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Protein

30S ribosomal protein S11

Gene

rpsK

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

Located on the upper part of the platform of the 30S subunit, where it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome, where it interacts both with the Shine-Dalgarno helix and mRNA.

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-1705-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S11
Gene namesi
Name:rpsK
Synonyms:rps11
Ordered Locus Names:TTHA1666
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 – 12912830S ribosomal protein S11PRO_0000123246Add
BLAST

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Interacts with proteins S7 and S18. Binds to the C-terminus of IF-3; however exactly how IF-3 interacts with the 30S subunit is unclear. May contact the C-terminus of Era.

Protein-protein interaction databases

STRINGi300852.TTHA1666.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 239Combined sources
Beta strandi24 – 263Combined sources
Beta strandi28 – 336Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 424Combined sources
Turni45 – 495Combined sources
Helixi53 – 564Combined sources
Helixi58 – 7316Combined sources
Turni74 – 763Combined sources
Beta strandi79 – 868Combined sources
Helixi91 – 999Combined sources
Beta strandi101 – 1077Combined sources
Helixi123 – 1253Combined sources
Turni126 – 1283Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00K1-129[»]
1HNWX-ray3.40K1-129[»]
1HNXX-ray3.40K1-129[»]
1HNZX-ray3.30K1-129[»]
1HR0X-ray3.20K1-129[»]
1I94X-ray3.20K2-129[»]
1I95X-ray4.50K2-129[»]
1I96X-ray4.20K2-129[»]
1I97X-ray4.50K2-129[»]
1IBKX-ray3.31K1-129[»]
1IBLX-ray3.11K1-129[»]
1IBMX-ray3.31K1-129[»]
1J5EX-ray3.05K1-129[»]
1JGOX-ray5.60N1-129[»]
1JGPX-ray7.00N1-129[»]
1JGQX-ray5.00N1-129[»]
1L1Umodel-K11-129[»]
1ML5electron microscopy14.00N1-129[»]
1N32X-ray3.00K1-129[»]
1N33X-ray3.35K1-129[»]
1N34X-ray3.80K1-129[»]
1N36X-ray3.65K1-129[»]
1VVJX-ray3.44QK/XK1-129[»]
1VY4X-ray2.60AK/CK1-129[»]
1VY5X-ray2.55AK/CK1-129[»]
1VY6X-ray2.90AK/CK1-129[»]
1VY7X-ray2.80AK/CK1-129[»]
1X18electron microscopy13.50G11-129[»]
1XMOX-ray3.25K1-129[»]
