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Protein

30S ribosomal protein S18

Gene

rpsR

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

Located on the back of the platform of the 30S subunit where it stabilizes the close packing of several RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome, where it probably interacts with the Shine-Dalgarno helix.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-252-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S18
Gene namesi
Name:rpsR
Ordered Locus Names:TTHA0243
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 – 888730S ribosomal protein S18PRO_0000111250Add
BLAST

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Forms a tight heterodimer with protein S6, also interacts with protein S11. Binds to the C-terminus of IF3 and to the central section of Era.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0243.

Structurei

Secondary structure

1
88
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni22 – 243Combined sources
Beta strandi28 – 303Combined sources
Helixi37 – 426Combined sources
Beta strandi46 – 483Combined sources
Helixi53 – 564Combined sources
Beta strandi59 – 613Combined sources
Helixi62 – 7615Combined sources
Beta strandi77 – 793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00R1-88[»]
1FKAX-ray3.30R1-88[»]
1G1XX-ray2.60C/H1-88[»]
1HNWX-ray3.40R1-88[»]
1HNXX-ray3.40R1-88[»]
1HNZX-ray3.30R1-88[»]
1HR0X-ray3.20R1-88[»]
1I94X-ray3.20R2-88[»]
1I95X-ray4.50R2-88[»]
1I96X-ray4.20R2-88[»]
1I97X-ray4.50R2-88[»]
1IBKX-ray3.31R1-88[»]
1IBLX-ray3.11R1-88[»]
1IBMX-ray3.31R1-88[»]
1J5EX-ray3.05R1-88[»]
1JGOX-ray5.60U1-88[»]
1JGPX-ray7.00U1-88[»]
1JGQX-ray5.00U1-88[»]
1L1Umodel-R16-88[»]
1ML5electron microscopy14.00U1-88[»]
1N32X-ray3.00R1-88[»]
1N33X-ray3.35R1-88[»]
1N34X-ray3.80R1-88[»]
1N36X-ray3.65R1-88[»]
1VVJX-ray3.44QR/XR1-88[»]
1VY4X-ray2.60AR/CR1-88[»]
1VY5X-ray2.55AR/CR1-88[»]
1VY6X-ray2.90AR/CR1-88[»]
1VY7X-ray2.80AR/CR1-88[»]
1X18electron microscopy13.50H16-88[»]
1XMOX-ray3.25R1-88[»]
1XMQX-ray3.00R1-88[»]
1XNQX-ray3.05R1-88[»]
1XNRX-ray3.10R1-88[»]
2E5LX-ray3.30R2-88[»]
2F4VX-ray3.80R1-88[»]
2HHHX-ray3.35R1-88[»]
2UU9X-ray3.10R2-88[»]
2UUAX-ray2.90R2-88[»]
2UUBX-ray2.80R2-88[»]
2UUCX-ray3.10R2-88[»]
2UXBX-ray3.10R2-88[»]
2UXCX-ray2.90R2-88[»]
2UXDX-ray3.20R2-88[»]
2ZM6X-ray3.30R2-88[»]
3OTOX-ray3.69R1-88[»]
3T1HX-ray3.11R1-88[»]
3T1YX-ray2.80R1-88[»]
4AQYX-ray3.50R1-88[»]
4B3MX-ray2.90R1-88[»]
4B3RX-ray3.00R1-88[»]
4B3SX-ray3.15R1-88[»]
4B3TX-ray3.00R1-88[»]
4DR1X-ray3.60R1-88[»]
4DR2X-ray3.25R1-88[»]
4DR3X-ray3.35R1-88[»]
4DR4X-ray3.97R1-88[»]
4DR5X-ray3.45R1-88[»]
4DR6X-ray3.30R1-88[»]
4DR7X-ray3.75R1-88[»]
4DUYX-ray3.39R1-88[»]
4DUZX-ray3.65R1-88[»]
4DV0X-ray3.85R1-88[»]
4DV1X-ray3.85R1-88[»]
4DV2X-ray3.65R1-88[»]
4DV3X-ray3.55R1-88[»]
4DV4X-ray3.65R1-88[»]
4DV5X-ray3.68R1-88[»]
4DV6X-ray3.30R1-88[»]
4DV7X-ray3.29R1-88[»]
4GKJX-ray3.30R16-88[»]
4GKKX-ray3.20R16-88[»]
4JI0X-ray3.49R1-88[»]
4JI1X-ray3.14R1-88[»]
4JI2X-ray3.64R1-88[»]
4JI3X-ray3.35R1-88[»]
4JI4X-ray3.69R1-88[»]
4JI5X-ray3.85R1-88[»]
4JI6X-ray3.55R1-88[»]
