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Protein

30S ribosomal protein S5

Gene

rpsE

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 S12 plays an important role in translational accuracy.By similarity
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Binds mRNA in the 70S ribosome, positioning it for translation.

GO - Molecular functioni

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

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1714-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S5
Gene namesi
Name:rpsE
Ordered Locus Names:TTHA1675
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: 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 – 16216130S ribosomal protein S5PRO_0000131621Add
BLAST

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S4 and S8.

Protein-protein interaction databases

STRINGi300852.TTHA1675.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1913Combined sources
Beta strandi21 – 3515Combined sources
Beta strandi37 – 393Combined sources
Beta strandi41 – 5010Combined sources
Helixi51 – 6313Combined sources
Beta strandi65 – 673Combined sources
Beta strandi72 – 754Combined sources
Beta strandi80 – 845Combined sources
Beta strandi87 – 937Combined sources
Turni96 – 983Combined sources
Beta strandi100 – 1023Combined sources
Helixi104 – 11310Combined sources
Beta strandi117 – 1248Combined sources
Helixi128 – 13912Combined sources
Helixi145 – 1517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00E1-162[»]
1FKAX-ray3.30E1-162[»]
1HNWX-ray3.40E1-162[»]
1HNXX-ray3.40E1-162[»]
1HNZX-ray3.30E1-162[»]
1HR0X-ray3.20E1-162[»]
1I94X-ray3.20E2-162[»]
1I95X-ray4.50E2-162[»]
1I96X-ray4.20E2-162[»]
1I97X-ray4.50E2-162[»]
1IBKX-ray3.31E1-162[»]
1IBLX-ray3.11E1-162[»]
1IBMX-ray3.31E1-162[»]
1J5EX-ray3.05E2-162[»]
1JGOX-ray5.60H1-162[»]
1JGPX-ray7.00H1-162[»]
1JGQX-ray5.00H1-162[»]
1L1Umodel-E5-154[»]
1ML5electron microscopy14.00H1-162[»]
1N32X-ray3.00E2-162[»]
1N33X-ray3.35E2-162[»]
1N34X-ray3.80E2-162[»]
1N36X-ray3.65E2-162[»]
1QD7X-ray5.50D22-130[»]
1VVJX-ray3.44QE/XE1-162[»]
1VY4X-ray2.60AE/CE1-162[»]
1VY5X-ray2.55AE/CE1-162[»]
1VY6X-ray2.90AE/CE1-162[»]
1VY7X-ray2.80AE/CE1-162[»]
1XMOX-ray3.25E1-162[»]
1XMQX-ray3.00E1-162[»]
1XNQX-ray3.05E1-162[»]
1XNRX-ray3.10E1-162[»]
2E5LX-ray3.30E2-162[»]
2F4VX-ray3.80E1-162[»]
2HHHX-ray3.35E1-162[»]
2UU9X-ray3.10E2-162[»]
2UUAX-ray2.90E2-162[»]
2UUBX-ray2.80E2-162[»]
2UUCX-ray3.10E2-162[»]
2UXBX-ray3.10E2-162[»]
2UXCX-ray2.90E2-162[»]
2UXDX-ray3.20E2-162[»]
2VQEX-ray2.50E1-162[»]
2VQFX-ray2.90E1-162[»]
2ZM6X-ray3.30E2-162[»]
3OTOX-ray3.69E1-162[»]
3T1HX-ray3.11E1-162[»]
3T1YX-ray2.80E1-162[»]
4AQYX-ray3.50E2-162[»]
4B3MX-ray2.90E2-162[»]
4B3RX-ray3.00E2-162[»]
4B3SX-ray3.15E2-162[»]
4B3TX-ray3.00E2-162[»]
4DR1X-ray3.60E1-162[»]
4DR2X-ray3.25E1-162[»]
4DR3X-ray3.35E1-162[»]
4DR4X-ray3.97E1-162[»]
4DR5X-ray3.45E1-162[»]
4DR6X-ray3.30E1-162[»]
4DR7X-ray3.75E1-162[»]
4DUYX-ray3.39E1-162[»]
4DUZX-ray3.65E1-162[»]
4DV0X-ray3.85E1-162[»]
4DV1X-ray3.85E1-162[»]
