Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

30S ribosomal protein S12

Gene

rpsL

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

With S4 and S5 plays an important role in translational accuracy.By similarity
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1736-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S12
Gene namesi
Name:rpsL
Ordered Locus Names:TTHA1697
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 13213130S ribosomal protein S12PRO_0000146341Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 8913-methylthioaspartic acid1 Publication

Keywords - PTMi

Methylation

Proteomic databases

PRIDEiQ5SHN3.

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S8 and S17. May interact with IF1 in the 30S initiation complex.

Protein-protein interaction databases

STRINGi300852.TTHA1697.

Structurei

Secondary structure

1
132
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 96Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 358Combined sources
Beta strandi50 – 523Combined sources
Beta strandi54 – 574Combined sources
Turni58 – 603Combined sources
Beta strandi62 – 665Combined sources
Beta strandi69 – 713Combined sources
Beta strandi79 – 846Combined sources
Beta strandi88 – 903Combined sources
Beta strandi95 – 973Combined sources
Turni101 – 1044Combined sources
Helixi114 – 1174Combined sources
Helixi123 – 1253Combined sources
Beta strandi128 – 1303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00L2-132[»]
1HNWX-ray3.40L2-132[»]
1HNXX-ray3.40L2-132[»]
1HNZX-ray3.30L2-132[»]
1HR0X-ray3.20L2-132[»]
1I94X-ray3.20L2-132[»]
1I95X-ray4.50L2-132[»]
1I96X-ray4.20L2-132[»]
1I97X-ray4.50L2-132[»]
1IBKX-ray3.31L2-132[»]
1IBLX-ray3.11L2-132[»]
1IBMX-ray3.31L2-132[»]
1J5EX-ray3.05L2-132[»]
1JGOX-ray5.60O2-132[»]
1JGPX-ray7.00O2-132[»]
1JGQX-ray5.00O2-132[»]
1L1Umodel-L1-125[»]
1ML5electron microscopy14.00O2-132[»]
1MVRelectron microscopy12.80O2-132[»]
1N32X-ray3.00L2-132[»]
1N33X-ray3.35L2-132[»]
1N34X-ray3.80L2-132[»]
1N36X-ray3.65L2-132[»]
1PN7electron microscopy10.80O2-125[»]
1PN8electron microscopy10.80O2-125[»]
1QZCelectron microscopy9.00L2-132[»]
1VVJX-ray3.44QL/XL1-132[»]
1VY4X-ray2.60AL/CL1-132[»]
1VY5X-ray2.55AL/CL1-132[»]
1VY6X-ray2.90AL/CL1-132[»]
1VY7X-ray2.80AL/CL1-132[»]
1XMOX-ray3.25L2-132[»]
1XMQX-ray3.00L2-132[»]
1XNQX-ray3.05L2-132[»]
1XNRX-ray3.10L2-132[»]
2E5LX-ray3.30L2-132[»]
2F4VX-ray3.80L1-132[»]
2HHHX-ray3.35L2-132[»]
2UU9X-ray3.10L2-132[»]
2UUAX-ray2.90L2-132[»]
2UUBX-ray2.80L2-132[»]
2UUCX-ray3.10L2-132[»]
2UXBX-ray3.10L2-132[»]
2UXCX-ray2.90L2-132[»]
2UXDX-ray3.20L2-132[»]
2VQEX-ray2.50L2-132[»]
2VQFX-ray2.90L2-132[»]
2ZM6X-ray3.30L2-132[»]
3OTOX-ray3.69L2-132[»]
3T1HX-ray3.11L1-132[»]
3T1YX-ray2.80L1-132[»]
4AQYX-ray3.50L2-132[»]
4B3MX-ray2.90L1-132[»]
4B3RX-ray3.00L1-132[»]
4B3SX-ray3.15L1-132[»]
4B3TX-ray3.00L1-132[»]
4DUYX-ray3.39L2-132[»]
4DUZX-ray3.65L2-132[»]
4DV0X-ray3.85L2-132[»]
4DV1X-ray3.85L2-132[»]
4DV2X-ray3.65L2-132[»]
4DV3X-ray3.55L2-132[»]
4DV4X-ray3.65L2-132[»]
4DV5X-ray3.68L2-132[»]
4DV6X-ray3.30L2-132[»]
4DV7X-ray3.29L2-132[»]
4GKJX-ray3.30L2-125[»]
