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Protein

30S ribosomal protein S12

Gene

rpsL

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 5 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 (PubMed:11014182, PubMed:11007480, PubMed:11163189, PubMed:11014183, PubMed:11511350, PubMed:11296217, PubMed:11228145, PubMed:11228145, PubMed:11283358, PubMed:11340196, PubMed:11866529). 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 (PubMed:11283358).10 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

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
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001463412 – 13230S ribosomal protein S12Add BLAST131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei893-methylthioaspartic acid2 Publications1

Post-translational modificationi

The methythiolated Asp-89 contacts a modifed residue of the 16S rRNA close to the decoding center, and might be important for decoding center assembly.1 Publication

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:11014182, PubMed:11007480, PubMed:11163189, PubMed:11014183, PubMed:11511350, PubMed:11296217, PubMed:11228145, PubMed:11228145, PubMed:11283358, PubMed:11340196, PubMed:11866529, PubMed:25775268, PubMed:26792896). Contacts proteins S8 and S17 (PubMed:11866529). Interacts with IF1 in the 30S initiation complex (PubMed:11228145).10 Publications

Protein-protein interaction databases

STRINGi300852.TTHA1697.

Structurei

Secondary structure

1132
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 9Combined sources6
Beta strandi24 – 26Combined sources3
Beta strandi28 – 35Combined sources8
Beta strandi50 – 52Combined sources3
Beta strandi54 – 57Combined sources4
Turni58 – 60Combined sources3
Beta strandi62 – 66Combined sources5
Beta strandi69 – 71Combined sources3
Beta strandi79 – 84Combined sources6
Beta strandi88 – 90Combined sources3
Beta strandi95 – 97Combined sources3
Turni101 – 104Combined sources4
Helixi114 – 117Combined sources4
Helixi123 – 125Combined sources3
Beta strandi128 – 130Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4W4GX-ray3.30QL/XL1-132[»]
4WPOX-ray2.80BL/DL1-132[»]
4WQ1X-ray3.103A/3I1-132[»]
4WQFX-ray2.80BL/DL1-132[»]
4WQRX-ray3.153A/3I1-132[»]
4WQUX-ray2.80BL/DL1-132[»]
4WQYX-ray2.80BL/DL1-132[»]
4WR6X-ray3.053A/3I1-132[»]
4WRAX-ray3.053A/3I1-132[»]
4WROX-ray3.053I1-132[»]
4WSDX-ray2.953A/3I1-132[»]
4WSMX-ray3.303A/3I1-132[»]
4WT1X-ray3.053A/3I1-132[»]
4WT8X-ray3.40AL/BL2-125[»]
4WU1X-ray3.203A/3I1-132[»]
4WZDX-ray3.103A/3I1-132[»]
4WZOX-ray3.303A/3I1-132[»]
4X62X-ray3.45L2-126[»]
4X64X-ray3.35L2-126[»]
4X65X-ray3.35L2-126[»]
4X66X-ray3.45L2-126[»]
4Y4OX-ray2.301l/2l1-132[»]
4Y4PX-ray2.501l/2l1-132[»]
4YHHX-ray3.42L2-125[»]
4YPBX-ray3.40QL/XL1-132[»]
4YY3X-ray3.60L1-132[»]
4YZVX-ray3.10QL/XL1-132[»]
4Z3SX-ray2.651l/2l1-132[»]
4Z8CX-ray2.901l/2l1-132[»]
4ZERX-ray3.101l/2l2-123[»]
4ZSNX-ray3.60QL/XL1-132[»]
5A9Zelectron microscopy4.70BP2-125[»]
5AA0electron microscopy5.00BP2-125[»]
5BR8X-ray3.40L2-132[»]
5CZPX-ray3.30QL/XL1-132[»]
5D8BX-ray3.63IC/MA1-132[»]
5DFEX-ray3.10QL/XL1-132[»]
5DOXX-ray3.101l/2l1-132[»]
5DOYX-ray2.601l/2l1-132[»]
5E7KX-ray3.203A/3I1-132[»]
5E81X-ray2.953A/3I1-132[»]
5EL4X-ray3.153A/3I1-132[»]
5EL5X-ray3.153A/3I1-132[»]
5EL6X-ray3.103A/3I1-132[»]
5EL7X-ray3.153A/3I1-132[»]
5F8KX-ray2.801l/2l2-123[»]
5FDUX-ray2.901l/2l2-123[»]
5FDVX-ray2.801l/2l2-123[»]
5HAUX-ray3.001l/2l1-132[»]
5HCPX-ray2.891l/2l1-132[»]
5HCQX-ray2.801l/2l1-132[»]
5HCRX-ray2.801l/2l1-132[»]
5HD1X-ray2.701l/2l1-132[»]
5IB7X-ray2.993A/3I1-132[»]
5IB8X-ray3.133A/3I1-132[»]
5IBBX-ray2.963A/3I1-132[»]
5IMQelectron microscopy3.80P1-132[»]
5IMRelectron microscopy-P1-132[»]
5IWAX-ray3.50L2-125[»]
5J30X-ray3.20QL/XL1-132[»]
5J3CX-ray3.04QL/XL1-132[»]
5J4BX-ray2.601l/2l1-132[»]
5J4CX-ray2.801l/2l1-132[»]
5J8BX-ray2.60l1-132[»]
5LMNelectron microscopy3.55L1-132[»]
5LMOelectron microscopy4.30L1-132[»]
5LMPelectron microscopy5.35L1-132[»]
5LMQelectron microscopy4.20L1-132[»]
5LMRelectron microscopy4.45L1-132[»]
5LMSelectron microscopy5.10L1-132[»]
5LMTelectron microscopy4.15L1-132[»]
5LMUelectron microscopy4.00L1-132[»]
5LMVelectron microscopy4.90L1-132[»]
ProteinModelPortaliQ5SHN3.
SMRiQ5SHN3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHN3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S12P family.Curated

Phylogenomic databases

eggNOGiENOG4108UKE. Bacteria.
COG0048. LUCA.
HOGENOMiHOG000040063.
KOiK02950.
OMAiRIVRGRY.

