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P17291 (RS7_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 137. 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 S7
Gene names
Name:rpsG
Synonyms:rps7
Ordered Locus Names:TTHA1696
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the primary rRNA binding proteins, it binds directly to 3'-end of the 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center. Binds mRNA and the E site tRNA blocking its exit path in the ribosome. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA. HAMAP-Rule MF_00480_B

Subunit structure

Part of the 30S ribosomal subunit. Contacts proteins S9 and S11. Binds to the C-terminus of IF3 and to the C-terminus of Era. Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the ribosomal protein S7P family.

Mass spectrometry

Molecular mass is 17886 Da from positions 2 - 156. Determined by MALDI. Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 15615530S ribosomal protein S7 HAMAP-Rule MF_00480_B
PRO_0000124369

Secondary structure

........................... 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17291 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BC20C4487623B0E9

FASTA15618,016
        10         20         30         40         50         60 
MARRRRAEVR QLQPDLVYGD VLVTAFINKI MRDGKKNLAA RIFYDACKII QEKTGQEPLK 

        70         80         90        100        110        120 
VFKQAVENVK PRMEVRSRRV GGANYQVPME VSPRRQQSLA LRWLVQAANQ RPERRAAVRI 

       130        140        150 
AHELMDAAEG KGGAVKKKED VERMAEANRA YAHYRW 

« 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 2-50.
[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: MASS SPECTROMETRY.
[5]"The structure of ribosomal protein S7 at 1.9-A resolution reveals a beta-hairpin motif that binds double-stranded nucleic acids."
Wimberly B.T., White S.W., Ramakrishnan V.
Structure 5:1187-1198(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]"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.
[7]"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).
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly."
Sharma M.R., Barat C., Wilson D.N., Booth T.M., Kawazoe M., Hori-Takemoto C., Shirouzu M., Yokoyama S., Fucini P., Agrawal R.K.
Mol. Cell 18:319-329(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (13.50 ANGSTROMS), INTERACTION WITH ERA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52165 Genomic DNA. Translation: CAA36419.1.
AP008226 Genomic DNA. Translation: BAD71519.1.
RefSeqYP_144962.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DV4X-ray4.50G12-146[»]
1FJGX-ray3.00G1-156[»]
1FKAX-ray3.30G1-151[»]
1GIXX-ray5.50J1-156[»]
1HNWX-ray3.40G1-156[»]
1HNXX-ray3.40G1-156[»]