4GKKX-ray3.20L2-125[»]
4JI0X-ray3.49L2-132[»]
4JI1X-ray3.14L2-132[»]
4JI2X-ray3.64L2-132[»]
4JI3X-ray3.35L2-132[»]
4JI4X-ray3.69L2-132[»]
4JI5X-ray3.85L2-132[»]
4JI6X-ray3.55L2-132[»]
4JI7X-ray3.50L2-132[»]
4JI8X-ray3.74L2-132[»]
4JV5X-ray3.16L2-126[»]
4JYAX-ray3.10L2-126[»]
4K0KX-ray3.40L2-127[»]
4KHPX-ray3.10L2-126[»]
4L47X-ray3.22QL/XL1-132[»]
4L71X-ray3.90QL/XL1-132[»]
4LELX-ray3.90QL/XL1-132[»]
4LFZX-ray3.92QL/XL1-132[»]
4LNTX-ray2.94QL/XL1-132[»]
4LSKX-ray3.48QL/XL1-132[»]
4LT8X-ray3.14QL/XL1-132[»]
4OX9X-ray3.80L1-131[»]
4P6FX-ray3.60QL/XL1-132[»]
4P70X-ray3.68QL/XL1-132[»]
4TUAX-ray3.60QL/XL1-132[»]
4TUBX-ray3.60QL/XL1-132[»]
4TUCX-ray3.60QL/XL1-132[»]
4TUDX-ray3.60QL/XL1-132[»]
4TUEX-ray3.50QL/XL1-132[»]
4V42X-ray5.50AO2-132[»]
4V49X-ray8.70L2-125[»]
4V4AX-ray9.50L2-125[»]
4V4IX-ray3.71m1-132[»]
4V4PX-ray5.50BO2-132[»]
4V4RX-ray5.90L2-132[»]
4V4SX-ray6.76L2-132[»]
4V4TX-ray6.46L2-132[»]
4V4XX-ray5.00AO1-132[»]
4V4YX-ray5.50AO1-132[»]
4V4ZX-ray4.51AO1-132[»]
4V51X-ray2.80AL/CL2-132[»]
4V5AX-ray3.50AL/CL2-132[»]
4V5CX-ray3.30AL/CL2-132[»]
4V5DX-ray3.50AL/CL2-132[»]
4V5EX-ray3.45AL/CL1-132[»]
4V5FX-ray3.60AL/CL1-132[»]
4V5GX-ray3.60AL/CL2-132[»]
4V5JX-ray3.10AL/CL1-132[»]
4V5KX-ray3.20AL/CL2-132[»]
4V5LX-ray3.10AL2-132[»]
4V5Melectron microscopy7.80AL1-132[»]
4V5Nelectron microscopy7.60AL1-132[»]
4V5PX-ray3.10AL/CL2-132[»]
4V5QX-ray3.10AL/CL1-132[»]
4V5RX-ray3.10AL/CL2-132[»]
4V5SX-ray3.10AL/CL2-132[»]
4V68electron microscopy6.40AL2-126[»]
4V6AX-ray3.10AL/CL1-132[»]
4V6FX-ray3.10BO/CO1-132[»]
4V6GX-ray3.50AO/CO1-132[»]
4V7JX-ray3.30Al/Bl1-132[»]
4V7KX-ray3.60Al/Bl1-132[»]
4V7LX-ray3.00AL/CL1-132[»]
4V7MX-ray3.45AL/CL1-132[»]
4V7WX-ray3.00AL/CL1-132[»]
4V7XX-ray3.00AL/CL1-132[»]
4V7YX-ray3.00AL/CL1-132[»]
4V7ZX-ray3.10AL/CL1-132[»]
4V87X-ray3.10BO/CO1-132[»]
4V8AX-ray3.20CL/DL1-132[»]
4V8BX-ray3.00AO/CO1-128[»]
4V8CX-ray3.30CO/DO1-132[»]
4V8DX-ray3.00AO/CO1-132[»]
4V8EX-ray3.30BO/DO1-132[»]
4V8FX-ray3.30BO/CO1-132[»]
4V8GX-ray3.00AL/CL1-132[»]
4V8HX-ray3.10AL/CL1-132[»]
4V8IX-ray2.70AL/CL1-132[»]
4V8JX-ray3.90AL/CL1-132[»]
4V8NX-ray3.10AL/CL2-132[»]
4V8OX-ray3.80AL2-132[»]
4V8QX-ray3.10BL2-132[»]
4V8UX-ray3.70AL/CL1-132[»]
4V8XX-ray3.35AL/CL1-132[»]
4V90X-ray2.95AL1-132[»]
4V95X-ray3.20AL/CL1-132[»]
4V97X-ray3.52AL/CL1-132[»]
4V9AX-ray3.30AO/CO1-127[»]
4V9BX-ray3.10AO/CO1-127[»]
4V9HX-ray2.86AL2-125[»]
4V9IX-ray3.30AL/CL2-125[»]
4V9RX-ray3.00AL/CL1-132[»]
4V9SX-ray3.10AL/CL1-132[»]
4W2EX-ray2.90l1-132[»]
4W2FX-ray2.40AL/CL1-132[»]
4W2GX-ray2.55AL/CL1-132[»]
4W2HX-ray2.70AL/CL1-132[»]
4W2IX-ray2.70AL/CL1-132[»]
4WPOX-ray2.80BL/DL1-132[»]
4WQFX-ray2.80BL/DL1-132[»]
4WQUX-ray2.80BL/DL1-132[»]
4WQYX-ray2.80BL/DL1-132[»]
4WT8X-ray3.40L2-125[»]
4WUSX-ray3.40L2-125[»]
4Y4OX-ray2.301l/2l1-132[»]
4Y4PX-ray2.501l/2l1-132[»]
4YHHX-ray3.42L2-125[»]
4Z3QX-ray2.601l/2l1-132[»]
4Z3RX-ray3.101l/2l1-132[»]
4Z3SX-ray2.651l/2l1-132[»]
4Z8CX-ray2.901l/2l1-132[»]
4ZERX-ray3.101l/2l2-123[»]
ProteinModelPortaliQ5SHN3.
SMRiQ5SHN3. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHN3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12P family.Curated

