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Protein

30S ribosomal protein S7

Gene

rpsG

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro
  3. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1735-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S7
Gene namesi
Name:rpsG
Synonyms:rps7
Ordered Locus Names:TTHA1696
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. small ribosomal subunit Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 15615530S ribosomal protein S7PRO_0000124369Add
BLAST

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

MINTiMINT-112129.
STRINGi300852.TTHA1696.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Turni16 – 183Combined sources
Helixi21 – 3010Combined sources
Beta strandi32 – 343Combined sources
Helixi36 – 5419Combined sources
Helixi58 – 6912Combined sources
Beta strandi72 – 809Combined sources
Beta strandi83 – 908Combined sources
Helixi93 – 10816Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi113 – 1153Combined sources
Helixi116 – 12813Combined sources
Helixi133 – 14513Combined sources
Helixi149 – 1546Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DV4X-ray4.50G12-146[»]
1FJGX-ray3.00G1-156[»]
1FKAX-ray3.30G1-151[»]
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[»]
1QD7X-ray5.50F12-146[»]
1RSSX-ray1.90A7-156[»]
1TWTmodel-J2-156[»]
1VVJX-ray3.44G1-156[»]
1VY4X-ray2.60G1-156[»]
1VY5X-ray2.55G1-156[»]
1VY6X-ray2.90G1-156[»]
1VY7X-ray2.80G1-156[»]
1X18electron microscopy13.50F2-156[»]
1XMOX-ray3.25G1-156[»]
1XMQX-ray3.00G1-156[»]
1XNQX-ray3.05G1-156[»]
1XNRX-ray3.10G1-156[»]
2E5LX-ray3.30G2-156[»]
2F4VX-ray3.80G1-156[»]
2HHHX-ray3.35G1-156[»]
2J00X-ray2.80G2-156[»]
2J02X-ray2.80G2-156[»]
2UU9X-ray3.10G2-156[»]
2UUAX-ray2.90G2-156[»]
2UUBX-ray2.80G2-156[»]
2UUCX-ray3.10G2-156[»]
2UXBX-ray3.10G2-156[»]
2UXCX-ray2.90G2-156[»]
2UXDX-ray3.20G2-156[»]
2V46X-ray3.50G2-156[»]
2V48X-ray3.50G2-156[»]
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[»]
2ZM6X-ray3.30G2-156[»]
3OTOX-ray3.69G1-156[»]
3T1HX-ray3.11G1-156[»]
3T1YX-ray2.80G1-156[»]
4AQYX-ray3.50G2-156[»]
4B3MX-ray2.90G2-156[»]
4B3RX-ray3.00G2-156[»]
4B3SX-ray3.15G2-156[»]
4B3TX-ray3.00G2-156[»]
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[»]
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[»]
4JV5X-ray3.16G2-156[»]
4JYAX-ray3.10G2-156[»]
4K0KX-ray3.40G2-156[»]
4KHPX-ray3.10G2-156[»]
4L47X-ray3.22G1-156[»]
4L71X-ray3.90G1-156[»]
4LELX-ray3.90G1-156[»]
4LF4X-ray3.34G1-156[»]
4LF5X-ray3.75G1-156[»]
4LF6X-ray3.31G1-156[»]
4LF7X-ray3.15G1-156[»]
4LF8X-ray3.15G1-156[»]
4LF9X-ray3.28G1-156[»]
4LFAX-ray3.65G1-156[»]
4LFBX-ray3.01G1-156[»]
4LFCX-ray3.60G1-156[»]
4LFZX-ray3.92G1-156[»]
4LNTX-ray2.94G1-156[»]
4LSKX-ray3.48G1-156[»]
4LT8X-ray3.14G1-156[»]
4NXMX-ray3.65G1-156[»]
4NXNX-ray3.54G1-156[»]
4OX9X-ray3.80G2-156[»]
4P6FX-ray3.60H1-156[»]
4P70X-ray3.68G1-156[»]
4RB7X-ray2.40G1-156[»]
4V42X-ray5.50J1-156[»]
4V49X-ray8.70G2-156[»]
4V4AX-ray9.50G2-156[»]
4V4IX-ray3.71h-[»]
4V4PX-ray5.50J1-156[»]
4V4RX-ray5.90G1-156[»]
4V4SX-ray6.76G1-156[»]
4V4TX-ray6.46G1-156[»]
4V4XX-ray5.00J1-156[»]
4V4YX-ray5.50J1-156[»]
4V4ZX-ray4.51J1-156[»]
4V5FX-ray3.60G1-156[»]
4V5GX-ray3.60G1-156[»]
4V5JX-ray3.10G1-156[»]
4V5KX-ray3.20G1-156[»]
4V5LX-ray3.10G1-156[»]
4V5Melectron microscopy7.80G1-156[»]
4V5Nelectron microscopy7.60G1-156[»]
4V5PX-ray3.10G1-156[»]
4V5QX-ray3.10G1-156[»]
4V5RX-ray3.10G1-156[»]
4V5SX-ray3.10G1-156[»]
4V68electron microscopy6.40G2-156[»]
4V6AX-ray3.10G1-156[»]
4V6FX-ray3.10J1-156[»]
4V6GX-ray3.50J1-156[»]
4V7JX-ray3.30g1-156[»]
4V7KX-ray3.60g1-156[»]
4V7LX-ray3.15G1-156[»]
4V7MX-ray3.45G1-156[»]
4V7WX-ray3.00G1-156[»]
4V7XX-ray3.00G1-156[»]
4V7YX-ray3.00G1-156[»]
4V7ZX-ray3.10G1-156[»]
4V87X-ray3.10J1-156[»]
4V8AX-ray3.20G1-156[»]
4V8BX-ray3.00J1-156[»]
4V8CX-ray3.30J1-156[»]
4V8DX-ray3.00J1-156[»]
4V8EX-ray3.30J1-156[»]
4V8FX-ray3.30J1-156[»]
4V8GX-ray3.00G1-156[»]
4V8HX-ray3.10G1-156[»]
4V8IX-ray2.70G1-156[»]
4V8JX-ray3.90G1-156[»]
4V8NX-ray3.10G1-156[»]
4V8OX-ray3.80G1-156[»]
4V8QX-ray3.10G1-156[»]
4V8UX-ray3.70G1-156[»]
4V8XX-ray3.35G1-156[»]
4V90X-ray2.95G1-156[»]
4V95X-ray3.20G1-156[»]
4V97X-ray3.52G1-156[»]
4V9AX-ray3.30J1-156[»]
4V9BX-ray3.10J1-156[»]
4V9HX-ray2.86G2-156[»]
4V9IX-ray3.30G2-156[»]
4V9RX-ray3.00G1-156[»]
4V9SX-ray3.10G1-156[»]
4W2EX-ray2.90g1-156[»]
4W2GX-ray2.55G1-156[»]
4W2HX-ray2.70G1-156[»]
4W2IX-ray2.70G1-156[»]
ProteinModelPortaliP17291.
SMRiP17291. Positions 2-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17291.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S7P family.Curated