4JI7X-ray3.50R1-88[»]
4JI8X-ray3.74R1-88[»]
4JV5X-ray3.16R19-88[»]
4JYAX-ray3.10R19-88[»]
4K0KX-ray3.40R19-88[»]
4KHPX-ray3.10R19-88[»]
4L47X-ray3.22QR/XR1-88[»]
4L71X-ray3.90QR/XR1-88[»]
4LELX-ray3.90QR/XR1-88[»]
4LF4X-ray3.34R1-88[»]
4LF5X-ray3.75R1-88[»]
4LF6X-ray3.31R1-88[»]
4LF7X-ray3.15R1-88[»]
4LF8X-ray3.15R1-88[»]
4LF9X-ray3.28R1-88[»]
4LFAX-ray3.65R1-88[»]
4LFBX-ray3.01R1-88[»]
4LFCX-ray3.60R1-88[»]
4LFZX-ray3.92QR/XR1-88[»]
4LNTX-ray2.94QR/XR1-88[»]
4LSKX-ray3.48QR/XR1-88[»]
4LT8X-ray3.14QR/XR1-88[»]
4NXMX-ray3.65R1-88[»]
4NXNX-ray3.54R1-88[»]
4OX9X-ray3.80R1-88[»]
4P6FX-ray3.60QR/XR1-88[»]
4P70X-ray3.68QR/XR1-88[»]
4TUAX-ray3.60QR/XR1-88[»]
4TUBX-ray3.60QR/XR1-88[»]
4TUCX-ray3.60QR/XR1-88[»]
4TUDX-ray3.60QR/XR1-88[»]
4TUEX-ray3.50QR/XR1-88[»]
4V42X-ray5.50U1-88[»]
4V49X-ray8.70R16-88[»]
4V4AX-ray9.50R16-88[»]
4V4GX-ray11.50R16-88[»]
4V4IX-ray3.71s1-88[»]
4V4PX-ray5.50BU1-88[»]
4V4RX-ray5.90AR1-88[»]
4V4SX-ray6.76AR1-88[»]
4V4TX-ray6.46AR1-88[»]
4V4XX-ray5.00AU1-88[»]
4V4YX-ray5.50AU1-88[»]
4V4ZX-ray4.51AU1-88[»]
4V51X-ray2.80AR/CR2-88[»]
4V5AX-ray3.50AR/CR2-88[»]
4V5CX-ray3.30AR/CR1-88[»]
4V5DX-ray3.50AR/CR1-88[»]
4V5EX-ray3.45AR/CR1-88[»]
4V5FX-ray3.60AR/CR1-88[»]
4V5GX-ray3.60AR/CR1-88[»]
4V5JX-ray3.10AR/CR1-88[»]
4V5KX-ray3.20AR/CR1-88[»]
4V5LX-ray3.10R1-88[»]
4V5Melectron microscopy7.80AR1-88[»]
4V5Nelectron microscopy7.60AR1-88[»]
4V5PX-ray3.10AR/CR1-88[»]
4V5QX-ray3.10AR/CR1-88[»]
4V5RX-ray3.10AR/CR1-88[»]
4V5SX-ray3.10AR/CR1-88[»]
4V68electron microscopy6.40AR19-88[»]
4V6AX-ray3.10AR/CR1-88[»]
4V6FX-ray3.10BU/CU1-88[»]
4V6GX-ray3.50AU/CU1-88[»]
4V7JX-ray3.30Ar/Br1-88[»]
4V7KX-ray3.60Ar/Br1-88[»]
4V7LX-ray3.00AR/CR1-88[»]
4V7MX-ray3.45AR/CR1-88[»]
4V7WX-ray3.00AR/CR1-88[»]
4V7XX-ray3.00AR/CR1-88[»]
4V7YX-ray3.00AR/CR1-88[»]
4V7ZX-ray3.10AR/CR1-88[»]
4V87X-ray3.10BU/CU1-88[»]
4V8AX-ray3.20CR/DR1-88[»]
4V8BX-ray3.00AU/CU1-88[»]
4V8CX-ray3.30CU/DU1-88[»]
4V8DX-ray3.00AU/CU1-88[»]
4V8EX-ray3.30BU/DU1-88[»]
4V8FX-ray3.30BU/CU1-88[»]
4V8GX-ray3.00AR/CR1-88[»]
4V8HX-ray3.10AR/CR1-88[»]
4V8IX-ray2.70AR/CR1-88[»]
4V8JX-ray3.90AR/CR1-88[»]
4V8NX-ray3.10AR/CR1-88[»]
4V8OX-ray3.80AR1-88[»]
4V8QX-ray3.10BR1-88[»]
4V8UX-ray3.70AR/CR1-88[»]
4V8XX-ray3.35AR/CR1-88[»]
4V90X-ray2.95AR1-88[»]
4V95X-ray3.20AR/CR1-88[»]
4V97X-ray3.52AR/CR1-88[»]
4V9AX-ray3.30AU/CU1-88[»]
4V9BX-ray3.10AU/CU1-88[»]
4V9HX-ray2.86AR19-88[»]
4V9IX-ray3.30AR/CR19-88[»]
4V9RX-ray3.00AR/CR1-88[»]
4V9SX-ray3.10AR/CR1-88[»]
4W2EX-ray2.90r1-88[»]
4W2FX-ray2.40AR/CR1-88[»]
4W2GX-ray2.55AR/CR1-88[»]
4W2HX-ray2.70AR/CR1-88[»]
4W2IX-ray2.70AR/CR1-88[»]
4WPOX-ray2.80BR/DR1-88[»]
4WQFX-ray2.80BR/DR1-88[»]
4WQUX-ray2.80BR/DR1-88[»]
4WQYX-ray2.80BR/DR1-88[»]
4WT8X-ray3.40S19-88[»]
4WUSX-ray3.40S19-88[»]
4Y4OX-ray2.301r/2r1-88[»]
4Y4PX-ray2.501r/2r1-88[»]
4YHHX-ray3.42R16-88[»]
4Z3QX-ray2.601r/2r1-88[»]
4Z3RX-ray3.101r/2r1-88[»]
4Z3SX-ray2.651r/2r1-88[»]
4Z8CX-ray2.901r/2r1-88[»]
4ZERX-ray3.101r/2r20-87[»]
ProteinModelPortaliQ5SLQ0.
SMRiQ5SLQ0. Positions 8-88.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLQ0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S18P family.Curated

