]
ProteinModelPortalQ8VVE2.
SMRQ8VVE2. Positions 3-125.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA0210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70033; BAD70033; BAD70033.
GeneID3168576.
KEGGttj:TTHA0210.
PATRIC23955361. VBITheThe93045_0208.

Phylogenomic databases

eggNOGCOG0222.
HOGENOMHOG000248813.
KOK02935.
OMAESKINVI.
OrthoDBEOG6WMJ69.
ProtClustDBPRK00157.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-219-MONOMER.

Family and domain databases

Gene3D3.30.1390.10. 1 hit.
HAMAPMF_00368. Ribosomal_L7_L12.
InterProIPR000206. Ribosomal_L7/12.
IPR014719. Ribosomal_L7/12_C/ClpS-like.
IPR013823. Ribosomal_L7/L12_C.
IPR008932. Ribosomal_L7/L12_oligo.
[Graphical view]
PANTHERPTHR11809. PTHR11809. 1 hit.
PfamPF00542. Ribosomal_L12. 1 hit.
[Graphical view]
ProDomPD001326. Ribosomal_L7/L12_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF48300. SSF48300. 1 hit.
SSF54736. SSF54736. 1 hit.
TIGRFAMsTIGR00855. L12. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8VVE2.

Entry information

Entry nameRL7_THET8
AccessionPrimary (citable) accession number: Q8VVE2
Secondary accession number(s): Q5SLT3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 85 of the entry and version 4 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