4DV2X-ray3.65E1-162[»]
4DV3X-ray3.55E1-162[»]
4DV4X-ray3.65E1-162[»]
4DV5X-ray3.68E1-162[»]
4DV6X-ray3.30E1-162[»]
4DV7X-ray3.29E1-162[»]
4GKJX-ray3.30E5-154[»]
4GKKX-ray3.20E5-154[»]
4JI0X-ray3.49E1-162[»]
4JI1X-ray3.14E1-162[»]
4JI2X-ray3.64E1-162[»]
4JI3X-ray3.35E1-162[»]
4JI4X-ray3.69E1-162[»]
4JI5X-ray3.85E1-162[»]
4JI6X-ray3.55E1-162[»]
4JI7X-ray3.50E1-162[»]
4JI8X-ray3.74E1-162[»]
4JV5X-ray3.16E5-154[»]
4JYAX-ray3.10E5-154[»]
4K0KX-ray3.40E5-155[»]
4KHPX-ray3.10E5-154[»]
4L47X-ray3.22QE/XE1-162[»]
4L71X-ray3.90QE/XE1-162[»]
4LELX-ray3.90QE/XE1-162[»]
4LF4X-ray3.34E1-162[»]
4LF5X-ray3.75E1-162[»]
4LF6X-ray3.31E1-162[»]
4LF7X-ray3.15E1-162[»]
4LF8X-ray3.15E1-162[»]
4LF9X-ray3.28E1-162[»]
4LFAX-ray3.65E1-162[»]
4LFBX-ray3.01E1-162[»]
4LFCX-ray3.60E1-162[»]
4LFZX-ray3.92QE/XE1-162[»]
4LNTX-ray2.94QE/XE1-162[»]
4LSKX-ray3.48QE/XE1-162[»]
4LT8X-ray3.14QE/XE1-162[»]
4NXMX-ray3.65E1-162[»]
4NXNX-ray3.54E1-162[»]
4OX9X-ray3.80E2-162[»]
4P6FX-ray3.60QE/XE1-162[»]
4P70X-ray3.68QE/XE1-162[»]
4V42X-ray5.50AH1-162[»]
4V49X-ray8.70E5-154[»]
4V4AX-ray9.50E5-154[»]
4V4GX-ray11.50E5-154[»]
4V4IX-ray3.71f-[»]
4V4PX-ray5.50BH1-162[»]
4V4RX-ray5.90E1-162[»]
4V4SX-ray6.76E1-162[»]
4V4TX-ray6.46E1-162[»]
4V4XX-ray5.00AH1-162[»]
4V4YX-ray5.50H1-162[»]
4V4ZX-ray4.51H1-162[»]
4V51X-ray2.80AE/CE2-162[»]
4V5AX-ray3.50AE/CE2-162[»]
4V5CX-ray3.30AE/CE1-162[»]
4V5DX-ray3.50AE/CE1-162[»]
4V5EX-ray3.45AE/CE1-162[»]
4V5FX-ray3.60AE/CE1-162[»]
4V5GX-ray3.60AE/CE1-162[»]
4V5JX-ray3.10AE/CE1-162[»]
4V5KX-ray3.20AE/CE1-162[»]
4V5LX-ray3.10E1-162[»]
4V5Melectron microscopy7.80AE1-162[»]
4V5Nelectron microscopy7.60AE1-162[»]
4V5PX-ray3.10AE/CE1-162[»]
4V5QX-ray3.10AE/CE1-162[»]
4V5RX-ray3.10AE/CE1-162[»]
4V5SX-ray3.10AE/CE1-162[»]
4V68electron microscopy6.40AE5-155[»]
4V6AX-ray3.10AE/CE1-162[»]
4V6FX-ray3.10BH/CH1-162[»]
4V6GX-ray3.50AH/CH1-162[»]
4V7JX-ray3.30Ae/Be1-162[»]
4V7KX-ray3.60Ae/Be1-162[»]
4V7LX-ray3.00AE/CE1-162[»]
4V7MX-ray3.45AE/CE1-162[»]
4V7WX-ray3.00AE/CE1-162[»]
4V7XX-ray3.00AE/CE1-160[»]
4V7YX-ray3.00AE/CE1-162[»]
4V7ZX-ray3.10AE/CE1-162[»]
4V87X-ray3.10BH/CH1-162[»]
4V8AX-ray3.20CE/DE1-162[»]
4V8BX-ray3.00AH/CH1-162[»]
4V8CX-ray3.30CH/DH1-162[»]
4V8DX-ray3.00AH/CH1-162[»]
4V8EX-ray3.30BH/DH1-162[»]
4V8FX-ray3.30BH/CH1-162[»]
4V8GX-ray3.00AE/CE1-162[»]
4V8HX-ray3.10AE/CE1-162[»]
4V8IX-ray2.70AE/CE1-162[»]
4V8JX-ray3.90AE/CE1-162[»]
4V8NX-ray3.10AE/CE1-162[»]
4V8OX-ray3.80AE1-162[»]
4V8QX-ray3.10BE1-162[»]
4V8UX-ray3.70AE/CE1-162[»]
4V8XX-ray3.35AE/CE1-162[»]
4V90X-ray2.95AE1-162[»]
4V95X-ray3.20AE/CE1-162[»]
4V97X-ray3.52AE/CE1-162[»]
4V9AX-ray3.30AH/CH1-162[»]
4V9BX-ray3.10AH/CH1-162[»]
4V9HX-ray2.86AE5-154[»]
4V9IX-ray3.30AE/CE5-154[»]
4V9RX-ray3.00AE/CE1-162[»]
4V9SX-ray3.10AE/CE1-162[»]
4W2EX-ray2.90e1-162[»]
4W2FX-ray2.40AE/CE1-162[»]
4W2GX-ray2.55AE/CE1-162[»]
4W2HX-ray2.70AE/CE1-162[»]
4W2IX-ray2.70AE/CE1-162[»]
ProteinModelPortaliQ5SHQ5.
SMRiQ5SHQ5. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHQ5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 6964S5 DRBMAdd
BLAST