Phylogenomic databases

eggNOGiCOG0238.
HOGENOMiHOG000218466.
KOiK02963.
OMAiNFMNDKG.
OrthoDBiEOG6PCQ4R.
PhylomeDBiQ5SLQ0.

Family and domain databases

Gene3Di4.10.640.10. 1 hit.
HAMAPiMF_00270. Ribosomal_S18.
InterProiIPR001648. Ribosomal_S18.
IPR018275. Ribosomal_S18_CS.
[Graphical view]
PANTHERiPTHR13479. PTHR13479. 1 hit.
PfamiPF01084. Ribosomal_S18. 1 hit.
[Graphical view]
PRINTSiPR00974. RIBOSOMALS18.
ProDomiPD002239. Ribosomal_S18. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46911. SSF46911. 1 hit.
TIGRFAMsiTIGR00165. S18. 1 hit.
PROSITEiPS00057. RIBOSOMAL_S18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5SLQ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKNAKPKK EAQRRPSRKA KVKATLGEFD LRDYRNVEVL KRFLSETGKI
60 70 80
LPRRRTGLSA KEQRILAKTI KRARILGLLP FTEKLVRK
Length:88
Mass (Da):10,231
Last modified:January 23, 2007 - v3
Checksum:iCFDE7AC4953EF809
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171S → T AA sequence (PubMed:7957245).Curated

Mass spectrometryi

Molecular mass is 10101 Da from positions 2 - 88. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70066.1.
RefSeqiWP_008630522.1. NC_006461.1.
YP_143509.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70066; BAD70066; BAD70066.
GeneIDi3169870.
KEGGittj:TTHA0243.
PATRICi23955431. VBITheThe93045_0243.

