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Q5SHN3 (RS12_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30S ribosomal protein S12
Gene names
Name:rpsL
Ordered Locus Names:TTHA1697
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [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. 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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14

Sequence similarities

Belongs to the ribosomal protein S12P family.

Mass spectrometry

Molecular mass is 14516 Da from positions 2 - 132. Determined by MALDI. Ref.4

Sequence caution

The sequence BAD71520.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA36418.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 13213130S ribosomal protein S12 HAMAP-Rule MF_00403_B
PRO_0000146341

Amino acid modifications

Modified residue8913-methylthioaspartic acid HAMAP-Rule MF_00403_B

Secondary structure

................................ 132
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SHN3 [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

« Hide 'large scale' references
[1]"Nucleotide sequence of the Thermus thermophilus HB8 rps12 and rps7 genes coding for the ribosomal proteins S12 and S7."
Yakhnin A.V., Vorozheykina D.P., Matvienko N.I.
Nucleic Acids Res. 18:3659-3659(1990) [PubMed] [Europe PMC] [Abstract]
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]"Purification and characterization of the 30S ribosomal proteins from the bacterium Thermus thermophilus."
Tsiboli P., Herfurth E., Choli T.
Eur. J. Biochem. 226:169-177(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-29.
[4]"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: BETA-METHYLTHIOLATION AT ASP-89, MASS SPECTROMETRY.
[5]"Structure of the 30S ribosomal subunit."
Wimberly B.T., Brodersen D.E., Clemons W.M. Jr., Morgan-Warren R.J., Carter A.P., Vonrhein C., Hartsch T., Ramakrishnan V.
Nature 407:327-339(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
[6]"Structure of functionally activated small ribosomal subunit at 3.3 A resolution."
Schluenzen F., Tocilj A., Zarivach R., Harms J., Gluehmann M., Janell D., Bashan A., Bartels H., Agmon I., Franceschi F., Yonath A.
Cell 102:615-623(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
[7]"The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit."
Brodersen D.E., Clemons W.M. Jr., Carter A.P., Morgan-Warren R.J., Wimberly B.T., Ramakrishnan V.
Cell 103:1143-1154(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
[8]"Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics."
Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J., Wimberly B.T., Ramakrishnan V.
Nature 407:340-348(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 30S SUBUNIT.
[9]"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 (5.00 ANGSTROMS) OF THE RIBOSOME.
[10]"Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3."
Pioletti M., Schluenzen F., Harms J., Zarivach R., Gluehmann M., Avila H., Bashan A., Bartels H., Auerbach T., Jacobi C., Hartsch T., Yonath A., Franceschi F.
EMBO J. 20:1829-1839(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
