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P17293 (RS12_THETH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 112. 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:
30S ribosomal protein S12
Gene names
Name:rpsL
Synonyms:rps12
OrganismThermus thermophilus
Taxonomic identifier274 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

With S4 and S5 plays an important role in translational accuracy By similarity. HAMAP-Rule MF_00403_B

Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit By similarity. HAMAP-Rule MF_00403_B

Subunit structure

Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex By similarity.

Sequence similarities

Belongs to the ribosomal protein S12P family.

Mass spectrometry

Molecular mass is 14516 Da from positions 2 - 132. Determined by MALDI. Strain IB-21. Ref.3

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 13213130S ribosomal protein S12 HAMAP-Rule MF_00403_B
PRO_0000146342

Amino acid modifications

Modified residue8913-methylthioaspartic acid Probable

Natural variations

Natural variant421P → S in strain: Isolate HG18; streptomycin resistant.
Natural variant431K → R in strain: Isolate HG3; streptomycin resistant.
Natural variant861R → C in strain: Isolate HG14; streptomycin pseudo-dependent.
Natural variant861R → H in strain: Isolate HG31; streptomycin pseudo-dependent.
Natural variant881K → E in strain: Isolate HG19; streptomycin resistant.
Natural variant881K → R in strain: Isolate HG1; streptomycin resistant.
Natural variant911P → L in strain: Isolate HG11; streptomycin dependent.

Secondary structure

............... 132
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17293 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9943D095FAD4D9BC

FASTA13214,599
        10         20         30         40         50         60 
MPTINQLVRK GREKVRKKSK VPALKGAPFR RGVCTVVRTV TPKKPNSALR KVAKVRLTSG 

        70         80         90        100        110        120 
YEVTAYIPGE GHNLQEHSVV LIRGGRVKDL PGVRYHIVRG VYDAAGVKDR KKSRSKYGTK 

       130 
KPKEAAKTAA KK 

« Hide

References

[1]"Ribosomal proteins from Thermus thermophilus for structural investigations."
Garber M.B., Agalarov S.C., Eliseikina I.A., Fomenkova N.P., Nikonov S.V., Sedelnikova S.E., Shikaeva O.S., Vasiliev D., Zhdanov A.S., Liljas A., Svensson L.A.
Biochimie 74:327-336(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8.
Strain: VK1.
[2]"Streptomycin-resistant and streptomycin-dependent mutants of the extreme thermophile Thermus thermophilus."
Gregory S.T., Cate J.H.D., Dahlberg A.E.
J. Mol. Biol. 309:333-338(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-132, STREPTOMYCIN RESISTANT VARIANTS.
Strain: ATCC 43815 / IB-21.
[3]"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.
Strain: ATCC 43815 / IB-21.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF316617 Genomic DNA. Translation: AAG38586.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TWTmodel-O-[»]
2OM7electron microscopy7.30E2-132[»]
4BYBX-ray3.35L1-132[»]
ProteinModelPortalP17293.
SMRP17293. Positions 2-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-270023.
STRING262724.TTC1333.

Proteomic databases

PRIDEP17293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.40.50.140. 1 hit.
HAMAPMF_00403_B. Ribosomal_S12_B.
InterProIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]
PANTHERPTHR11652. PTHR11652. 1 hit.
PfamPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFPIRSF002133. Ribosomal_S12/S23. 1 hit.
PRINTSPR01034. RIBOSOMALS12.
SUPFAMSSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00981. rpsL_bact. 1 hit.
PROSITEPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17293.

Entry information

Entry nameRS12_THETH
AccessionPrimary (citable) accession number: P17293
Secondary accession number(s): Q9EYQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 112 of the entry and version 3 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