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: BAD70066.1.
RefSeqiWP_008630522.1. NC_006461.1.
YP_143509.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00R1-88[»]
1FKAX-ray3.30R1-88[»]
1G1XX-ray2.60C/H1-88[»]
1HNWX-ray3.40R1-88[»]
1HNXX-ray3.40R1-88[»]
1HNZX-ray3.30R1-88[»]
1HR0X-ray3.20R1-88[»]
1I94X-ray3.20R2-88[»]
1I95X-ray4.50R2-88[»]
1I96X-ray4.20R2-88[»]
1I97X-ray4.50R2-88[»]
1IBKX-ray3.31R1-88[»]
1IBLX-ray3.11R1-88[»]
1IBMX-ray3.31R1-88[»]
1J5EX-ray3.05R1-88[»]
1JGOX-ray5.60U1-88[»]
1JGPX-ray7.00U1-88[»]
1JGQX-ray5.00U1-88[»]
1L1Umodel-R16-88[»]
1ML5electron microscopy14.00U1-88[»]
1N32X-ray3.00R1-88[»]
1N33X-ray3.35R1-88[»]
1N34X-ray3.80R1-88[»]
1N36X-ray3.65R1-88[»]
1VVJX-ray3.44QR/XR1-88[»]
1VY4X-ray2.60AR/CR1-88[»]
1VY5X-ray2.55AR/CR1-88[»]
1VY6X-ray2.90AR/CR1-88[»]
1VY7X-ray2.80AR/CR1-88[»]
1X18electron microscopy13.50H16-88[»]
1XMOX-ray3.25R1-88[»]
1XMQX-ray3.00R1-88[»]
1XNQX-ray3.05R1-88[»]
1XNRX-ray3.10R1-88[»]
2E5LX-ray3.30R2-88[»]
2F4VX-ray3.80R1-88[»]
2HHHX-ray3.35R1-88[»]
2UU9X-ray3.10R2-88[»]
2UUAX-ray2.90R2-88[»]
2UUBX-ray2.80R2-88[»]
2UUCX-ray3.10R2-88[»]
2UXBX-ray3.10R2-88[»]
2UXCX-ray2.90R2-88[»]
2UXDX-ray3.20R2-88[»]
2ZM6X-ray3.30R2-88[»]
3OTOX-ray3.69R1-88[»]
3T1HX-ray3.11R1-88[»]
3T1YX-ray2.80R1-88[»]
4AQYX-ray3.50R1-88[»]
4B3MX-ray2.90R1-88[»]
4B3RX-ray3.00R1-88[»]
4B3SX-ray3.15R1-88[»]
4B3TX-ray3.00R1-88[»]
4DR1X-ray3.60R1-88[»]
4DR2X-ray3.25R1-88[»]
4DR3X-ray3.35R1-88[»]
4DR4X-ray3.97R1-88[»]
4DR5X-ray3.45R1-88[»]
4DR6X-ray3.30R1-88[»]
4DR7X-ray3.75R1-88[»]
4DUYX-ray3.39R1-88[»]
4DUZX-ray3.65R1-88[»]
4DV0X-ray3.85R1-88[»]
4DV1X-ray3.85R1-88[»]
4DV2X-ray3.65R1-88[»]
4DV3X-ray3.55R1-88[»]
4DV4X-ray3.65R1-88[»]
4DV5X-ray3.68R1-88[»]
4DV6X-ray3.30R1-88[»]
4DV7X-ray3.29R1-88[»]
4GKJX-ray3.30R16-88[»]
4GKKX-ray3.20R16-88[»]
4JI0X-ray3.49R1-88[»]
4JI1X-ray3.14R1-88[»]
4JI2X-ray3.64R1-88[»]
4JI3X-ray3.35R1-88[»]
4JI4X-ray3.69R1-88[»]
4JI5X-ray3.85R1-88[»]
4JI6X-ray3.55R1-88[»]
4JI7X-ray3.50R1-88[»]
4JI8X-ray3.74R1-88[»]
4JV5X-ray3.16R19-88[»]
4JYAX-ray3.10R19-88[»]
4K0KX-ray3.40R19-88[»]
4KHPX-ray3.10R19-88[»]
4L47X-ray3.22QR/XR1-88[»]
4L71X-ray3.90QR/XR1-88[»]
4LELX-ray3.90QR/XR1-88[»]
4LF4X-ray3.34R1-88[»]
4LF5X-ray3.75R1-88[»]
4LF6X-ray3.31R1-88[»]
4LF7X-ray3.15R1-88[»]
4LF8X-ray3.15R1-88[»]
4LF9X-ray3.28R1-88[»]
4LFAX-ray3.65R1-88[»]
4LFBX-ray3.01R1-88[»]
4LFCX-ray3.60R1-88[»]
4LFZX-ray3.92QR/XR1-88[»]
4LNTX-ray2.94QR/XR1-88[»]
4LSKX-ray3.48QR/XR1-88[»]
4LT8X-ray3.14QR/XR1-88[»]
4NXMX-ray3.65R1-88[»]
4NXNX-ray3.54R1-88[»]
4OX9X-ray3.80R1-88[»]