Domaini

The N-terminal domain interacts with the head of the 30S subunit; the C-terminal domain interacts with the body and contacts protein S4. The interaction surface between S4 and S5 is involved in control of translational fidelity.

Sequence similaritiesi

Belongs to the ribosomal protein S5P family.Curated
Contains 1 S5 DRBM domain.Curated

Phylogenomic databases

eggNOGiCOG0098.
HOGENOMiHOG000072595.
KOiK02988.
OMAiVKGTIPH.
OrthoDBiEOG6FJNM5.
PhylomeDBiQ5SHQ5.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
HAMAPiMF_01307_B. Ribosomal_S5_B.
InterProiIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005712. Ribosomal_S5_bac-type.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01021. rpsE_bact. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5SHQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPETDFEEKM ILIRRTARMQ AGGRRFRFGA LVVVGDRQGR VGLGFGKAPE
60 70 80 90 100
VPLAVQKAGY YARRNMVEVP LQNGTIPHEI EVEFGASKIV LKPAAPGTGV
110 120 130 140 150
IAGAVPRAIL ELAGVTDILT KELGSRNPIN IAYATMEALR QLRTKADVER
160
LRKGEAHAQA QG
Length:162
Mass (Da):17,557
Last modified:January 22, 2007 - v3
Checksum:iBE3367CB619E68D2
GO

Mass spectrometryi

Molecular mass is 17428 Da from positions 2 - 162. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71498.1.
RefSeqiYP_144941.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71498; BAD71498; BAD71498.
GeneIDi3169827.
KEGGittj:TTHA1675.
PATRICi23958305. VBITheThe93045_1645.