Family and domain databases

CDDicd03368. Ribosomal_S12. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B. 1 hit.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA36418 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.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
PDB 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[»]
4W4GX-ray3.30QL/XL1-132[»]
4WPOX-ray2.80BL/DL1-132[»]
4WQ1X-ray3.103A/3I1-132[»]
4WQFX-ray2.80BL/DL1-132[»]
4WQRX-ray3.153A/3I1-132[»]
4WQUX-ray2.80BL/DL1-132[»]
4WQYX-ray2.80BL/DL1-132[»]
4WR6X-ray3.053A/3I1-132[»]
4WRAX-ray3.053A/3I1-132[»]
4WROX-ray3.053I1-132[»]
4WSDX-ray2.953A/3I1-132[»]
4WSMX-ray3.303A/3I1-132[»]
4WT1X-ray3.053A/3I1-132[»]
4WT8X-ray3.40AL/BL2-125[»]
4WU1X-ray3.203A/3I1-132[»]
4WZDX-ray3.103A/3I1-132[»]
4WZOX-ray3.303A/3I1-132[»]
4X62X-ray3.45L2-126[»]
4X64X-ray3.35L2-126[»]
4X65X-ray3.35L2-126[»]
4X66X-ray3.45L2-126[»]
4Y4OX-ray2.301l/2l1-132[»]
4Y4PX-ray2.501l/2l1-132[»]
4YHHX-ray3.42L2-125[»]
4YPBX-ray3.40QL/XL1-132[»]
4YY3X-ray3.60L1-132[»]
4YZVX-ray3.10QL/XL1-132[»]
4Z3SX-ray2.651l/2l1-132[»]
4Z8CX-ray2.901l/2l1-132[»]
4ZERX-ray3.101l/2l2-123[»]
4ZSNX-ray3.60QL/XL1-132[»]
5A9Zelectron microscopy4.70BP2-125[»]
5AA0electron microscopy5.00BP2-125[»]
5BR8X-ray3.40L2-132[»]
5CZPX-ray3.30QL/XL1-132[»]
5D8BX-ray3.63IC/MA1-132[»]
5DFEX-ray3.10QL/XL1-132[»]
5DOXX-ray3.101l/2l1-132[»]
5DOYX-ray2.601l/2l1-132[»]
5E7KX-ray3.203A/3I1-132[»]
5E81X-ray2.953A/3I1-132[»]
5EL4X-ray3.153A/3I1-132[»]
5EL5X-ray3.153A/3I1-132[»]
5EL6X-ray3.103A/3I1-132[»]
5EL7X-ray3.153A/3I1-132[»]
5F8KX-ray2.801l/2l2-123[»]
5FDUX-ray2.901l/2l2-123[»]
5FDVX-ray2.801l/2l2-123[»]
5HAUX-ray3.001l/2l1-132[»]
5HCPX-ray2.891l/2l1-132[»]
5HCQX-ray2.801l/2l1-132[»]
5HCRX-ray2.801l/2l1-132[»]
5HD1X-ray2.701l/2l1-132[»]
5IB7X-ray2.993A/3I1-132[»]
5IB8X-ray3.133A/3I1-132[»]
5IBBX-ray2.963A/3I1-132[»]
5IMQelectron microscopy3.80P1-132[»]
5IMRelectron microscopy-P1-132[»]
5IWAX-ray3.50L2-125[»]
5J30X-ray3.20QL/XL1-132[»]
5J3CX-ray3.04QL/XL1-132[»]
5J4BX-ray2.601l/2l1-132[»]
5J4CX-ray2.801l/2l1-132[»]
5J8BX-ray2.60l1-132[»]
5LMNelectron microscopy3.55L1-132[»]
5LMOelectron microscopy4.30L1-132[»]
5LMPelectron microscopy5.35L1-132[»]
5LMQelectron microscopy4.20L1-132[»]
5LMRelectron microscopy4.45L1-132[»]
5LMSelectron microscopy5.10L1-132[»]
5LMTelectron microscopy4.15L1-132[»]
5LMUelectron microscopy4.00L1-132[»]
5LMVelectron microscopy4.90L1-132[»]
ProteinModelPortaliQ5SHN3.
SMRiQ5SHN3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4108UKE. Bacteria.
COG0048. LUCA.
HOGENOMiHOG000040063.
KOiK02950.
OMAiRIVRGRY.

Miscellaneous databases

EvolutionaryTraceiQ5SHN3.

Family and domain databases

CDDicd03368. Ribosomal_S12. 1 hit.
HAMAPiMF_00403_B. Ribosomal_S12_B. 1 hit.
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...

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: November 30, 2016
This is version 118 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

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 one 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.