1XMQX-ray3.00K1-129[»]
1XNQX-ray3.05K1-129[»]
1XNRX-ray3.10K1-129[»]
2E5LX-ray3.30K2-129[»]
2F4VX-ray3.80K1-129[»]
2HHHX-ray3.35K1-129[»]
2UU9X-ray3.10K2-129[»]
2UUAX-ray2.90K2-129[»]
2UUBX-ray2.90K2-129[»]
2UUCX-ray3.10K2-129[»]
2UXBX-ray3.10K2-129[»]
2UXCX-ray2.90K2-129[»]
2UXDX-ray3.20K2-129[»]
2VQEX-ray2.50K1-129[»]
2VQFX-ray2.90K1-129[»]
2ZM6X-ray3.30K2-129[»]
3OTOX-ray3.69K1-129[»]
3T1HX-ray3.11K1-129[»]
3T1YX-ray2.80K1-129[»]
4AQYX-ray3.50K1-129[»]
4B3MX-ray2.90K1-129[»]
4B3RX-ray3.00K1-129[»]
4B3SX-ray3.15K1-129[»]
4B3TX-ray3.00K1-129[»]
4DR1X-ray3.60K1-129[»]
4DR2X-ray3.25K1-129[»]
4DR3X-ray3.35K1-129[»]
4DR4X-ray3.97K1-129[»]
4DR5X-ray3.45K1-129[»]
4DR6X-ray3.30K1-129[»]
4DR7X-ray3.75K1-129[»]
4DUYX-ray3.39K1-129[»]
4DUZX-ray3.65K1-129[»]
4DV0X-ray3.85K1-129[»]
4DV1X-ray3.85K1-129[»]
4DV2X-ray3.65K1-129[»]
4DV3X-ray3.55K1-129[»]
4DV4X-ray3.65K1-129[»]
4DV5X-ray3.68K1-129[»]
4DV6X-ray3.30K1-129[»]
4DV7X-ray3.29K1-129[»]
4GKJX-ray3.30K11-129[»]
4GKKX-ray3.20K11-129[»]
4JI0X-ray3.49K1-129[»]
4JI1X-ray3.14K1-129[»]
4JI2X-ray3.64K1-129[»]
4JI3X-ray3.35K1-129[»]
4JI4X-ray3.69K1-129[»]
4JI5X-ray3.85K1-129[»]
4JI6X-ray3.55K1-129[»]
4JI7X-ray3.50K1-129[»]
4JI8X-ray3.74K1-129[»]
4JV5X-ray3.16K11-129[»]
4JYAX-ray3.10K11-129[»]
4K0KX-ray3.40K11-129[»]
4KHPX-ray3.10K11-129[»]
4L47X-ray3.22QK/XK1-129[»]
4L71X-ray3.90QK/XK1-129[»]
4LELX-ray3.90QK/XK1-129[»]
4LF4X-ray3.34K1-129[»]
4LF5X-ray3.75K1-129[»]
4LF6X-ray3.31K1-129[»]
4LF7X-ray3.15K1-129[»]
4LF8X-ray3.15K1-129[»]
4LF9X-ray3.28K1-129[»]
4LFAX-ray3.65K1-129[»]
4LFBX-ray3.01K1-129[»]
4LFCX-ray3.60K1-129[»]
4LFZX-ray3.92QK/XK1-129[»]
4LNTX-ray2.94QK/XK1-129[»]
4LSKX-ray3.48QK/XK1-129[»]
4LT8X-ray3.14QK/XK1-129[»]
4NXMX-ray3.65K1-129[»]
4NXNX-ray3.54K1-129[»]
4OX9X-ray3.80K1-129[»]
4P6FX-ray3.60QK/XK1-129[»]
4P70X-ray3.68QK/XK1-129[»]
4TUAX-ray3.60QK/XK1-129[»]
4TUBX-ray3.60QK/XK1-129[»]
4TUCX-ray3.60QK/XK1-129[»]
4TUDX-ray3.60QK/XK1-129[»]
4TUEX-ray3.50QK/XK1-129[»]
4V42X-ray5.50AN1-129[»]
4V49X-ray8.70K11-129[»]
4V4AX-ray9.50K11-129[»]
4V4IX-ray3.71l-[»]
4V4PX-ray5.50BN1-129[»]
4V4RX-ray5.90AK1-129[»]
4V4SX-ray6.76AK1-129[»]
4V4TX-ray6.46AK1-129[»]
4V4XX-ray5.00AN1-129[»]
4V4YX-ray5.50AN1-129[»]
