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Q5SHQ5 (RS5_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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 S5
Gene names
Name:rpsE
Ordered Locus Names:TTHA1675
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference 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. HAMAP-Rule MF_01307_B

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-Rule MF_01307_B

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-Rule MF_01307_B

Miscellaneous

Is positioned such that it could physically interact with spectinomycin.

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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 16216130S ribosomal protein S5 HAMAP-Rule MF_01307_B
PRO_0000131621

Regions

Domain6 – 6964S5 DRBM

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SHQ5 [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].
Strain: HB8 / ATCC 27634 / DSM 579.
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [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
AP008226 Genomic DNA. Translation: BAD71498.1.
RefSeqYP_144941.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
1ML5electron microscopy14.00H1-162[»]
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[»]
2B9MX-ray6.76E1-162[»]
2B9OX-ray6.46E1-162[»]
2E5LX-ray3.30E2-162[»]
2F4VX-ray3.80E1-162[»]
2HGIX-ray5.00H1-162[»]
2HGPX-ray5.50H1-162[»]
2HGRX-ray4.51H1-162[»]
2HHHX-ray3.35E1-162[»]
2J00X-ray2.80E2-161[»]
2J02X-ray2.80E2-161[»]
2OW8X-ray3.71f-[»]
2UU9X-ray3.10E2-161[»]
2UUAX-ray2.90E1-162[»]
2UUBX-ray2.90E2-161[»]
2UUCX-ray3.10E2-161[»]
2UXBX-ray3.10E1-162[»]
2UXCX-ray2.90E1-162[»]
2UXDX-ray3.20E1-162[»]
2V46X-ray3.80E2-161[»]
2V48X-ray3.50E1-162[»]
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[»]
2WRIX-ray3.60E1-162[»]
2WRKX-ray3.60E1-162[»]
2WRNX-ray3.60E1-162[»]
2WRQX-ray3.60E1-162[»]
2X9RX-ray3.10E1-162[»]
2X9TX-ray3.10E1-162[»]
2XFZX-ray3.20E1-162[»]
2XG1X-ray3.20E1-162[»]
2XQDX-ray3.10E1-162[»]
2XSYelectron microscopy7.80E1-162[»]
2XUYelectron microscopy7.60E1-162[»]
2Y0UX-ray3.10E1-162[»]
2Y0WX-ray3.10E1-162[»]
2Y0YX-ray3.10E1-162[»]
2Y10X-ray3.10E1-162[»]
2Y12X-ray3.10E1-162[»]
2Y14X-ray3.10E1-162[»]
2Y16X-ray3.10E1-162[»]
2Y18X-ray3.10E1-162[»]
2ZM6X-ray3.30E2-162[»]
3FICelectron microscopy6.40E5-155[»]
3HUWX-ray3.10E1-162[»]
3HUYX-ray3.10E1-162[»]
3I8GX-ray3.10H1-162[»]
3I8HX-ray3.10H1-162[»]
3I9BX-ray3.50H1-162[»]
3I9DX-ray3.50H1-162[»]
3KIQX-ray3.30e1-162[»]
3KISX-ray3.30e1-162[»]
3KIUX-ray3.60e1-162[»]
3KIXX-ray3.60e1-162[»]
3KNHX-ray3.00E1-162[»]
3KNJX-ray3.15E1-162[»]
3KNLX-ray3.45E1-162[»]
3KNNX-ray3.45E1-162[»]
3OGEX-ray3.00E1-162[»]
3OGYX-ray3.00E1-162[»]
3OHCX-ray3.00E1-160[»]
3OHDX-ray3.00E1-160[»]
3OHYX-ray3.00E1-162[»]
3OI0X-ray3.00E1-162[»]
3OI2X-ray3.10E1-162[»]
3OI4X-ray3.10E1-162[»]
3OTOX-ray3.69E1-162[»]
3T1HX-ray3.11E1-162[»]
