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Protein

30S ribosomal protein S9

Gene

rpsI

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Part of the top of the head of the 30S subunit. The C-terminal region penetrates the head emerging in the P-site where it contacts tRNA.

GO - Molecular functioni

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

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-1500-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S9
Gene namesi
Name:rpsI
Synonyms:rps9
Ordered Locus Names:TTHA1464
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12812830S ribosomal protein S9PRO_0000111431Add
BLAST

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S7 and S10.

Protein-protein interaction databases

STRINGi300852.TTHA1464.

Structurei

Secondary structure

1
128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Beta strandi13 – 2412Combined sources
Beta strandi26 – 283Combined sources
Beta strandi30 – 323Combined sources
Helixi33 – 364Combined sources
Turni37 – 393Combined sources
Helixi41 – 455Combined sources
Turni46 – 483Combined sources
Helixi49 – 524Combined sources
Turni56 – 583Combined sources
Beta strandi59 – 6810Combined sources
Helixi70 – 8819Combined sources
Helixi90 – 923Combined sources
Turni94 – 1007Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi116 – 1205Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00I1-128[»]
1HNWX-ray3.40I1-128[»]
1HNXX-ray3.40I1-128[»]
1HNZX-ray3.30I1-128[»]
1HR0X-ray3.20I1-128[»]
1I94X-ray3.20I1-128[»]
1I95X-ray4.50I1-128[»]
1I96X-ray4.20I1-128[»]
1I97X-ray4.50I1-128[»]
1IBKX-ray3.31I1-128[»]
1IBLX-ray3.11I1-128[»]
1IBMX-ray3.31I1-128[»]
1J5EX-ray3.05I1-128[»]
1JGOX-ray5.60L1-128[»]
1JGPX-ray7.00L1-128[»]
1JGQX-ray5.00L1-128[»]
1L1Umodel-I2-128[»]
1ML5electron microscopy14.00L1-128[»]
1N32X-ray3.00I1-128[»]
1N33X-ray3.35I1-128[»]
1N34X-ray3.80I1-128[»]
1N36X-ray3.65I1-128[»]
1VVJX-ray3.44I1-128[»]
1VY4X-ray2.60I1-128[»]
1VY5X-ray2.55I1-128[»]
1VY6X-ray2.90I1-128[»]
1VY7X-ray2.80I1-128[»]
1XMOX-ray3.25I1-128[»]
1XNQX-ray3.05I1-128[»]
1XNRX-ray3.10I1-128[»]
2E5LX-ray3.30I1-128[»]
2F4VX-ray3.80I1-128[»]
2HHHX-ray3.35I1-128[»]
2UU9X-ray3.10I1-128[»]
2UUAX-ray2.90I1-128[»]
2UUBX-ray2.90I1-128[»]
2UUCX-ray3.10I1-128[»]
2ZM6X-ray3.30I1-128[»]
3OTOX-ray3.69I1-128[»]
4AQYX-ray3.50I1-128[»]
4B3MX-ray2.90I1-128[»]
4B3RX-ray3.00I1-128[»]
4B3SX-ray3.15I1-128[»]
4B3TX-ray3.00I1-128[»]
4DR1X-ray3.60I1-128[»]
4DR2X-ray3.25I1-128[»]
4DR3X-ray3.35I1-128[»]
4DR4X-ray3.97I1-128[»]
4DR5X-ray3.45I1-128[»]
4DR6X-ray3.30I1-128[»]
4DR7X-ray3.75I1-128[»]
4DUYX-ray3.39I1-128[»]
4DUZX-ray3.65I1-128[»]
4DV0X-ray3.85I1-128[»]
4DV1X-ray3.85I1-128[»]