[11]"Crystal structure of an initiation factor bound to the 30S ribosomal subunit."
Carter A.P., Clemons W.M. Jr., Brodersen D.E., Morgan-Warren R.J., Hartsch T., Wimberly B.T., Ramakrishnan V.
Science 291:498-501(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
[12]"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.
[13]"Recognition of cognate transfer RNA by the 30S ribosomal subunit."
Ogle J.M., Brodersen D.E., Clemons W.M. Jr., Tarry M.J., Carter A.P., Ramakrishnan V.
Science 292:897-902(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF THE 30S SUBUNIT.
[14]"Crystal structure of the 30S ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16S RNA."
Brodersen D.E., Clemons W.M. Jr., Carter A.P., Wimberly B.T., Ramakrishnan V.
J. Mol. Biol. 316:725-768(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52165 Genomic DNA. Translation: CAA36418.1. Different initiation.
AP008226 Genomic DNA. Translation: BAD71520.1. Different initiation.
PIRR3TW12. S10249.
RefSeqYP_144963.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00L2-132[»]
1GIXX-ray5.50O2-132[»]
1HNWX-ray3.40L2-132[»]
1HNXX-ray3.40L2-132[»]
1HNZX-ray3.30L2-132[»]
1HR0X-ray3.20L2-132[»]
1I94X-ray3.20L2-132[»]
1I95X-ray4.50L2-132[»]
1I96X-ray4.20L2-132[»]
1I97X-ray4.50L2-132[»]
1IBKX-ray3.31L2-132[»]
1IBLX-ray3.11L2-132[»]
1IBMX-ray3.31L2-132[»]
1J5EX-ray3.05L2-132[»]
1JGOX-ray5.60O2-132[»]
1JGPX-ray7.00O2-132[»]
1JGQX-ray5.00O2-132[»]
1L1Umodel-L1-125[»]
1ML5electron microscopy14.00O2-132[»]
1MVRelectron microscopy12.80O2-132[»]
1N32X-ray3.00L2-132[»]
1N33X-ray3.35L2-132[»]
1N34X-ray3.80L2-132[»]
1N36X-ray3.65L2-132[»]
1PN7electron microscopy10.80O2-125[»]
1PN8electron microscopy10.80O2-125[»]
1PNSX-ray8.70L2-125[»]
1PNXX-ray9.50L2-125[»]
1QZCelectron microscopy9.00L2-132[»]
1XMOX-ray3.25L2-132[»]
1XMQX-ray3.00L2-132[»]
1XNQX-ray3.05L2-132[»]
1XNRX-ray3.10L2-132[»]
1YL4X-ray5.50O2-132[»]
2B64X-ray5.90L2-132[»]
2B9MX-ray6.76L2-132[»]
2B9OX-ray6.46L2-132[»]
2E5LX-ray3.30L2-132[»]
2F4VX-ray3.80L1-132[»]
2HGIX-ray5.00O1-132[»]
2HGPX-ray5.50O1-132[»]
2HGRX-ray4.51O1-132[»]
2HHHX-ray3.35L2-132[»]
2J00X-ray2.80L2-131[»]
2J02X-ray2.80L2-132[»]
2OW8X-ray3.71m1-132[»]
2UU9X-ray3.10L2-132[»]
2UUAX-ray2.90L2-132[»]
2UUBX-ray2.80L2-132[»]
2UUCX-ray3.10L2-132[»]
2UXBX-ray3.10L2-132[»]
2UXCX-ray2.90L2-132[»]
2UXDX-ray3.20L2-132[»]
2V46X-ray3.50L2-132[»]
2V48X-ray3.50L2-132[»]
2VQEX-ray2.50L2-132[»]
2VQFX-ray2.90L2-132[»]
2WDGX-ray3.30L2-132[»]
2WDHX-ray3.30L2-132[»]
2WDKX-ray3.50L2-132[»]
2WDMX-ray3.50L2-132[»]
2WH1X-ray3.45L1-132[»]
2WH3X-ray3.45L1-132[»]
2WRIX-ray3.60L1-132[»]
2WRKX-ray3.60L1-132[»]
2WRNX-ray3.60L2-132[»]
2WRQX-ray3.60L2-132[»]
2X9RX-ray3.10L1-132[»]
2X9TX-ray3.10L1-132[»]
2XFZX-ray3.20L2-132[»]
2XG1X-ray3.20L2-132[»]
2XQDX-ray3.10L2-132[»]
2XSYelectron microscopy7.80L1-132[»]
2XUYelectron microscopy7.60L1-132[»]
2Y0UX-ray3.10L2-132[»]
2Y0WX-ray3.10L2-132[»]
2Y0YX-ray3.10L1-132[»]
2Y10X-ray3.10L2-132[»]
2Y12X-ray3.10L1-132[»]
2Y14X-ray3.10L2-132[»]
2Y16X-ray3.10L2-132[»]
2Y18X-ray3.10L2-132[»]
2ZM6X-ray3.30L2-132[»]