Phylogenomic databases

eggNOGiCOG0048.
HOGENOMiHOG000040063.
KOiK02950.
OMAiQVTSARR.
OrthoDBiEOG61ZTNF.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
PRINTSiPR01034. RIBOSOMALS12.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00981. rpsL_bact. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5SHN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTINQLVRK GREKVRKKSK VPALKGAPFR RGVCTVVRTV TPKKPNSALR
60 70 80 90 100
KVAKVRLTSG YEVTAYIPGE GHNLQEHSVV LIRGGRVKDL PGVRYHIVRG
110 120 130
VYDAAGVKDR KKSRSKYGTK KPKEAAKTAA KK
Length:132
Mass (Da):14,599
Last modified:January 23, 2007 - v3
Checksum:i9943D095FAD4D9BC
GO

Sequence cautioni

The sequence BAD71520.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA36418.1 differs from that shown. Reason: Erroneous initiation. Curated

Mass spectrometryi

Molecular mass is 14516 Da from positions 2 - 132. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52165 Genomic DNA. Translation: CAA36418.1. Different initiation.
AP008226 Genomic DNA. Translation: BAD71520.1. Different initiation.
PIRiS10249. R3TW12.
RefSeqiYP_144963.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71520; BAD71520; BAD71520.
GeneIDi3169892.
KEGGittj:TTHA1697.
PATRICi23958349. VBITheThe93045_1667.