4V4ZX-ray4.51AN1-129[»]
4V51X-ray2.80AK/CK2-129[»]
4V5AX-ray3.50AK/CK2-129[»]
4V5CX-ray3.30AK/CK1-129[»]
4V5DX-ray3.50AK/CK1-129[»]
4V5EX-ray3.45AK/CK1-129[»]
4V5FX-ray3.60AK/CK1-129[»]
4V5GX-ray3.60AK/CK1-129[»]
4V5JX-ray3.10AK/CK1-129[»]
4V5KX-ray3.20AK/CK1-129[»]
4V5LX-ray3.10AK1-129[»]
4V5Melectron microscopy7.80AK1-129[»]
4V5Nelectron microscopy7.60AK1-129[»]
4V5PX-ray3.10AK/CK1-129[»]
4V5QX-ray3.10AK/CK1-129[»]
4V5RX-ray3.10AK/CK1-129[»]
4V5SX-ray3.10AK/CK1-129[»]
4V68electron microscopy6.40AK11-129[»]
4V6AX-ray3.10AK/CK1-129[»]
4V6FX-ray3.10BN/CN1-129[»]
4V6GX-ray3.50AN/CN1-129[»]
4V7JX-ray3.30Ak/Bk1-129[»]
4V7KX-ray3.60Ak/Bk1-129[»]
4V7LX-ray3.00AK/CK1-129[»]
4V7MX-ray3.45AK/CK1-129[»]
4V7WX-ray3.00AK/CK1-129[»]
4V7XX-ray3.00AK/CK1-129[»]
4V7YX-ray3.00AK/CK1-129[»]
4V7ZX-ray3.10AK/CK1-129[»]
4V87X-ray3.10BN/CN1-129[»]
4V8AX-ray3.20CK/DK1-129[»]
4V8BX-ray3.00AN/CN1-129[»]
4V8CX-ray3.30CN/DN1-129[»]
4V8DX-ray3.00AN/CN1-129[»]
4V8EX-ray3.30BN/DN1-129[»]
4V8FX-ray3.30BN/CN1-129[»]
4V8GX-ray3.00AK/CK1-129[»]
4V8HX-ray3.10AK/CK1-129[»]
4V8IX-ray2.70AK/CK1-129[»]
4V8JX-ray3.90AK/CK1-129[»]
4V8NX-ray3.10AK/CK1-129[»]
4V8OX-ray3.80AK1-129[»]
4V8QX-ray3.10BK1-129[»]
4V8UX-ray3.70AK/CK1-129[»]
4V8XX-ray3.35AK/CK1-129[»]
4V90X-ray2.95AK1-129[»]
4V95X-ray3.20AK/CK1-129[»]
4V97X-ray3.52AK/CK1-129[»]
4V9AX-ray3.30AN/CN1-129[»]
4V9BX-ray3.10AN/CN1-129[»]
4V9HX-ray2.86AK11-129[»]
4V9IX-ray3.30AK/CK11-129[»]
4V9RX-ray3.00AK/CK1-129[»]
4V9SX-ray3.10AK/CK1-129[»]
4W2EX-ray2.90k1-129[»]
4W2FX-ray2.40AK/CK1-129[»]
4W2GX-ray2.55AK/CK1-129[»]
4W2HX-ray2.70AK/CK1-129[»]
4W2IX-ray2.70AK/CK1-129[»]
4WPOX-ray2.80BK/DK1-129[»]
4WQFX-ray2.80BK/DK1-129[»]
4WQUX-ray2.80BK/DK1-129[»]
4WQYX-ray2.80BK/DK1-129[»]
4WT8X-ray3.40K11-129[»]
4WUSX-ray3.40K11-129[»]
4Y4OX-ray2.301k/2k1-129[»]
4Y4PX-ray2.501k/2k1-129[»]
4YHHX-ray3.42K11-125[»]
4Z3QX-ray2.601k/2k1-129[»]
4Z3RX-ray3.101k/2k1-129[»]
4Z3SX-ray2.651k/2k1-129[»]
4Z8CX-ray2.901k/2k1-129[»]
4ZERX-ray3.101k/2k13-126[»]
ProteinModelPortaliP80376.
SMRiP80376. Positions 7-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80376.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S11P family.Curated