4P6FX-ray3.60QR/XR1-88[»]
4P70X-ray3.68QR/XR1-88[»]
4TUAX-ray3.60QR/XR1-88[»]
4TUBX-ray3.60QR/XR1-88[»]
4TUCX-ray3.60QR/XR1-88[»]
4TUDX-ray3.60QR/XR1-88[»]
4TUEX-ray3.50QR/XR1-88[»]
4V42X-ray5.50U1-88[»]
4V49X-ray8.70R16-88[»]
4V4AX-ray9.50R16-88[»]
4V4GX-ray11.50R16-88[»]
4V4IX-ray3.71s1-88[»]
4V4PX-ray5.50BU1-88[»]
4V4RX-ray5.90AR1-88[»]
4V4SX-ray6.76AR1-88[»]
4V4TX-ray6.46AR1-88[»]
4V4XX-ray5.00AU1-88[»]
4V4YX-ray5.50AU1-88[»]
4V4ZX-ray4.51AU1-88[»]
4V51X-ray2.80AR/CR2-88[»]
4V5AX-ray3.50AR/CR2-88[»]
4V5CX-ray3.30AR/CR1-88[»]
4V5DX-ray3.50AR/CR1-88[»]
4V5EX-ray3.45AR/CR1-88[»]
4V5FX-ray3.60AR/CR1-88[»]
4V5GX-ray3.60AR/CR1-88[»]
4V5JX-ray3.10AR/CR1-88[»]
4V5KX-ray3.20AR/CR1-88[»]
4V5LX-ray3.10R1-88[»]
4V5Melectron microscopy7.80AR1-88[»]
4V5Nelectron microscopy7.60AR1-88[»]
4V5PX-ray3.10AR/CR1-88[»]
4V5QX-ray3.10AR/CR1-88[»]
4V5RX-ray3.10AR/CR1-88[»]
4V5SX-ray3.10AR/CR1-88[»]
4V68electron microscopy6.40AR19-88[»]
4V6AX-ray3.10AR/CR1-88[»]
4V6FX-ray3.10BU/CU1-88[»]
4V6GX-ray3.50AU/CU1-88[»]
4V7JX-ray3.30Ar/Br1-88[»]
4V7KX-ray3.60Ar/Br1-88[»]
4V7LX-ray3.00AR/CR1-88[»]
4V7MX-ray3.45AR/CR1-88[»]
4V7WX-ray3.00AR/CR1-88[»]
4V7XX-ray3.00AR/CR1-88[»]
4V7YX-ray3.00AR/CR1-88[»]
4V7ZX-ray3.10AR/CR1-88[»]
4V87X-ray3.10BU/CU1-88[»]
4V8AX-ray3.20CR/DR1-88[»]
4V8BX-ray3.00AU/CU1-88[»]
4V8CX-ray3.30CU/DU1-88[»]
4V8DX-ray3.00AU/CU1-88[»]
4V8EX-ray3.30BU/DU1-88[»]
4V8FX-ray3.30BU/CU1-88[»]
4V8GX-ray3.00AR/CR1-88[»]
4V8HX-ray3.10AR/CR1-88[»]
4V8IX-ray2.70AR/CR1-88[»]
4V8JX-ray3.90AR/CR1-88[»]
4V8NX-ray3.10AR/CR1-88[»]
4V8OX-ray3.80AR1-88[»]
4V8QX-ray3.10BR1-88[»]
4V8UX-ray3.70AR/CR1-88[»]
4V8XX-ray3.35AR/CR1-88[»]
4V90X-ray2.95AR1-88[»]
4V95X-ray3.20AR/CR1-88[»]
4V97X-ray3.52AR/CR1-88[»]
4V9AX-ray3.30AU/CU1-88[»]
4V9BX-ray3.10AU/CU1-88[»]
4V9HX-ray2.86AR19-88[»]
4V9IX-ray3.30AR/CR19-88[»]
4V9RX-ray3.00AR/CR1-88[»]
4V9SX-ray3.10AR/CR1-88[»]
4W2EX-ray2.90r1-88[»]
4W2FX-ray2.40AR/CR1-88[»]
4W2GX-ray2.55AR/CR1-88[»]
4W2HX-ray2.70AR/CR1-88[»]
4W2IX-ray2.70AR/CR1-88[»]
4WPOX-ray2.80BR/DR1-88[»]
4WQFX-ray2.80BR/DR1-88[»]
4WQUX-ray2.80BR/DR1-88[»]
4WQYX-ray2.80BR/DR1-88[»]
4WT8X-ray3.40S19-88[»]
4WUSX-ray3.40S19-88[»]
4Y4OX-ray2.301r/2r1-88[»]
4Y4PX-ray2.501r/2r1-88[»]
4YHHX-ray3.42R16-88[»]
4Z3QX-ray2.601r/2r1-88[»]
4Z3RX-ray3.101r/2r1-88[»]
4Z3SX-ray2.651r/2r1-88[»]
4Z8CX-ray2.901r/2r1-88[»]
4ZERX-ray3.101r/2r20-87[»]
ProteinModelPortaliQ5SLQ0.
SMRiQ5SLQ0. Positions 8-88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70066; BAD70066; BAD70066.
GeneIDi3169870.
KEGGittj:TTHA0243.
PATRICi23955431. VBITheThe93045_0243.