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: CAA36418.1. Different initiation.
AP008226 Genomic DNA. Translation: BAD71520.1. Different initiation.
PIRiS10249. R3TW12.
RefSeqiYP_144963.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00L2-132[»]
1HNWX-ray3.40L2-132[»]
1HNXX-ray3.40L2-132[»]
1HNZX-ray3.30L2-132[»]
1HR0X-ray3.20L2-132[»]
1I94X-ray3.20L2-132[»]
1I95X-ray4.50L2-132[»]
1I96X-ray4.20L2-132[»]
1I97X-ray4.50L2-132[»]
1IBKX-ray3.31L2-132[»]
1IBLX-ray3.11L2-132[»]
1IBMX-ray3.31L2-132[»]
1J5EX-ray3.05L2-132[»]
1JGOX-ray5.60O2-132[»]
1JGPX-ray7.00O2-132[»]
1JGQX-ray5.00O2-132[»]
1L1Umodel-L1-125[»]
1ML5electron microscopy14.00O2-132[»]
1MVRelectron microscopy12.80O2-132[»]
1N32X-ray3.00L2-132[»]
1N33X-ray3.35L2-132[»]
1N34X-ray3.80L2-132[»]
1N36X-ray3.65L2-132[»]
1PN7electron microscopy10.80O2-125[»]
1PN8electron microscopy10.80O2-125[»]
1QZCelectron microscopy9.00L2-132[»]
1VVJX-ray3.44QL/XL1-132[»]
1VY4X-ray2.60AL/CL1-132[»]
1VY5X-ray2.55AL/CL1-132[»]
1VY6X-ray2.90AL/CL1-132[»]
1VY7X-ray2.80AL/CL1-132[»]
1XMOX-ray3.25L2-132[»]
1XMQX-ray3.00L2-132[»]
1XNQX-ray3.05L2-132[»]
1XNRX-ray3.10L2-132[»]
2E5LX-ray3.30L2-132[»]
2F4VX-ray3.80L1-132[»]
2HHHX-ray3.35L2-132[»]
2UU9X-ray3.10L2-132[»]
2UUAX-ray2.90L2-132[»]
2UUBX-ray2.80L2-132[»]
2UUCX-ray3.10L2-132[»]
2UXBX-ray3.10L2-132[»]
2UXCX-ray2.90L2-132[»]
2UXDX-ray3.20L2-132[»]
2VQEX-ray2.50L2-132[»]
2VQFX-ray2.90L2-132[»]
2ZM6X-ray3.30L2-132[»]
3OTOX-ray3.69L2-132[»]
3T1HX-ray3.11L1-132[»]
3T1YX-ray2.80L1-132[»]
4AQYX-ray3.50L2-132[»]
4B3MX-ray2.90L1-132[»]
4B3RX-ray3.00L1-132[»]
4B3SX-ray3.15L1-132[»]
4B3TX-ray3.00L1-132[»]
4DUYX-ray3.39L2-132[»]
4DUZX-ray3.65L2-132[»]
4DV0X-ray3.85L2-132[»]
4DV1X-ray3.85L2-132[»]
4DV2X-ray3.65L2-132[»]
4DV3X-ray3.55L2-132[»]
4DV4X-ray3.65L2-132[»]
4DV5X-ray3.68L2-132[»]
4DV6X-ray3.30L2-132[»]
4DV7X-ray3.29L2-132[»]
4GKJX-ray3.30L2-125[»]
4GKKX-ray3.20L2-125[»]
4JI0X-ray3.49L2-132[»]
4JI1X-ray3.14L2-132[»]
4JI2X-ray3.64L2-132[»]
4JI3X-ray3.35L2-132[»]
4JI4X-ray3.69L2-132[»]
4JI5X-ray3.85L2-132[»]
4JI6X-ray3.55L2-132[»]
4JI7X-ray3.50L2-132[»]
4JI8X-ray3.74L2-132[»]
4JV5X-ray3.16L2-126[»]
4JYAX-ray3.10L2-126[»]
4K0KX-ray3.40L2-127[»]
4KHPX-ray3.10L2-126[»]
4L47X-ray3.22QL/XL1-132[»]
4L71X-ray3.90QL/XL1-132[»]
4LELX-ray3.90QL/XL1-132[»]
4LFZX-ray3.92QL/XL1-132[»]
4LNTX-ray2.94QL/XL1-132[»]
4LSKX-ray3.48QL/XL1-132[»]
4LT8X-ray3.14QL/XL1-132[»]
4OX9X-ray3.80L1-131[»]
4P6FX-ray3.60QL/XL1-132[»]
4P70X-ray3.68QL/XL1-132[»]
4TUAX-ray3.60QL/XL1-132[»]
4TUBX-ray3.60QL/XL1-132[»]
4TUCX-ray3.60QL/XL1-132[»]
4TUDX-ray3.60QL/XL1-132[»]
4TUEX-ray3.50QL/XL1-132[»]
4V42X-ray5.50AO2-132[»]
4V49X-ray8.70L2-125[»]
4V4AX-ray9.50L2-125[»]
4V4IX-ray3.71m1-132[»]
4V4PX-ray5.50BO2-132[»]
4V4RX-ray5.90L2-132[»]
4V4SX-ray6.76L2-132[»]
4V4TX-ray6.46L2-132[»]
4V4XX-ray5.00AO1-132[»]
4V4YX-ray5.50AO1-132[»]
4V4ZX-ray4.51AO1-132[»]
4V51X-ray2.80AL/CL2-132[»]
4V5AX-ray3.50AL/CL2-132[»]
4V5CX-ray3.30AL/CL2-132[»]
4V5DX-ray3.50AL/CL2-132[»]
4V5EX-ray3.45AL/CL1-132[»]
4V5FX-ray3.60AL/CL1-132[»]
4V5GX-ray3.60AL/CL2-132[»]
4V5JX-ray3.10AL/CL1-132[»]
4V5KX-ray3.20AL/CL2-132[»]
4V5LX-ray3.10AL2-132[»]
4V5Melectron microscopy7.80AL1-132[»]
4V5Nelectron microscopy7.60AL1-132[»]
4V5PX-ray3.10AL/CL2-132[»]
4V5QX-ray3.10AL/CL1-132[»]
4V5RX-ray3.10AL/CL2-132[»]
4V5SX-ray3.10AL/CL2-132[»]
4V68electron microscopy6.40AL2-126[»]
4V6AX-ray3.10AL/CL1-132[»]
4V6FX-ray3.10BO/CO1-132[»]
4V6GX-ray3.50AO/CO1-132[»]
4V7JX-ray3.30Al/Bl1-132[»]
4V7KX-ray3.60Al/Bl1-132[»]
4V7LX-ray3.00AL/CL1-132[»]
4V7MX-ray3.45AL/CL1-132[»]
4V7WX-ray3.00AL/CL1-132[»]
4V7XX-ray3.00AL/CL1-132[»]
4V7YX-ray3.00AL/CL1-132[»]
4V7ZX-ray3.10AL/CL1-132[»]
4V87X-ray3.10BO/CO1-132[»]
4V8AX-ray3.20CL/DL1-132[»]
4V8BX-ray3.00AO/CO1-128[»]
4V8CX-ray3.30CO/DO1-132[»]
4V8DX-ray3.00AO/CO1-132[»]
4V8EX-ray3.30BO/DO1-132[»]
4V8FX-ray3.30BO/CO1-132[»]
4V8GX-ray3.00AL/CL1-132[»]
4V8HX-ray3.10AL/CL1-132[»]
4V8IX-ray2.70AL/CL1-132[»]
4V8JX-ray3.90AL/CL1-132[»]
4V8NX-ray3.10AL/CL2-132[»]
4V8OX-ray3.80AL2-132[»]
4V8QX-ray3.10BL2-132[»]
4V8UX-ray3.70AL/CL1-132[»]
4V8XX-ray3.35AL/CL1-132[»]
4V90X-ray2.95AL1-132[»]
4V95X-ray3.20AL/CL1-132[»]
4V97X-ray3.52AL/CL1-132[»]
4V9AX-ray3.30AO/CO1-127[»]
4V9BX-ray3.10AO/CO1-127[»]
4V9HX-ray2.86AL2-125[»]
4V9IX-ray3.30AL/CL2-125[»]
4V9RX-ray3.00AL/CL1-132[»]
4V9SX-ray3.10AL/CL1-132[»]
4W2EX-ray2.90l1-132[»]
4W2FX-ray2.40AL/CL1-132[»]
4W2GX-ray2.55AL/CL1-132[»]
4W2HX-ray2.70AL/CL1-132[»]
4W2IX-ray2.70AL/CL1-132[»]
4WPOX-ray2.80BL/DL1-132[»]
4WQFX-ray2.80BL/DL1-132[»]
4WQUX-ray2.80BL/DL1-132[»]
4WQYX-ray2.80BL/DL1-132[»]
4WT8X-ray3.40L2-125[»]
4WUSX-ray3.40L2-125[»]
4Y4OX-ray2.301l/2l1-132[»]
4Y4PX-ray2.501l/2l1-132[»]
4YHHX-ray3.42L2-125[»]
4Z3QX-ray2.601l/2l1-132[»]
4Z3RX-ray3.101l/2l1-132[»]
4Z3SX-ray2.651l/2l1-132[»]
4Z8CX-ray2.901l/2l1-132[»]
4ZERX-ray3.101l/2l2-123[»]
ProteinModelPortaliQ5SHN3.
SMRiQ5SHN3. Positions 2-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1697.