Phylogenomic databases

eggNOGiCOG0100.
HOGENOMiHOG000111597.
KOiK02948.
OMAiKNVANGH.
OrthoDBiEOG6ZSPF3.
PhylomeDBiP80376.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
TIGRFAMsiTIGR03632. uS11_bact. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P80376-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKPSKKKV KRQVASGRAY IHASYNNTIV TITDPDGNPI TWSSGGVIGY
60 70 80 90 100
KGSRKGTPYA AQLAALDAAK KAMAYGMQSV DVIVRGTGAG REQAIRALQA
110 120
SGLQVKSIVD DTPVPHNGCR PKKKFRKAS
Length:129
Mass (Da):13,713
Last modified:January 23, 2007 - v3
Checksum:i028E047E6DCE3CA2
GO

Mass spectrometryi

Molecular mass is 13583 Da from positions 2 - 129. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024328 Genomic DNA. Translation: BAA75547.1.
AP008226 Genomic DNA. Translation: BAD71489.1.
RefSeqiWP_008633365.1. NC_006461.1.
YP_144932.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71489; BAD71489; BAD71489.
GeneIDi3168024.
KEGGittj:TTHA1666.
PATRICi23958287. VBITheThe93045_1636.

Cross-referencesi

Web resourcesi

T.thermophilus ribosome structure and function

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024328 Genomic DNA. Translation: BAA75547.1.
AP008226 Genomic DNA. Translation: BAD71489.1.
RefSeqiWP_008633365.1. NC_006461.1.
YP_144932.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00K1-129[»]
1HNWX-ray3.40K1-129[»]
1HNXX-ray3.40K1-129[»]
1HNZX-ray3.30K1-129[»]
1HR0X-ray3.20K1-129[»]
1I94X-ray3.20K2-129[»]
1I95X-ray4.50K2-129[»]
1I96X-ray4.20K2-129[»]
1I97X-ray4.50K2-129[»]
1IBKX-ray3.31K1-129[»]
1IBLX-ray3.11K1-129[»]
1IBMX-ray3.31K1-129[»]
1J5EX-ray3.05K1-129[»]
1JGOX-ray5.60N1-129[»]
1JGPX-ray7.00N1-129[»]
1JGQX-ray5.00N1-129[»]
1L1Umodel-K11-129[»]
1ML5electron microscopy14.00N1-129[»]
1N32X-ray3.00K1-129[»]
1N33X-ray3.35K1-129[»]
1N34X-ray3.80K1-129[»]
1N36X-ray3.65K1-129[»]
1VVJX-ray3.44QK/XK1-129[»]
1VY4X-ray2.60AK/CK1-129[»]
1VY5X-ray2.55AK/CK1-129[»]
1VY6X-ray2.90AK/CK1-129[»]
1VY7X-ray2.80AK/CK1-129[»]
1X18electron microscopy13.50G11-129[»]
1XMOX-ray3.25K1-129[»]
1XMQX-ray3.00K1-129[»]
1XNQX-ray3.05K1-129[»]
1XNRX-ray3.10K1-129[»]
2E5LX-ray3.30K2-129[»]
2F4VX-ray3.80K1-129[»]
2HHHX-ray3.35K1-129[»]
2UU9X-ray3.10K2-129[»]
2UUAX-ray2.90K2-129[»]
2UUBX-ray2.90K2-129[»]
2UUCX-ray3.10K2-129[»]
2UXBX-ray3.10K2-129[»]
2UXCX-ray2.90K2-129[»]
2UXDX-ray3.20K2-129[»]
2VQEX-ray2.50K1-129[»]
2VQFX-ray2.90K1-129[»]
2ZM6X-ray3.30K2-129[»]
3OTOX-ray3.69K1-129[»]
3T1HX-ray3.11K1-129[»]
3T1YX-ray2.80K1-129[»]
4AQYX-ray3.50K1-129[»]
4B3MX-ray2.90K1-129[»]
4B3RX-ray3.00K1-129[»]