1HNZX-ray3.30G1-156[»]
1HR0X-ray3.20G1-156[»]
1I94X-ray3.20G2-156[»]
1I95X-ray4.50G2-156[»]
1I96X-ray4.20G2-156[»]
1I97X-ray4.50G2-156[»]
1IBKX-ray3.31G1-156[»]
1IBLX-ray3.11G1-156[»]
1IBMX-ray3.31G1-156[»]
1J5EX-ray3.05G2-156[»]
1JGOX-ray5.60J1-156[»]
1JGPX-ray7.00J1-156[»]
1JGQX-ray5.00J1-156[»]
1L1Umodel-G1-156[»]
1N32X-ray3.00G2-156[»]
1N33X-ray3.35G2-156[»]
1N34X-ray3.80G2-156[»]
1N36X-ray3.65G2-156[»]
1PNSX-ray8.70G2-156[»]
1PNXX-ray9.50G2-156[»]
1QD7X-ray5.50F12-146[»]
1RSSX-ray1.90A7-156[»]
1TWTmodel-J2-156[»]
1X18electron microscopy13.50F2-156[»]
1XMOX-ray3.25G1-156[»]
1XMQX-ray3.00G1-156[»]
1XNQX-ray3.05G1-156[»]
1XNRX-ray3.10G1-156[»]
1YL4X-ray5.50J1-156[»]
2B64X-ray5.90G1-156[»]
2B9MX-ray6.76G1-156[»]
2B9OX-ray6.46G1-156[»]
2E5LX-ray3.30G2-156[»]
2F4VX-ray3.80G1-156[»]
2HGIX-ray5.00J1-156[»]
2HGPX-ray5.50J1-156[»]
2HGRX-ray4.51J1-156[»]
2HHHX-ray3.35G1-156[»]
2J00X-ray2.80G2-155[»]
2J02X-ray2.80G2-155[»]
2OW8X-ray3.71h-[»]
2UU9X-ray3.10G2-155[»]
2UUAX-ray2.90G1-156[»]
2UUBX-ray2.90G2-155[»]
2UUCX-ray3.10G2-155[»]
2UXBX-ray3.10G1-156[»]
2UXCX-ray2.90G1-156[»]
2UXDX-ray3.20G1-156[»]
2V46X-ray3.80G2-155[»]
2V48X-ray3.50G1-156[»]
2VQEX-ray2.50G1-156[»]
2VQFX-ray2.90G1-156[»]
2WDGX-ray3.30G1-156[»]
2WDHX-ray3.30G1-156[»]
2WDKX-ray3.50G1-156[»]
2WDMX-ray3.50G1-156[»]
2WH1X-ray3.45G1-156[»]
2WH3X-ray3.45G1-156[»]
2WRIX-ray3.60G1-156[»]
2WRKX-ray3.60G1-156[»]
2WRNX-ray3.60G1-156[»]
2WRQX-ray3.60G1-156[»]
2X9RX-ray3.10G1-156[»]
2X9TX-ray3.10G1-156[»]
2XFZX-ray3.20G1-156[»]
2XG1X-ray3.20G1-156[»]
2XQDX-ray3.10G1-156[»]
2XSYelectron microscopy7.80G1-156[»]
2XUYelectron microscopy7.60G1-156[»]
2Y0UX-ray3.10G1-156[»]
2Y0WX-ray3.10G1-156[»]
2Y0YX-ray3.10G1-156[»]
2Y10X-ray3.10G1-156[»]
2Y12X-ray3.10G1-156[»]
2Y14X-ray3.10G1-156[»]
2Y16X-ray3.10G1-156[»]
2Y18X-ray3.10G1-156[»]
2ZM6X-ray3.30G2-156[»]
3FICelectron microscopy6.40G2-156[»]
3HUWX-ray3.10G1-156[»]
3HUYX-ray3.10G1-156[»]
3I8GX-ray3.10J1-156[»]
3I8HX-ray3.10J1-156[»]
3I9BX-ray3.50J1-156[»]
3I9DX-ray3.50J1-156[»]
3KIQX-ray3.30g1-156[»]
3KISX-ray3.30g1-156[»]
3KIUX-ray3.60g1-156[»]
3KIXX-ray3.60g1-156[»]
3KNHX-ray3.00G1-156[»]
3KNJX-ray3.15G1-156[»]
3KNLX-ray3.45G1-156[»]
3KNNX-ray3.45G1-156[»]
3OGEX-ray3.00G1-156[»]
3OGYX-ray3.00G1-156[»]
3OHCX-ray3.00G1-156[»]
3OHDX-ray3.00G1-156[»]
3OHYX-ray3.00G1-156[»]
3OI0X-ray3.00G1-156[»]
3OI2X-ray3.10G1-156[»]
3OI4X-ray3.10G1-156[»]
3OTOX-ray3.69G1-156[»]
3T1HX-ray3.11G1-156[»]
3T1YX-ray2.80G1-156[»]
3TVFX-ray3.10J1-156[»]
3TVGX-ray3.10J1-156[»]
3UXSX-ray3.20G1-156[»]
3UXTX-ray3.20G1-156[»]
3UYDX-ray3.00J1-156[»]
3UYFX-ray3.00J1-156[»]
3UZ3X-ray3.30J1-156[»]
3UZ4X-ray3.30J1-156[»]
3UZ6X-ray3.00J1-156[»]
3UZ7X-ray3.00J1-156[»]
3UZGX-ray3.30J1-156[»]
3UZIX-ray3.30J1-156[»]