Phylogenomic databases

eggNOGiCOG0238.
HOGENOMiHOG000218466.
KOiK02963.
OMAiNFMNDKG.
OrthoDBiEOG6PCQ4R.
PhylomeDBiQ5SLQ0.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-252-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SLQ0.

Family and domain databases

Gene3Di4.10.640.10. 1 hit.
HAMAPiMF_00270. Ribosomal_S18.
InterProiIPR001648. Ribosomal_S18.
IPR018275. Ribosomal_S18_CS.
[Graphical view]
PANTHERiPTHR13479. PTHR13479. 1 hit.
PfamiPF01084. Ribosomal_S18. 1 hit.
[Graphical view]
PRINTSiPR00974. RIBOSOMALS18.
ProDomiPD002239. Ribosomal_S18. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46911. SSF46911. 1 hit.
TIGRFAMsiTIGR00165. S18. 1 hit.
PROSITEiPS00057. RIBOSOMAL_S18. 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 (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 2-26.
  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. "Structure of the S15,S6,S18-rRNA complex: assembly of the 30S ribosome central domain."
    Agalarov S.C., Prasad G.S., Funke P.M., Stout C.D., Williamson J.R.
    Science 288:107-113(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF A 30S SUBUNIT FRAGMENT.
  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 (5.0 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.
  15. "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 nameiRS18_THET8
AccessioniPrimary (citable) accession number: Q5SLQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 104 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.