4B3SX-ray3.15K1-129[»]
4B3TX-ray3.00K1-129[»]
4DR1X-ray3.60K1-129[»]
4DR2X-ray3.25K1-129[»]
4DR3X-ray3.35K1-129[»]
4DR4X-ray3.97K1-129[»]
4DR5X-ray3.45K1-129[»]
4DR6X-ray3.30K1-129[»]
4DR7X-ray3.75K1-129[»]
4DUYX-ray3.39K1-129[»]
4DUZX-ray3.65K1-129[»]
4DV0X-ray3.85K1-129[»]
4DV1X-ray3.85K1-129[»]
4DV2X-ray3.65K1-129[»]
4DV3X-ray3.55K1-129[»]
4DV4X-ray3.65K1-129[»]
4DV5X-ray3.68K1-129[»]
4DV6X-ray3.30K1-129[»]
4DV7X-ray3.29K1-129[»]
4GKJX-ray3.30K11-129[»]
4GKKX-ray3.20K11-129[»]
4JI0X-ray3.49K1-129[»]
4JI1X-ray3.14K1-129[»]
4JI2X-ray3.64K1-129[»]
4JI3X-ray3.35K1-129[»]
4JI4X-ray3.69K1-129[»]
4JI5X-ray3.85K1-129[»]
4JI6X-ray3.55K1-129[»]
4JI7X-ray3.50K1-129[»]
4JI8X-ray3.74K1-129[»]
4JV5X-ray3.16K11-129[»]
4JYAX-ray3.10K11-129[»]
4K0KX-ray3.40K11-129[»]
4KHPX-ray3.10K11-129[»]
4L47X-ray3.22QK/XK1-129[»]
4L71X-ray3.90QK/XK1-129[»]
4LELX-ray3.90QK/XK1-129[»]
4LF4X-ray3.34K1-129[»]
4LF5X-ray3.75K1-129[»]
4LF6X-ray3.31K1-129[»]
4LF7X-ray3.15K1-129[»]
4LF8X-ray3.15K1-129[»]
4LF9X-ray3.28K1-129[»]
4LFAX-ray3.65K1-129[»]
4LFBX-ray3.01K1-129[»]
4LFCX-ray3.60K1-129[»]
4LFZX-ray3.92QK/XK1-129[»]
4LNTX-ray2.94QK/XK1-129[»]
4LSKX-ray3.48QK/XK1-129[»]
4LT8X-ray3.14QK/XK1-129[»]
4NXMX-ray3.65K1-129[»]
4NXNX-ray3.54K1-129[»]
4OX9X-ray3.80K1-129[»]
4P6FX-ray3.60QK/XK1-129[»]
4P70X-ray3.68QK/XK1-129[»]
4TUAX-ray3.60QK/XK1-129[»]
4TUBX-ray3.60QK/XK1-129[»]
4TUCX-ray3.60QK/XK1-129[»]
4TUDX-ray3.60QK/XK1-129[»]
4TUEX-ray3.50QK/XK1-129[»]
4V42X-ray5.50AN1-129[»]
4V49X-ray8.70K11-129[»]
4V4AX-ray9.50K11-129[»]
4V4IX-ray3.71l-[»]
4V4PX-ray5.50BN1-129[»]
4V4RX-ray5.90AK1-129[»]
4V4SX-ray6.76AK1-129[»]
4V4TX-ray6.46AK1-129[»]
4V4XX-ray5.00AN1-129[»]
4V4YX-ray5.50AN1-129[»]
4V4ZX-ray4.51AN1-129[»]
4V51X-ray2.80AK/CK2-129[»]
4V5AX-ray3.50AK/CK2-129[»]
4V5CX-ray3.30AK/CK1-129[»]
4V5DX-ray3.50AK/CK1-129[»]
4V5EX-ray3.45AK/CK1-129[»]
4V5FX-ray3.60AK/CK1-129[»]
4V5GX-ray3.60AK/CK1-129[»]
4V5JX-ray3.10AK/CK1-129[»]
4V5KX-ray3.20AK/CK1-129[»]
4V5LX-ray3.10AK1-129[»]
4V5Melectron microscopy7.80AK1-129[»]
4V5Nelectron microscopy7.60AK1-129[»]
4V5PX-ray3.10AK/CK1-129[»]
4V5QX-ray3.10AK/CK1-129[»]
4V5RX-ray3.10AK/CK1-129[»]
4V5SX-ray3.10AK/CK1-129[»]
4V68electron microscopy6.40AK11-129[»]
4V6AX-ray3.10AK/CK1-129[»]
4V6FX-ray3.10BN/CN1-129[»]
4V6GX-ray3.50AN/CN1-129[»]
4V7JX-ray3.30Ak/Bk1-129[»]
4V7KX-ray3.60Ak/Bk1-129[»]
4V7LX-ray3.00AK/CK1-129[»]
4V7MX-ray3.45AK/CK1-129[»]
4V7WX-ray3.00AK/CK1-129[»]
4V7XX-ray3.00AK/CK1-129[»]
4V7YX-ray3.00AK/CK1-129[»]
4V7ZX-ray3.10AK/CK1-129[»]
4V87X-ray3.10BN/CN1-129[»]
4V8AX-ray3.20CK/DK1-129[»]