4DV2X-ray3.65I1-128[»]
4DV3X-ray3.55I1-128[»]
4DV4X-ray3.65I1-128[»]
4DV5X-ray3.68I1-128[»]
4DV6X-ray3.30I1-128[»]
4DV7X-ray3.29I1-128[»]
4GKJX-ray3.30I2-128[»]
4GKKX-ray3.20I2-128[»]
4JI0X-ray3.49I1-128[»]
4JI1X-ray3.14I1-128[»]
4JI2X-ray3.64I1-128[»]
4JI3X-ray3.35I1-128[»]
4JI4X-ray3.69I1-128[»]
4JI5X-ray3.85I1-128[»]
4JI6X-ray3.55I1-128[»]
4JI7X-ray3.50I1-128[»]
4JI8X-ray3.74I1-128[»]
4JV5X-ray3.16I2-128[»]
4JYAX-ray3.10I2-128[»]
4K0KX-ray3.40I2-128[»]
4KHPX-ray3.10I2-128[»]
4L47X-ray3.22I1-128[»]
4L71X-ray3.90I1-128[»]
4LELX-ray3.90I1-128[»]
4LF4X-ray3.34I1-128[»]
4LF5X-ray3.75I1-128[»]
4LF6X-ray3.31I1-128[»]
4LF7X-ray3.15I1-128[»]
4LF8X-ray3.15I1-128[»]
4LF9X-ray3.28I1-128[»]
4LFAX-ray3.65I1-128[»]
4LFBX-ray3.01I1-128[»]
4LFCX-ray3.60I1-128[»]
4LFZX-ray3.92I1-128[»]
4LNTX-ray2.94I1-128[»]
4LSKX-ray3.48I1-128[»]
4LT8X-ray3.14I1-128[»]
4NXMX-ray3.65I1-128[»]
4NXNX-ray3.54I1-128[»]
4OX9X-ray3.80I1-128[»]
4P6FX-ray3.60J1-128[»]
4P70X-ray3.68I1-128[»]
4RB7X-ray2.40I1-128[»]
4V42X-ray5.50L1-128[»]
4V49X-ray8.70I2-128[»]
4V4AX-ray9.50I2-128[»]
4V4IX-ray3.71j1-128[»]
4V4PX-ray5.50L1-128[»]
4V4RX-ray5.90I1-128[»]
4V4SX-ray6.76I1-128[»]
4V4TX-ray6.46I1-128[»]
4V4XX-ray5.00L1-128[»]
4V4YX-ray5.50L1-128[»]
4V4ZX-ray4.51L1-128[»]
4V5FX-ray3.60I1-128[»]
4V5GX-ray3.60I1-128[»]
4V5JX-ray3.10I1-128[»]
4V5KX-ray3.20I1-128[»]
4V5LX-ray3.10I1-128[»]
4V5Melectron microscopy7.80I1-128[»]
4V5Nelectron microscopy7.60I1-128[»]
4V5PX-ray3.10I1-128[»]
4V5QX-ray3.10I1-128[»]
4V5RX-ray3.10I1-128[»]
4V5SX-ray3.10I1-128[»]
4V68electron microscopy6.40I2-128[»]
4V6AX-ray3.10I1-128[»]
4V6FX-ray3.10L1-128[»]
4V6GX-ray3.50L1-128[»]
4V7JX-ray3.30i1-128[»]
4V7KX-ray3.60i1-128[»]
4V7LX-ray3.00I1-128[»]
4V7MX-ray3.45I1-128[»]
4V7WX-ray3.00I1-128[»]
4V7XX-ray3.00I1-128[»]
4V7YX-ray3.00I1-128[»]
4V7ZX-ray3.10I1-128[»]
4V87X-ray3.10L1-128[»]
4V8AX-ray3.20I1-128[»]
4V8BX-ray3.00L1-128[»]
4V8CX-ray3.30L1-128[»]
4V8DX-ray3.00L1-128[»]
4V8EX-ray3.30L1-128[»]
4V8FX-ray3.30L1-128[»]
4V8GX-ray3.00I1-128[»]
4V8HX-ray3.10I1-128[»]
4V8IX-ray2.70I1-128[»]
4V8JX-ray3.90I1-128[»]
4V8NX-ray3.10I1-128[»]
4V8OX-ray3.80I1-128[»]
4V8QX-ray3.10I1-128[»]
4V8UX-ray3.70I1-128[»]
4V8XX-ray3.35I1-128[»]
4V90X-ray2.95I1-128[»]
4V95X-ray3.20I1-128[»]
4V97X-ray3.52I1-128[»]
4V9AX-ray3.30L1-128[»]
4V9BX-ray3.10L1-128[»]
4V9HX-ray2.86I2-128[»]
4V9IX-ray3.30I2-128[»]
4V9RX-ray3.00I1-128[»]
4V9SX-ray3.10I1-128[»]
4W2EX-ray2.90i1-128[»]
4W2FX-ray2.40I1-128[»]
4W2GX-ray2.55I1-128[»]
4W2HX-ray2.70I1-128[»]
4W2IX-ray2.70I1-128[»]
ProteinModelPortaliP80374.
SMRiP80374. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80374.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S9P family.Curated