Proteomic databases

PRIDEiQ5SHN3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71520; BAD71520; BAD71520.
GeneIDi3169892.
KEGGittj:TTHA1697.
PATRICi23958349. VBITheThe93045_1667.

Phylogenomic databases

eggNOGiCOG0048.
HOGENOMiHOG000040063.
KOiK02950.
OMAiQVTSARR.
OrthoDBiEOG61ZTNF.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1736-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHN3.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR006032. Ribosomal_S12/S23.
IPR005679. Ribosomal_S12_bac.
[Graphical view]
PANTHERiPTHR11652. PTHR11652. 1 hit.
PfamiPF00164. Ribosom_S12_S23. 1 hit.
[Graphical view]
PIRSFiPIRSF002133. Ribosomal_S12/S23. 1 hit.
PRINTSiPR01034. RIBOSOMALS12.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00981. rpsL_bact. 1 hit.
PROSITEiPS00055. RIBOSOMAL_S12. 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 2-29.
  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: METHYLTHIOLATION AT ASP-89, MASS SPECTROMETRY.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
  6. "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.
  7. "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.
  8. "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.
  9. "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 (5.00 ANGSTROMS) OF THE RIBOSOME.
  10. "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.
  11. "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.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
  13. "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.
  14. "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 nameiRS12_THET8
AccessioniPrimary (citable) accession number: Q5SHN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 105 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.