4V8BX-ray3.00AN/CN1-129[»]
4V8CX-ray3.30CN/DN1-129[»]
4V8DX-ray3.00AN/CN1-129[»]
4V8EX-ray3.30BN/DN1-129[»]
4V8FX-ray3.30BN/CN1-129[»]
4V8GX-ray3.00AK/CK1-129[»]
4V8HX-ray3.10AK/CK1-129[»]
4V8IX-ray2.70AK/CK1-129[»]
4V8JX-ray3.90AK/CK1-129[»]
4V8NX-ray3.10AK/CK1-129[»]
4V8OX-ray3.80AK1-129[»]
4V8QX-ray3.10BK1-129[»]
4V8UX-ray3.70AK/CK1-129[»]
4V8XX-ray3.35AK/CK1-129[»]
4V90X-ray2.95AK1-129[»]
4V95X-ray3.20AK/CK1-129[»]
4V97X-ray3.52AK/CK1-129[»]
4V9AX-ray3.30AN/CN1-129[»]
4V9BX-ray3.10AN/CN1-129[»]
4V9HX-ray2.86AK11-129[»]
4V9IX-ray3.30AK/CK11-129[»]
4V9RX-ray3.00AK/CK1-129[»]
4V9SX-ray3.10AK/CK1-129[»]
4W2EX-ray2.90k1-129[»]
4W2FX-ray2.40AK/CK1-129[»]
4W2GX-ray2.55AK/CK1-129[»]
4W2HX-ray2.70AK/CK1-129[»]
4W2IX-ray2.70AK/CK1-129[»]
4WPOX-ray2.80BK/DK1-129[»]
4WQFX-ray2.80BK/DK1-129[»]
4WQUX-ray2.80BK/DK1-129[»]
4WQYX-ray2.80BK/DK1-129[»]
4WT8X-ray3.40K11-129[»]
4WUSX-ray3.40K11-129[»]
4Y4OX-ray2.301k/2k1-129[»]
4Y4PX-ray2.501k/2k1-129[»]
4YHHX-ray3.42K11-125[»]
4Z3QX-ray2.601k/2k1-129[»]
4Z3RX-ray3.101k/2k1-129[»]
4Z3SX-ray2.651k/2k1-129[»]
4Z8CX-ray2.901k/2k1-129[»]
4ZERX-ray3.101k/2k13-126[»]
ProteinModelPortaliP80376.
SMRiP80376. Positions 7-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1666.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71489; BAD71489; BAD71489.
GeneIDi3168024.
KEGGittj:TTHA1666.
PATRICi23958287. VBITheThe93045_1636.

Phylogenomic databases

eggNOGiCOG0100.
HOGENOMiHOG000111597.
KOiK02948.
OMAiKNVANGH.
OrthoDBiEOG6ZSPF3.
PhylomeDBiP80376.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1705-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP80376.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR019981. Ribosomal_S11_bac-type.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
TIGRFAMsiTIGR03632. uS11_bact. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the RNA polymerase alpha subunit gene from Thermus thermophilus HB8 and characterization of the protein."
    Wada T., Yamazaki T., Kuramitsu S., Kyogoku Y.
    J. Biochem. 125:143-150(1999) [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 2-26.
  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: 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 (5.0 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), POSSIBLE INTERACTION WITH ERA.

Entry informationi

Entry nameiRS11_THET8
AccessioniPrimary (citable) accession number: P80376
Secondary accession number(s): Q5SHR4, Q9RA66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: July 22, 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.