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: BAD71498.1.
RefSeqiYP_144941.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00E1-162[»]
1FKAX-ray3.30E1-162[»]
1HNWX-ray3.40E1-162[»]
1HNXX-ray3.40E1-162[»]
1HNZX-ray3.30E1-162[»]
1HR0X-ray3.20E1-162[»]
1I94X-ray3.20E2-162[»]
1I95X-ray4.50E2-162[»]
1I96X-ray4.20E2-162[»]
1I97X-ray4.50E2-162[»]
1IBKX-ray3.31E1-162[»]
1IBLX-ray3.11E1-162[»]
1IBMX-ray3.31E1-162[»]
1J5EX-ray3.05E2-162[»]
1JGOX-ray5.60H1-162[»]
1JGPX-ray7.00H1-162[»]
1JGQX-ray5.00H1-162[»]
1L1Umodel-E5-154[»]
1ML5electron microscopy14.00H1-162[»]
1N32X-ray3.00E2-162[»]
1N33X-ray3.35E2-162[»]
1N34X-ray3.80E2-162[»]
1N36X-ray3.65E2-162[»]
1QD7X-ray5.50D22-130[»]
1VVJX-ray3.44QE/XE1-162[»]
1VY4X-ray2.60AE/CE1-162[»]
1VY5X-ray2.55AE/CE1-162[»]
1VY6X-ray2.90AE/CE1-162[»]
1VY7X-ray2.80AE/CE1-162[»]
1XMOX-ray3.25E1-162[»]
1XMQX-ray3.00E1-162[»]
1XNQX-ray3.05E1-162[»]
1XNRX-ray3.10E1-162[»]
2E5LX-ray3.30E2-162[»]
2F4VX-ray3.80E1-162[»]
2HHHX-ray3.35E1-162[»]
2UU9X-ray3.10E2-162[»]
2UUAX-ray2.90E2-162[»]
2UUBX-ray2.80E2-162[»]
2UUCX-ray3.10E2-162[»]
2UXBX-ray3.10E2-162[»]
2UXCX-ray2.90E2-162[»]
2UXDX-ray3.20E2-162[»]
2VQEX-ray2.50E1-162[»]
2VQFX-ray2.90E1-162[»]
2ZM6X-ray3.30E2-162[»]
3OTOX-ray3.69E1-162[»]
3T1HX-ray3.11E1-162[»]
3T1YX-ray2.80E1-162[»]
4AQYX-ray3.50E2-162[»]
4B3MX-ray2.90E2-162[»]
4B3RX-ray3.00E2-162[»]
4B3SX-ray3.15E2-162[»]
4B3TX-ray3.00E2-162[»]
4DR1X-ray3.60E1-162[»]
4DR2X-ray3.25E1-162[»]
4DR3X-ray3.35E1-162[»]
4DR4X-ray3.97E1-162[»]
4DR5X-ray3.45E1-162[»]
4DR6X-ray3.30E1-162[»]
4DR7X-ray3.75E1-162[»]
4DUYX-ray3.39E1-162[»]
4DUZX-ray3.65E1-162[»]
4DV0X-ray3.85E1-162[»]
4DV1X-ray3.85E1-162[»]
4DV2X-ray3.65E1-162[»]
4DV3X-ray3.55E1-162[»]
4DV4X-ray3.65E1-162[»]
4DV5X-ray3.68E1-162[»]
4DV6X-ray3.30E1-162[»]
4DV7X-ray3.29E1-162[»]
4GKJX-ray3.30E5-154[»]
4GKKX-ray3.20E5-154[»]
4JI0X-ray3.49E1-162[»]
4JI1X-ray3.14E1-162[»]
4JI2X-ray3.64E1-162[»]
4JI3X-ray3.35E1-162[»]
4JI4X-ray3.69E1-162[»]
4JI5X-ray3.85E1-162[»]
4JI6X-ray3.55E1-162[»]
4JI7X-ray3.50E1-162[»]
4JI8X-ray3.74E1-162[»]
4JV5X-ray3.16E5-154[»]
4JYAX-ray3.10E5-154[»]
4K0KX-ray3.40E5-155[»]
4KHPX-ray3.10E5-154[»]
4L47X-ray3.22QE/XE1-162[»]
4L71X-ray3.90QE/XE1-162[»]
4LELX-ray3.90QE/XE1-162[»]
4LF4X-ray3.34E1-162[»]
4LF5X-ray3.75E1-162[»]
4LF6X-ray3.31E1-162[»]
4LF7X-ray3.15E1-162[»]
4LF8X-ray3.15E1-162[»]
4LF9X-ray3.28E1-162[»]
4LFAX-ray3.65E1-162[»]
4LFBX-ray3.01E1-162[»]
4LFCX-ray3.60E1-162[»]
4LFZX-ray3.92QE/XE1-162[»]
4LNTX-ray2.94QE/XE1-162[»]
4LSKX-ray3.48QE/XE1-162[»]
4LT8X-ray3.14QE/XE1-162[»]
4NXMX-ray3.65E1-162[»]
4NXNX-ray3.54E1-162[»]
4OX9X-ray3.80E2-162[»]
4P6FX-ray3.60QE/XE1-162[»]
4P70X-ray3.68QE/XE1-162[»]
4V42X-ray5.50AH1-162[»]
4V49X-ray8.70E5-154[»]
4V4AX-ray9.50E5-154[»]
4V4GX-ray11.50E5-154[»]
4V4IX-ray3.71f-[»]
4V4PX-ray5.50BH1-162[»]
4V4RX-ray5.90E1-162[»]
4V4SX-ray6.76E1-162[»]
4V4TX-ray6.46E1-162[»]
4V4XX-ray5.00AH1-162[»]
4V4YX-ray5.50H1-162[»]
4V4ZX-ray4.51H1-162[»]
4V51X-ray2.80AE/CE2-162[»]
4V5AX-ray3.50AE/CE2-162[»]
4V5CX-ray3.30AE/CE1-162[»]
4V5DX-ray3.50AE/CE1-162[»]
4V5EX-ray3.45AE/CE1-162[»]
4V5FX-ray3.60AE/CE1-162[»]
4V5GX-ray3.60AE/CE1-162[»]
4V5JX-ray3.10AE/CE1-162[»]
4V5KX-ray3.20AE/CE1-162[»]
4V5LX-ray3.10E1-162[»]
4V5Melectron microscopy7.80AE1-162[»]
4V5Nelectron microscopy7.60AE1-162[»]