Phylogenomic databases

eggNOGiCOG0103.
HOGENOMiHOG000019802.
KOiK02996.
OMAiIKQGAAR.
OrthoDBiEOG6MWNH0.
PhylomeDBiP80374.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00532_B. Ribosomal_S9_B.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR023035. Ribosomal_S9_bac/plastid.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80374-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEQYYGTGRR KEAVARVFLR PGNGKVTVNG QDFNEYFQGL VRAVAALEPL
60 70 80 90 100
RAVDALGHFD AYITVRGGGK SGQIDAIKLG IARALVQYNP DYRAKLKPLG
110 120
FLTRDARVVE RKKYGKHKAR RAPQYSKR
Length:128
Mass (Da):14,383
Last modified:May 10, 2005 - v3
Checksum:iFA9A4ED2CC5D8CC1
GO

Mass spectrometryi

Molecular mass is 14384 Da from positions 1 - 128. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71287.1.
RefSeqiWP_011228699.1. NC_006461.1.
YP_144730.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71287; BAD71287; BAD71287.
GeneIDi3169752.
KEGGittj:TTHA1464.
PATRICi23957885. VBITheThe93045_1438.

Cross-referencesi

Web resourcesi

T.thermophilus ribosome structure and function

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71287.1.
RefSeqiWP_011228699.1. NC_006461.1.
YP_144730.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00I1-128[»]
1HNWX-ray3.40I1-128[»]
1HNXX-ray3.40I1-128[»]
1HNZX-ray3.30I1-128[»]
1HR0X-ray3.20I1-128[»]
1I94X-ray3.20I1-128[»]
1I95X-ray4.50I1-128[»]
1I96X-ray4.20I1-128[»]
1I97X-ray4.50I1-128[»]
1IBKX-ray3.31I1-128[»]
1IBLX-ray3.11I1-128[»]
1IBMX-ray3.31I1-128[»]
1J5EX-ray3.05I1-128[»]
1JGOX-ray5.60L1-128[»]
1JGPX-ray7.00L1-128[»]
1JGQX-ray5.00L1-128[»]
1L1Umodel-I2-128[»]
1ML5electron microscopy14.00L1-128[»]
1N32X-ray3.00I1-128[»]
1N33X-ray3.35I1-128[»]
1N34X-ray3.80I1-128[»]
1N36X-ray3.65I1-128[»]
1VVJX-ray3.44I1-128[»]
1VY4X-ray2.60I1-128[»]
1VY5X-ray2.55I1-128[»]
1VY6X-ray2.90I1-128[»]
1VY7X-ray2.80I1-128[»]
1XMOX-ray3.25I1-128[»]
1XNQX-ray3.05I1-128[»]
1XNRX-ray3.10I1-128[»]
2E5LX-ray3.30I1-128[»]
2F4VX-ray3.80I1-128[»]
2HHHX-ray3.35I1-128[»]
2UU9X-ray3.10I1-128[»]
2UUAX-ray2.90I1-128[»]
2UUBX-ray2.90I1-128[»]
2UUCX-ray3.10I1-128[»]
2ZM6X-ray3.30I1-128[»]
3OTOX-ray3.69I1-128[»]
4AQYX-ray3.50I1-128[»]
4B3MX-ray2.90I1-128[»]
4B3RX-ray3.00I1-128[»]
4B3SX-ray3.15I1-128[»]
4B3TX-ray3.00I1-128[»]
4DR1X-ray3.60I1-128[»]
4DR2X-ray3.25I1-128[»]
4DR3X-ray3.35I1-128[»]
4DR4X-ray3.97I1-128[»]
4DR5X-ray3.45I1-128[»]
4DR6X-ray3.30I1-128[»]
4DR7X-ray3.75I1-128[»]
4DUYX-ray3.39I1-128[»]
4DUZX-ray3.65I1-128[»]
4DV0X-ray3.85I1-128[»]
4DV1X-ray3.85I1-128[»]
4DV2X-ray3.65I1-128[»]
4DV3X-ray3.55I1-128[»]
4DV4X-ray3.65I1-128[»]
4DV5X-ray3.68I1-128[»]
4DV6X-ray3.30I1-128[»]
4DV7X-ray3.29I1-128[»]
4GKJX-ray3.30I2-128[»]
4GKKX-ray3.20I2-128[»]
4JI0X-ray3.49I1-128[»]
4JI1X-ray3.14I1-128[»]
4JI2X-ray3.64I1-128[»]
4JI3X-ray3.35I1-128[»]
4JI4X-ray3.69I1-128[»]
4JI5X-ray3.85I1-128[»]
4JI6X-ray3.55I1-128[»]
4JI7X-ray3.50I1-128[»]
4JI8X-ray3.74I1-128[»]
4JV5X-ray3.16I2-128[»]
4JYAX-ray3.10I2-128[»]
4K0KX-ray3.40I2-128[»]
4KHPX-ray3.10I2-128[»]
4L47X-ray3.22I1-128[»]
4L71X-ray3.90I1-128[»]
4LELX-ray3.90I1-128[»]
4LF4X-ray3.34I1-128[»]
4LF5X-ray3.75I1-128[»]
4LF6X-ray3.31I1-128[»]
4LF7X-ray3.15I1-128[»]
4LF8X-ray3.15I1-128[»]
4LF9X-ray3.28I1-128[»]
4LFAX-ray3.65I1-128[»]
4LFBX-ray3.01I1-128[»]
4LFCX-ray3.60I1-128[»]
4LFZX-ray3.92I1-128[»]
4LNTX-ray2.94I1-128[»]