3FICelectron microscopy6.40L2-126[»]
3HUWX-ray3.10L1-132[»]
3HUYX-ray3.10L1-132[»]
3I8GX-ray3.10O1-132[»]
3I8HX-ray3.10O1-132[»]
3I9BX-ray3.50O1-132[»]
3I9DX-ray3.50O1-132[»]
3KIQX-ray3.30l1-132[»]
3KISX-ray3.30l1-132[»]
3KIUX-ray3.60l1-132[»]
3KIXX-ray3.60l1-132[»]
3KNHX-ray3.00L1-132[»]
3KNJX-ray3.15L1-132[»]
3KNLX-ray3.45L1-132[»]
3KNNX-ray3.45L1-132[»]
3OGEX-ray3.00L1-132[»]
3OGYX-ray3.00L1-132[»]
3OHCX-ray3.00L1-132[»]
3OHDX-ray3.00L1-132[»]
3OHYX-ray3.00L1-132[»]
3OI0X-ray3.00L1-132[»]
3OI2X-ray3.10L1-132[»]
3OI4X-ray3.10L1-132[»]
3OTOX-ray3.69L2-132[»]
3T1HX-ray3.11L1-132[»]
3T1YX-ray2.80L1-132[»]
3TVFX-ray3.10O1-132[»]
3TVGX-ray3.10O1-132[»]
3UXSX-ray3.20L1-132[»]
3UXTX-ray3.20L1-132[»]
3UYDX-ray3.00O1-128[»]
3UYFX-ray3.00O1-128[»]
3UZ3X-ray3.30O1-132[»]
3UZ4X-ray3.30O1-132[»]
3UZ6X-ray3.00O1-132[»]
3UZ7X-ray3.00O1-132[»]
3UZGX-ray3.30O1-132[»]
3UZIX-ray3.30O1-132[»]
3UZLX-ray3.30O1-128[»]
3UZMX-ray3.30O1-128[»]
3V22X-ray3.00L1-132[»]
3V24X-ray3.00L1-132[»]
3V26X-ray3.10L1-132[»]
3V28X-ray3.10L1-132[»]
3V2CX-ray2.70L1-132[»]
3V2EX-ray2.70L1-132[»]
3V6UX-ray3.90L1-132[»]
3V6VX-ray3.90L1-132[»]
3ZN7X-ray3.10L2-132[»]
3ZNDX-ray3.10L2-132[»]
3ZVOX-ray3.80L2-132[»]
4ABRX-ray3.10L2-132[»]
4AQYX-ray3.50L2-132[»]
4B3MX-ray2.90L1-132[»]
4B3RX-ray3.00L1-132[»]
4B3SX-ray3.15L1-132[»]
4B3TX-ray3.00L1-132[»]
4B8FX-ray3.70L1-132[»]
4B8HX-ray3.70L1-132[»]
4BYDX-ray3.35L1-132[»]
4CR1X-ray2.95L1-132[»]
4DH9X-ray3.20L1-132[»]
4DHBX-ray3.20L1-132[»]
4DUYX-ray3.39L2-132[»]
4DUZX-ray3.65L2-132[»]
4DV0X-ray3.85L2-132[»]
4DV1X-ray3.85L2-132[»]
4DV2X-ray3.65L2-132[»]
4DV3X-ray3.55L2-132[»]
4DV4X-ray3.65L2-132[»]
4DV5X-ray3.68L2-132[»]
4DV6X-ray3.30L2-132[»]
4DV7X-ray3.29L2-132[»]
4EJ9X-ray3.52L1-132[»]
4EJAX-ray3.52L1-132[»]
4G5KX-ray3.30O1-127[»]
4G5MX-ray3.30O1-127[»]
4G5TX-ray3.10O1-127[»]
4G5VX-ray3.10O1-127[»]
4GKJX-ray3.30L2-125[»]
4GKKX-ray3.20L2-125[»]
4JI0X-ray3.49L2-132[»]
4JI1X-ray3.14L2-132[»]
4JI2X-ray3.64L2-132[»]
4JI3X-ray3.35L2-132[»]
4JI4X-ray3.69L2-132[»]
4JI5X-ray3.85L2-132[»]
4JI6X-ray3.55L2-132[»]
4JI7X-ray3.50L2-132[»]
4JI8X-ray3.74L2-132[»]
4JUWX-ray2.86L2-125[»]
4JV5X-ray3.16L2-126[»]
4JYAX-ray3.10L2-126[»]
4K0KX-ray3.40L2-127[»]
4K0LX-ray3.30L2-125[»]
4K0PX-ray3.30L2-125[»]
4KHPX-ray3.10L2-126[»]
4NVUX-ray3.00L1-132[»]
4NVWX-ray3.00L1-132[»]
4NVYX-ray3.10L1-132[»]
4NW0X-ray3.10L1-132[»]
4OX9X-ray3.80L1-131[»]
ProteinModelPortalQ5SHN3.
SMRQ5SHN3. Positions 2-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1697.

Proteomic databases

PRIDEQ5SHN3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71520; BAD71520; BAD71520.
GeneID3169892.
KEGGttj:TTHA1697.
PATRIC23958349. VBITheThe93045_1667.

Phylogenomic databases

eggNOGCOG0048.
HOGENOMHOG000040063.
KOK02950.
OMAPALQWGY.
OrthoDBEOG61ZTNF.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1736-MONOMER.

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

EvolutionaryTraceQ5SHN3.

Entry information

Entry nameRS12_THET8
AccessionPrimary (citable) accession number: Q5SHN3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 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