4V5PX-ray3.10AE/CE1-162[»]
4V5QX-ray3.10AE/CE1-162[»]
4V5RX-ray3.10AE/CE1-162[»]
4V5SX-ray3.10AE/CE1-162[»]
4V68electron microscopy6.40AE5-155[»]
4V6AX-ray3.10AE/CE1-162[»]
4V6FX-ray3.10BH/CH1-162[»]
4V6GX-ray3.50AH/CH1-162[»]
4V7JX-ray3.30Ae/Be1-162[»]
4V7KX-ray3.60Ae/Be1-162[»]
4V7LX-ray3.00AE/CE1-162[»]
4V7MX-ray3.45AE/CE1-162[»]
4V7WX-ray3.00AE/CE1-162[»]
4V7XX-ray3.00AE/CE1-160[»]
4V7YX-ray3.00AE/CE1-162[»]
4V7ZX-ray3.10AE/CE1-162[»]
4V87X-ray3.10BH/CH1-162[»]
4V8AX-ray3.20CE/DE1-162[»]
4V8BX-ray3.00AH/CH1-162[»]
4V8CX-ray3.30CH/DH1-162[»]
4V8DX-ray3.00AH/CH1-162[»]
4V8EX-ray3.30BH/DH1-162[»]
4V8FX-ray3.30BH/CH1-162[»]
4V8GX-ray3.00AE/CE1-162[»]
4V8HX-ray3.10AE/CE1-162[»]
4V8IX-ray2.70AE/CE1-162[»]
4V8JX-ray3.90AE/CE1-162[»]
4V8NX-ray3.10AE/CE1-162[»]
4V8OX-ray3.80AE1-162[»]
4V8QX-ray3.10BE1-162[»]
4V8UX-ray3.70AE/CE1-162[»]
4V8XX-ray3.35AE/CE1-162[»]
4V90X-ray2.95AE1-162[»]
4V95X-ray3.20AE/CE1-162[»]
4V97X-ray3.52AE/CE1-162[»]
4V9AX-ray3.30AH/CH1-162[»]
4V9BX-ray3.10AH/CH1-162[»]
4V9HX-ray2.86AE5-154[»]
4V9IX-ray3.30AE/CE5-154[»]
4V9RX-ray3.00AE/CE1-162[»]
4V9SX-ray3.10AE/CE1-162[»]
4W2EX-ray2.90e1-162[»]
4W2FX-ray2.40AE/CE1-162[»]
4W2GX-ray2.55AE/CE1-162[»]
4W2HX-ray2.70AE/CE1-162[»]
4W2IX-ray2.70AE/CE1-162[»]
ProteinModelPortaliQ5SHQ5.
SMRiQ5SHQ5. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71498; BAD71498; BAD71498.
GeneIDi3169827.
KEGGittj:TTHA1675.
PATRICi23958305. VBITheThe93045_1645.

Phylogenomic databases

eggNOGiCOG0098.
HOGENOMiHOG000072595.
KOiK02988.
OMAiVKGTIPH.
OrthoDBiEOG6FJNM5.
PhylomeDBiQ5SHQ5.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1714-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHQ5.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
HAMAPiMF_01307_B. Ribosomal_S5_B.
InterProiIPR014720. dsRNA-bd_dom.
IPR000851. Ribosomal_S5.
IPR005712. Ribosomal_S5_bac-type.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01021. rpsE_bact. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 (OCT-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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-44.
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  4. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE 30S SUBUNIT.
  5. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.5 ANGSTROMS).
  6. Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
  7. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
  8. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 30S SUBUNIT.
  9. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 30S SUBUNIT.
  10. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
  11. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
  12. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF THE 30S SUBUNIT.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
  14. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF THE 30S SUBUNIT.
  15. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.

Entry informationi

Entry nameiRS5_THET8
AccessioniPrimary (citable) accession number: Q5SHQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2005
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Is positioned such that it could physically interact with spectinomycin.

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.