3UZLX-ray3.30J1-156[»]
3UZMX-ray3.30J1-156[»]
3V22X-ray3.00G1-156[»]
3V24X-ray3.00G1-156[»]
3V26X-ray3.10G1-156[»]
3V28X-ray3.10G1-156[»]
3V2CX-ray2.70G1-156[»]
3V2EX-ray2.70G1-156[»]
3V6UX-ray3.90G1-156[»]
3V6VX-ray3.90G1-156[»]
3ZN7X-ray3.10G1-156[»]
3ZNDX-ray3.10G1-156[»]
3ZVOX-ray3.80G1-156[»]
4ABRX-ray3.10G1-156[»]
4AQYX-ray3.50G2-156[»]
4B3MX-ray2.90G2-156[»]
4B3RX-ray3.00G2-156[»]
4B3SX-ray3.15G2-156[»]
4B3TX-ray3.00G2-156[»]
4B8FX-ray3.70G1-156[»]
4B8HX-ray3.70G1-156[»]
4BTCX-ray2.95G1-156[»]
4BYBX-ray3.35G1-156[»]
4BYDX-ray3.35G1-156[»]
4DH9X-ray3.20G1-156[»]
4DHBX-ray3.20G1-156[»]
4DR1X-ray3.60G1-156[»]
4DR2X-ray3.25G1-156[»]
4DR3X-ray3.35G1-156[»]
4DR4X-ray3.97G1-156[»]
4DR5X-ray3.45G1-156[»]
4DR6X-ray3.30G1-156[»]
4DR7X-ray3.75G1-156[»]
4DUYX-ray3.39G1-156[»]
4DUZX-ray3.65G1-156[»]
4DV0X-ray3.85G1-156[»]
4DV1X-ray3.85G1-156[»]
4DV2X-ray3.65G1-156[»]
4DV3X-ray3.55G1-156[»]
4DV4X-ray3.65G1-156[»]
4DV5X-ray3.68G1-156[»]
4DV6X-ray3.30G1-156[»]
4DV7X-ray3.29G1-156[»]
4EJ9X-ray3.52G1-156[»]
4EJAX-ray3.52G1-156[»]
4G5KX-ray3.30J1-156[»]
4G5MX-ray3.30J1-156[»]
4G5TX-ray3.10J1-156[»]
4G5VX-ray3.10J1-156[»]
4GKJX-ray3.30G2-156[»]
4GKKX-ray3.20G2-156[»]
4JI0X-ray3.49G1-156[»]
4JI1X-ray3.14G1-156[»]
4JI2X-ray3.64G1-156[»]
4JI3X-ray3.35G1-156[»]
4JI4X-ray3.69G1-156[»]
4JI5X-ray3.85G1-156[»]
4JI6X-ray3.55G1-156[»]
4JI7X-ray3.50G1-156[»]
4JI8X-ray3.74G1-156[»]
4JUWX-ray2.86G2-156[»]
4JV5X-ray3.16G2-156[»]
4JYAX-ray3.10G2-156[»]
4K0KX-ray3.40G2-156[»]
4K0LX-ray3.30G2-156[»]
4K0PX-ray3.30G2-156[»]
4KHPX-ray3.10G2-156[»]
ProteinModelPortalP17291.
SMRP17291. Positions 2-156.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-112129.
STRING300852.TTHA1696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71519; BAD71519; BAD71519.
GeneID3167931.
KEGGttj:TTHA1696.
PATRIC23958347. VBITheThe93045_1666.

Phylogenomic databases

eggNOGCOG0049.
HOGENOMHOG000039067.
KOK02992.
OMAEVHRMAD.
OrthoDBEOG6P5ZKW.
ProtClustDBPRK05302.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1735-MONOMER.

Family and domain databases

Gene3D1.10.455.10. 1 hit.
HAMAPMF_00480_B. Ribosomal_S7_B.
InterProIPR000235. Ribosomal_S5/S7.
IPR005717. Ribosomal_S7_bac/org-type.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERPTHR11205. PTHR11205. 1 hit.
PTHR11205:SF13. PTHR11205:SF13. 1 hit.
PfamPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMSSF47973. SSF47973. 1 hit.
TIGRFAMsTIGR01029. rpsG_bact. 1 hit.
PROSITEPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17291.

Entry information

Entry nameRS7_THET8
AccessionPrimary (citable) accession number: P17291
Secondary accession number(s): Q5SHN4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 137 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