Phylogenomic databases

eggNOGiCOG0049.
HOGENOMiHOG000039067.
KOiK02992.
OMAiEVHRMAD.
OrthoDBiEOG6P5ZKW.
PhylomeDBiP17291.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
HAMAPiMF_00480_B. Ribosomal_S7_B.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005717. Ribosomal_S7_bac/org-type.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01029. rpsG_bact. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17291-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARRRRAEVR QLQPDLVYGD VLVTAFINKI MRDGKKNLAA RIFYDACKII
60 70 80 90 100
QEKTGQEPLK VFKQAVENVK PRMEVRSRRV GGANYQVPME VSPRRQQSLA
110 120 130 140 150
LRWLVQAANQ RPERRAAVRI AHELMDAAEG KGGAVKKKED VERMAEANRA

YAHYRW
Length:156
Mass (Da):18,016
Last modified:January 23, 2007 - v3
Checksum:iBC20C4487623B0E9
GO

Mass spectrometryi

Molecular mass is 17886 Da from positions 2 - 156. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52165 Genomic DNA. Translation: CAA36419.1.
AP008226 Genomic DNA. Translation: BAD71519.1.
RefSeqiYP_144962.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71519; BAD71519; BAD71519.
GeneIDi3167931.
KEGGittj:TTHA1696.
PATRICi23958347. VBITheThe93045_1666.

Cross-referencesi

Web resourcesi

T.thermophilus ribosome structure and function

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52165 Genomic DNA. Translation: CAA36419.1.
AP008226 Genomic DNA. Translation: BAD71519.1.
RefSeqiYP_144962.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DV4X-ray4.50G12-146[»]
1FJGX-ray3.00G1-156[»]
1FKAX-ray3.30G1-151[»]
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[»]
1QD7X-ray5.50F12-146[»]
1RSSX-ray1.90A7-156[»]
1TWTmodel-J2-156[»]
1VVJX-ray3.44G1-156[»]
1VY4X-ray2.60G1-156[»]
1VY5X-ray2.55G1-156[»]
1VY6X-ray2.90G1-156[»]
1VY7X-ray2.80G1-156[»]
1X18electron microscopy13.50F2-156[»]
1XMOX-ray3.25G1-156[»]
1XMQX-ray3.00G1-156[»]
1XNQX-ray3.05G1-156[»]
1XNRX-ray3.10G1-156[»]
2E5LX-ray3.30G2-156[»]
2F4VX-ray3.80G1-156[»]
2HHHX-ray3.35G1-156[»]
2J00X-ray2.80G2-156[»]
2J02X-ray2.80G2-156[»]
2UU9X-ray3.10G2-156[»]
2UUAX-ray2.90G2-156[»]
2UUBX-ray2.80G2-156[»]
2UUCX-ray3.10G2-156[»]
2UXBX-ray3.10G2-156[»]
2UXCX-ray2.90G2-156[»]
2UXDX-ray3.20G2-156[»]
2V46X-ray3.50G2-156[»]
2V48X-ray3.50G2-156[»]
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[»]
2ZM6X-ray3.30G2-156[»]
3OTOX-ray3.69G1-156[»]
3T1HX-ray3.11G1-156[»]
3T1YX-ray2.80G1-156[»]
4AQYX-ray3.50G2-156[»]
4B3MX-ray2.90G2-156[»]
4B3RX-ray3.00G2-156[»]
4B3SX-ray3.15G2-156[»]
4B3TX-ray3.00G2-156[»]
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[»]
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[»]
4JV5X-ray3.16G2-156[»]
4JYAX-ray3.10G2-156[»]
4K0KX-ray3.40G2-156[»]
4KHPX-ray3.10G2-156[»]
4L47X-ray3.22G1-156[»]
4L71X-ray3.90G1-156[»]
4LELX-ray3.90G1-156[»]
4LF4X-ray3.34G1-156[»]
4LF5X-ray3.75G1-156[»]
4LF6X-ray3.31G1-156[»]
4LF7X-ray3.15G1-156[»]
4LF8X-ray3.15G1-156[»]
4LF9X-ray3.28G1-156[»]
4LFAX-ray3.65G1-156[»]
4LFBX-ray3.01G1-156[»]
4LFCX-ray3.60G1-156[»]
4LFZX-ray3.92G1-156[»]
4LNTX-ray2.94G1-156[»]
4LSKX-ray3.48G1-156[»]
4LT8X-ray3.14G1-156[»]
4NXMX-ray3.65G1-156[»]
4NXNX-ray3.54G1-156[»]
4OX9X-ray3.80G2-156[»]
4P6FX-ray3.60H1-156[»]
4P70X-ray3.68G1-156[»]
4RB7X-ray2.40G1-156[»]
4V42X-ray5.50J1-156[»]
4V49X-ray8.70G2-156[»]
4V4AX-ray9.50G2-156[»]
4V4IX-ray3.71h-[»]
4V4PX-ray5.50J1-156[»]
4V4RX-ray5.90G1-156[»]
4V4SX-ray6.76G1-156[»]
4V4TX-ray6.46G1-156[»]
4V4XX-ray5.00J1-156[»]
4V4YX-ray5.50J1-156[»]
4V4ZX-ray4.51J1-156[»]
4V5FX-ray3.60G1-156[»]
4V5GX-ray3.60G1-156[»]
4V5JX-ray3.10G1-156[»]
4V5KX-ray3.20G1-156[»]
4V5LX-ray3.10G1-156[»]
4V5Melectron microscopy7.80G1-156[»]
4V5Nelectron microscopy7.60G1-156[»]
4V5PX-ray3.10G1-156[»]
4V5QX-ray3.10G1-156[»]
4V5RX-ray3.10G1-156[»]
4V5SX-ray3.10G1-156[»]
4V68electron microscopy6.40G2-156[»]
4V6AX-ray3.10G1-156[»]
4V6FX-ray3.10J1-156[»]
4V6GX-ray3.50J1-156[»]
4V7JX-ray3.30g1-156[»]
4V7KX-ray3.60g1-156[»]
4V7LX-ray3.15G1-156[»]
4V7MX-ray3.45G1-156[»]
4V7WX-ray3.00G1-156[»]
4V7XX-ray3.00G1-156[»]
4V7YX-ray3.00G1-156[»]
4V7ZX-ray3.10G1-156[»]
4V87X-ray3.10J1-156[»]
4V8AX-ray3.20G1-156[»]
4V8BX-ray3.00J1-156[»]
4V8CX-ray3.30J1-156[»]
4V8DX-ray3.00J1-156[»]
4V8EX-ray3.30J1-156[»]
4V8FX-ray3.30J1-156[»]
4V8GX-ray3.00G1-156[»]
4V8HX-ray3.10G1-156[»]
4V8IX-ray2.70G1-156[»]
4V8JX-ray3.90G1-156[»]
4V8NX-ray3.10G1-156[»]
4V8OX-ray3.80G1-156[»]
4V8QX-ray3.10G1-156[»]
4V8UX-ray3.70G1-156[»]
4V8XX-ray3.35G1-156[»]
4V90X-ray2.95G1-156[»]
4V95X-ray3.20G1-156[»]
4V97X-ray3.52G1-156[»]
4V9AX-ray3.30J1-156[»]
4V9BX-ray3.10J1-156[»]
4V9HX-ray2.86G2-156[»]
4V9IX-ray3.30G2-156[»]
4V9RX-ray3.00G1-156[»]
4V9SX-ray3.10G1-156[»]
4W2EX-ray2.90g1-156[»]
4W2GX-ray2.55G1-156[»]
4W2HX-ray2.70G1-156[»]
4W2IX-ray2.70G1-156[»]
ProteinModelPortaliP17291.
SMRiP17291. Positions 2-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-112129.
STRINGi300852.TTHA1696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71519; BAD71519; BAD71519.
GeneIDi3167931.
KEGGittj:TTHA1696.
PATRICi23958347. VBITheThe93045_1666.

Phylogenomic databases

eggNOGiCOG0049.
HOGENOMiHOG000039067.
KOiK02992.
OMAiEVHRMAD.
OrthoDBiEOG6P5ZKW.
PhylomeDBiP17291.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1735-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP17291.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
HAMAPiMF_00480_B. Ribosomal_S7_B.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005717. Ribosomal_S7_bac/org-type.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01029. rpsG_bact. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiRS7_THET8
AccessioniPrimary (citable) accession number: P17291
Secondary accession number(s): Q5SHN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.