4LSKX-ray3.48I1-128[»]
4LT8X-ray3.14I1-128[»]
4NXMX-ray3.65I1-128[»]
4NXNX-ray3.54I1-128[»]
4OX9X-ray3.80I1-128[»]
4P6FX-ray3.60J1-128[»]
4P70X-ray3.68I1-128[»]
4RB7X-ray2.40I1-128[»]
4V42X-ray5.50L1-128[»]
4V49X-ray8.70I2-128[»]
4V4AX-ray9.50I2-128[»]
4V4IX-ray3.71j1-128[»]
4V4PX-ray5.50L1-128[»]
4V4RX-ray5.90I1-128[»]
4V4SX-ray6.76I1-128[»]
4V4TX-ray6.46I1-128[»]
4V4XX-ray5.00L1-128[»]
4V4YX-ray5.50L1-128[»]
4V4ZX-ray4.51L1-128[»]
4V5FX-ray3.60I1-128[»]
4V5GX-ray3.60I1-128[»]
4V5JX-ray3.10I1-128[»]
4V5KX-ray3.20I1-128[»]
4V5LX-ray3.10I1-128[»]
4V5Melectron microscopy7.80I1-128[»]
4V5Nelectron microscopy7.60I1-128[»]
4V5PX-ray3.10I1-128[»]
4V5QX-ray3.10I1-128[»]
4V5RX-ray3.10I1-128[»]
4V5SX-ray3.10I1-128[»]
4V68electron microscopy6.40I2-128[»]
4V6AX-ray3.10I1-128[»]
4V6FX-ray3.10L1-128[»]
4V6GX-ray3.50L1-128[»]
4V7JX-ray3.30i1-128[»]
4V7KX-ray3.60i1-128[»]
4V7LX-ray3.00I1-128[»]
4V7MX-ray3.45I1-128[»]
4V7WX-ray3.00I1-128[»]
4V7XX-ray3.00I1-128[»]
4V7YX-ray3.00I1-128[»]
4V7ZX-ray3.10I1-128[»]
4V87X-ray3.10L1-128[»]
4V8AX-ray3.20I1-128[»]
4V8BX-ray3.00L1-128[»]
4V8CX-ray3.30L1-128[»]
4V8DX-ray3.00L1-128[»]
4V8EX-ray3.30L1-128[»]
4V8FX-ray3.30L1-128[»]
4V8GX-ray3.00I1-128[»]
4V8HX-ray3.10I1-128[»]
4V8IX-ray2.70I1-128[»]
4V8JX-ray3.90I1-128[»]
4V8NX-ray3.10I1-128[»]
4V8OX-ray3.80I1-128[»]
4V8QX-ray3.10I1-128[»]
4V8UX-ray3.70I1-128[»]
4V8XX-ray3.35I1-128[»]
4V90X-ray2.95I1-128[»]
4V95X-ray3.20I1-128[»]
4V97X-ray3.52I1-128[»]
4V9AX-ray3.30L1-128[»]
4V9BX-ray3.10L1-128[»]
4V9HX-ray2.86I2-128[»]
4V9IX-ray3.30I2-128[»]
4V9RX-ray3.00I1-128[»]
4V9SX-ray3.10I1-128[»]
4W2EX-ray2.90i1-128[»]
4W2FX-ray2.40I1-128[»]
4W2GX-ray2.55I1-128[»]
4W2HX-ray2.70I1-128[»]
4W2IX-ray2.70I1-128[»]
ProteinModelPortaliP80374.
SMRiP80374. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1464.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71287; BAD71287; BAD71287.
GeneIDi3169752.
KEGGittj:TTHA1464.
PATRICi23957885. VBITheThe93045_1438.

Phylogenomic databases

eggNOGiCOG0103.
HOGENOMiHOG000019802.
KOiK02996.
OMAiIKQGAAR.
OrthoDBiEOG6MWNH0.
PhylomeDBiP80374.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1500-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP80374.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00532_B. Ribosomal_S9_B.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR023035. Ribosomal_S9_bac/plastid.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
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Publicationsi

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  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 1-28.
  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. Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
  5. "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.
  6. "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.
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
  12. "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.
  13. "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.

Entry informationi

Entry nameiRS9_THET8
AccessioniPrimary (citable) accession number: P80374
Secondary accession number(s): Q5SIB0, Q9ACJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 10, 2005
Last modified: February 4, 2015
This is version 130 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.