3T1YX-ray2.80E1-162[»]
3TVFX-ray3.10H1-162[»]
3TVGX-ray3.10H1-162[»]
3UXSX-ray3.20E1-162[»]
3UXTX-ray3.20E1-162[»]
3UYDX-ray3.00H1-162[»]
3UYFX-ray3.00H1-162[»]
3UZ3X-ray3.30H1-162[»]
3UZ4X-ray3.30H1-162[»]
3UZ6X-ray3.00H1-162[»]
3UZ7X-ray3.00H1-162[»]
3UZGX-ray3.30H1-162[»]
3UZIX-ray3.30H1-162[»]
3UZLX-ray3.30H1-162[»]
3UZMX-ray3.30H1-162[»]
3V22X-ray3.00E1-162[»]
3V24X-ray3.00E1-162[»]
3V26X-ray3.10E1-162[»]
3V28X-ray3.10E1-162[»]
3V2CX-ray2.70E1-162[»]
3V2EX-ray2.70E1-162[»]
3V6UX-ray3.90E1-162[»]
3V6VX-ray3.90E1-162[»]
3ZN7X-ray3.10E1-162[»]
3ZNDX-ray3.10E1-162[»]
3ZVOX-ray3.80E1-162[»]
4ABRX-ray3.10E1-162[»]
4AQYX-ray3.50E2-162[»]
4B3MX-ray2.90E2-162[»]
4B3RX-ray3.00E2-162[»]
4B3SX-ray3.15E2-162[»]
4B3TX-ray3.00E2-162[»]
4B8FX-ray3.70E1-162[»]
4B8HX-ray3.70E1-162[»]
4BTCX-ray2.95E1-162[»]
4BYDX-ray3.35E1-162[»]
4DH9X-ray3.20E1-162[»]
4DHBX-ray3.20E1-162[»]
4DR1X-ray3.60E1-162[»]
4DR2X-ray3.25E1-162[»]
4DR3X-ray3.35E1-162[»]
4DR4X-ray3.97E1-162[»]
4DR5X-ray3.45E1-162[»]
4DR6X-ray3.30E1-162[»]
4DR7X-ray3.75E1-162[»]
4DUYX-ray3.39E1-162[»]
4DUZX-ray3.65E1-162[»]
4DV0X-ray3.85E1-162[»]
4DV1X-ray3.85E1-162[»]
4DV2X-ray3.65E1-162[»]
4DV3X-ray3.55E1-162[»]
4DV4X-ray3.65E1-162[»]
4DV5X-ray3.68E1-162[»]
4DV6X-ray3.30E1-162[»]
4DV7X-ray3.29E1-162[»]
4EJ9X-ray3.52E1-162[»]
4EJAX-ray3.52E1-162[»]
4G5KX-ray3.30H1-162[»]
4G5MX-ray3.30H1-162[»]
4G5TX-ray3.10H1-162[»]
4G5VX-ray3.10H1-162[»]
4GKJX-ray3.30E5-154[»]
4GKKX-ray3.20E5-154[»]
4JI0X-ray3.49E1-162[»]
4JI1X-ray3.14E1-162[»]
4JI2X-ray3.64E1-162[»]
4JI3X-ray3.35E1-162[»]
4JI4X-ray3.69E1-162[»]
4JI5X-ray3.85E1-162[»]
4JI6X-ray3.55E1-162[»]
4JI7X-ray3.50E1-162[»]
4JI8X-ray3.74E1-162[»]
4JUWX-ray2.86E5-154[»]
4JV5X-ray3.16E5-154[»]
4JYAX-ray3.10E5-154[»]
4K0KX-ray3.40E5-155[»]
4K0LX-ray3.30E5-154[»]
4K0PX-ray3.30E5-154[»]
4KHPX-ray3.10E5-154[»]
ProteinModelPortalQ5SHQ5.
SMRQ5SHQ5. Positions 1-157.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1675.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71498; BAD71498; BAD71498.
GeneID3169827.
KEGGttj:TTHA1675.
PATRIC23958305. VBITheThe93045_1645.

Phylogenomic databases

eggNOGCOG0098.
HOGENOMHOG000072595.
KOK02988.
OMAYNASKIL.
OrthoDBEOG6FJNM5.
ProtClustDBPRK00550.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1714-MONOMER.

Family and domain databases

Gene3D3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
HAMAPMF_01307_B. Ribosomal_S5_B.
InterProIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005712. Ribosomal_S5_bac-type.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERPTHR13718. PTHR13718. 1 hit.
PfamPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
TIGRFAMsTIGR01021. rpsE_bact. 1 hit.
PROSITEPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5SHQ5.

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: February 19, 2014
This is version 88 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