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Reviewed, UniProtKB/Swiss-Prot P09415 (RL18_BACST)

Last modified November 25, 2008. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    50S ribosomal protein L18
Alternative name(s):
    BL22
Gene names
Name: rplR
OrganismBacillus stearothermophilus (Geobacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length120 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.

Subunit structure

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18 subcomplex. In B.stearothermophilus only 2 proteins, L5 and L18 have been shown to be part of this subcomplex, unlike the case in E.coli and T.thermophilus where L25 (TL5) is also found.

Post-translational modification

The protein, when overexpressed in E.coli, contains a phosphoserine, which is required for the protein to bind to 5S rRNA (Ref.4). It has been suggested, based solely on amino acid conservation, that this occurs on Ser-57.

Sequence similarities

Belongs to the ribosomal protein L18P family.

Ontologies

Keywords

   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   Technical term3D-structure
Direct protein sequencing

Gene Ontology (GO)

   Biological processtranslation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentribosome

Inferred from electronic annotation. Source: InterPro

   Molecular functionrRNA binding

Inferred from electronic annotation. Source: HAMAP

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12012050S ribosomal protein L18
PRO_0000131215

Secondary structure

.............. 120
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09415-1 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 1E58742142882667

FASTA12013,472
        10         20         30         40         50         60 
MITKVDRNAV RKKRHARIRK KIFGTTERPR LSVFRSNKHI YAQIIDDTKS ATIVSASTLD 

        70         80         90        100        110        120 
KEFGLDSTNN IEAAKKVGEL VAKRALEKGI KQVVFDRGGY LYHGRVKALA DAAREAGLEF 

« Hide

References

[1]"The complete amino acid sequences of the 5 S rRNA binding proteins L5 and L18 from the moderate thermophile Bacillus stearothermophilus ribosome."
Kimura J., Kimura M.
FEBS Lett. 210:85-90(1987) [PubMed: 3542562] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]"Cloning, sequencing, and overexpression of genes for ribosomal proteins from Bacillus stearothermophilus."
Ramakrishnan V., Gerchman S.E.
J. Biol. Chem. 266:880-885(1991) [PubMed: 1985969] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Isolation and characterization of 5S RNA-protein complexes from Bacillus stearothermophilus and Escherichia coli ribosomes."
Horne J.R., Erdmann V.A.
Mol. Gen. Genet. 119:337-344(1972) [PubMed: 4567807] [Abstract]
Cited for: ISOLATION OF 5S RRNA-PROTEIN COMPLEXES.
[4]"Phosphorylation of ribosomal protein L18 is required for its folding and binding to 5S rRNA."
Bloemink M.J., Moore P.B.
Biochemistry 38:13385-13390(1999) [PubMed: 10529214] [Abstract]
Cited for: PHOSPHORYLATION.
[5]"The solution structure of ribosomal protein L18 from Bacillus stearothermophilus."
Turner C.F., Moore P.B.
J. Mol. Biol. 335:679-684(2004) [PubMed: 14687565] [Abstract]
Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

M57624 Genomic DNA. Translation: AAA22702.1. Sequence problems.
PIRR5BS8F. B29102.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1OVYNMR-A1-120[»]
ModBaseSearch...

Family and domain databases

HAMAPMF_01337.
[Tree]
InterProIPR005484. Ribosomal_L18/L5.
IPR004389. Ribosomal_L18_bac.
[Graphical view]
PfamPF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
ProDomPD001394. Ribosomal_L18p. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00060. L18_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRL18_BACST
AccessionPrimary (citable) accession number: P09415
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 25, 2008
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents