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Reviewed, UniProtKB/Swiss-Prot Q5SHQ5 (RS5_THET8)

Last modified November 3, 2009. Version 49. 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 · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    30S ribosomal protein S5
Gene names
Name: rpsE
Ordered Locus Names: TTHA1675
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Complete proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length162 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 S12 plays an important role in translational accuracy By similarity.

Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Binds mRNA in the 70S ribosome, positioning it for translation. HAMAP MF_01307

Subunit structure

Part of the 30S ribosomal subunit. Contacts proteins S4 and S8. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15

Domain

The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity. HAMAP MF_01307

Miscellaneous

Is positioned such that it could physically interact with spectinomycin. HAMAP MF_01307

Sequence similarities

Belongs to the ribosomal protein S5P family.

Contains 1 S5 DRBM domain.

Mass spectrometry

Molecular mass is 17428 Da from positions 2 - 162. Determined by MALDI. Ref.3

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 16216130S ribosomal protein S5 HAMAP MF_01307
PRO_0000131621

Regions

Domain6 – 6964S5 DRBM

Secondary structure

........................ 162
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SHQ5-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BE3367CB619E68D2

FASTA16217,557
        10         20         30         40         50         60 
MPETDFEEKM ILIRRTARMQ AGGRRFRFGA LVVVGDRQGR VGLGFGKAPE VPLAVQKAGY 

        70         80         90        100        110        120 
YARRNMVEVP LQNGTIPHEI EVEFGASKIV LKPAAPGTGV IAGAVPRAIL ELAGVTDILT 

       130        140        150        160 
KELGSRNPIN IAYATMEALR QLRTKADVER LRKGEAHAQA QG 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"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: 7957245] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-44.
[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: 16287167] [Abstract]
Cited for: MASS SPECTROMETRY.
[4]"Structure of a bacterial 30S ribosomal subunit at 5.5 A resolution."
Clemons W.M. Jr., May J.L.C., Wimberly B.T., McCutcheon J.P., Capel M.S., Ramakrishnan V.
Nature 400:833-840(1999) [PubMed: 10476960] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE 30S SUBUNIT.
[5]"The small ribosomal subunit from Thermus thermophilus at 4.5 A resolution: pattern fittings and the identification of a functional site."
Tocilj A., Schluenzen F., Janell D., Gluehmann M., Hansen H.A., Harms J., Bashan A., Bartels H., Agmon I., Franceschi F., Yonath A.
Proc. Natl. Acad. Sci. U.S.A. 96:14252-14257(1999) [PubMed: 10588692] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
[6]"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: 11014182] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
[7]"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: 11007480] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
[8]"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: 11163189] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
[9]"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: 11014183] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 30S SUBUNIT.
[10]"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: 11511350] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
[11]"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: 11296217] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
[12]"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: 11228145] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
[13]"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: 11283358] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
[14]"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: 11340196] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF THE 30S SUBUNIT.
[15]"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: 11866529] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

AP008226 Genomic DNA. Translation: BAD71498.1.
RefSeqYP_144941.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00E1-162[»]
1FKAX-ray3.30E1-162[»]
1GIXX-ray5.50H1-162[»]
1HNWX-ray3.40E1-162[»]
1HNXX-ray3.40E1-162[»]
1HNZX-ray3.30E1-162[»]
1HR0X-ray3.20E1-162[»]
1I94X-ray3.20E2-162[»]
1I95X-ray4.50E2-162[»]
1I96X-ray4.20E2-162[»]
1I97X-ray4.50E2-162[»]
1IBKX-ray3.31E1-162[»]
1IBLX-ray3.11E1-162[»]
1IBMX-ray3.31E1-162[»]
1J5EX-ray3.05E2-162[»]
1JGOX-ray5.60H1-162[»]
1JGPX-ray7.00H1-162[»]
1JGQX-ray5.00H1-162[»]
1L1Umodel-E5-154[»]
1N32X-ray3.00E2-162[»]
1N33X-ray3.35E2-162[»]
1N34X-ray3.80E2-162[»]
1N36X-ray3.65E2-162[»]
1PNSX-ray8.70E5-154[»]
1PNXX-ray9.50E5-154[»]
1QD7X-ray5.50D22-130[»]
1XMOX-ray3.25E1-162[»]
1XMQX-ray3.00E1-162[»]
1XNQX-ray3.05E1-162[»]
1XNRX-ray3.10E1-162[»]
1YL4X-ray5.50H1-162[»]
2B64X-ray5.90E1-162[»]
2B9OX-ray6.46E1-162[»]
2E5LX-ray3.30E2-162[»]
2HGIX-ray5.00H1-162[»]
2HGPX-ray5.50H1-162[»]
2HGRX-ray4.51H1-162[»]
2J00X-ray2.80E2-161[»]
2J02X-ray2.80E2-161[»]
2OW8X-ray3.71f-[»]
2UU9X-ray3.10E2-161[»]
2UUAX-ray2.90E2-161[»]
2UUBX-ray2.90E2-161[»]
2UUCX-ray3.10E2-161[»]
2UXBX-ray3.10E2-161[»]
2UXCX-ray2.90E2-161[»]
2UXDX-ray3.20E2-161[»]
2V46X-ray3.80E2-161[»]
2V48X-ray3.80E2-161[»]
2VQEX-ray2.50E1-162[»]
2VQFX-ray2.90E1-162[»]
2WDGX-ray3.30E1-162[»]
2WDHX-ray3.30E1-162[»]
2WDKX-ray3.50E1-162[»]
2WDMX-ray3.50E1-162[»]
2WH1X-ray3.45E1-162[»]
2WH3X-ray3.45E1-162[»]
2ZM6X-ray3.30E2-162[»]
3FICelectron microscopy6.40E5-155[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5SHQ5.

Genome annotation databases

GeneID3169827.
GenomeReviewsGene locus TTHA1675 in contig AP008226_GR.
KEGGttj:TTHA1675.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5SHQ5.
OMAGSTIPHR.

Enzyme and pathway databases

BioCycTTHE300852:TTHA1675-MON.

Family and domain databases

HAMAPMF_01307.
[Tree]
InterProIPR014720. dsRNA-bd-like.
IPR000851. Ribosomal_S5.
IPR005712. Ribosomal_S5_bac-type.
IPR005324. Ribosomal_S5_C.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
Gene3DG3DSA:3.30.160.20. dsRNA-bd-like. 1 hit.
G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
PANTHERPTHR13718. Ribosomal_S5. 1 hit.
PfamPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR01021. rpsE_bact. 1 hit.
PROSITEPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRS5_THET8
AccessionPrimary (citable) accession number: Q5SHQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 23, 2007
Last modified: November 3, 2009
This is version 49 of the entry and version 3 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 · Web resources · Cross-references · Entry information · Relevant documents