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Protein

30S ribosomal protein S2

Gene

rpsB

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

Spans the head-body hinge region of the 30S subunit. Is loosely associated with the 30S subunit.

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-893-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S2
Gene namesi
Name:rpsB
Synonyms:rps2
Ordered Locus Names:TTHA0861
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 – 25625530S ribosomal protein S2PRO_0000134264Add
BLAST

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts protein S8 and may contact the N-terminus of Era.

Protein-protein interaction databases

STRINGi300852.TTHA0861.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Helixi9 – 113Combined sources
Helixi12 – 143Combined sources
Beta strandi15 – 184Combined sources
Beta strandi20 – 234Combined sources
Helixi26 – 283Combined sources
Helixi29 – 313Combined sources
Beta strandi32 – 365Combined sources
Beta strandi39 – 424Combined sources
Helixi44 – 6219Combined sources
Turni63 – 653Combined sources
Beta strandi68 – 714Combined sources
Beta strandi74 – 774Combined sources
Turni78 – 869Combined sources
Beta strandi87 – 893Combined sources
Turni99 – 1046Combined sources
Helixi105 – 12117Combined sources
Beta strandi122 – 1243Combined sources
Helixi127 – 1293Combined sources
Helixi132 – 1354Combined sources
Helixi138 – 14811Combined sources
Beta strandi149 – 1513Combined sources
Helixi152 – 1543Combined sources
Beta strandi156 – 1583Combined sources
Beta strandi160 – 1656Combined sources
Turni167 – 1704Combined sources
Helixi171 – 1799Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi190 – 1923Combined sources
Helixi194 – 1963Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi205 – 2073Combined sources
Helixi208 – 22316Combined sources
Turni224 – 2263Combined sources
Turni234 – 2396Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00B1-256[»]
1HNWX-ray3.40B1-256[»]
1HNXX-ray3.40B1-256[»]
1HNZX-ray3.30B1-256[»]
1HR0X-ray3.20B1-256[»]
1I94X-ray3.20B2-256[»]
1I95X-ray4.50B2-256[»]
1I96X-ray4.20B2-256[»]
1I97X-ray4.50B2-256[»]
1IBKX-ray3.31B1-256[»]
1IBLX-ray3.11B1-256[»]
1IBMX-ray3.31B1-256[»]
1J5EX-ray3.05B1-256[»]
1JGOX-ray5.60E1-256[»]
1JGPX-ray7.00E1-256[»]
1JGQX-ray5.00E1-256[»]
1L1Umodel-B7-240[»]
1ML5electron microscopy14.00E1-256[»]
1N32X-ray3.00B1-256[»]
1N33X-ray3.35B1-256[»]
1N34X-ray3.80B1-256[»]
1N36X-ray3.65B1-256[»]
1VVJX-ray3.44QB/XB1-256[»]
1VY4X-ray2.60AB/CB1-256[»]
1VY5X-ray2.55AB/CB1-256[»]
1VY6X-ray2.90AB/CB1-256[»]
1VY7X-ray2.80AB/CB1-256[»]
1X18electron microscopy13.50E7-240[»]
1XMOX-ray3.25B1-256[»]
1XMQX-ray3.00B1-256[»]
1XNQX-ray3.05B1-256[»]
1XNRX-ray3.10B1-256[»]
2E5LX-ray3.30B2-228[»]
2F4VX-ray3.80B1-256[»]
2HHHX-ray3.35B1-256[»]
2OM7electron microscopy7.30N1-256[»]
2UU9X-ray3.10B2-256[»]
2UUAX-ray2.90B2-256[»]
2UUBX-ray2.80B2-256[»]
2UUCX-ray3.10B2-256[»]
2UXBX-ray3.10B2-256[»]
2UXCX-ray2.90B2-256[»]
2UXDX-ray3.20B2-256[»]
2VQEX-ray2.50B1-256[»]
2VQFX-ray2.90B1-256[»]
2ZM6X-ray3.30B2-256[»]
3OTOX-ray3.69B1-256[»]
3T1HX-ray3.11B1-256[»]
3T1YX-ray2.80B1-256[»]
4AQYX-ray3.50B1-256[»]
4B3MX-ray2.90B1-256[»]
4B3RX-ray3.00B1-256[»]
4B3SX-ray3.15B1-256[»]
4B3TX-ray3.00B1-256[»]
4DR1X-ray3.60B1-256[»]
4DR2X-ray3.25B1-256[»]
4DR3X-ray3.35B1-256[»]
4DR4X-ray3.97B1-256[»]
4DR5X-ray3.45B1-256[»]
4DR6X-ray3.30B1-256[»]
4DR7X-ray3.75B1-256[»]
4DUYX-ray3.39B1-256[»]
4DUZX-ray3.65B1-256[»]
4DV0X-ray3.85B1-256[»]
4DV1X-ray3.85B1-256[»]
4DV2X-ray3.65B1-256[»]
4DV3X-ray3.55B1-256[»]
4DV4X-ray3.65B1-256[»]
4DV5X-ray3.68B1-256[»]
4DV6X-ray3.30B1-256[»]
4DV7X-ray3.29B1-256[»]
4GKJX-ray3.30B7-240[»]
4GKKX-ray3.20B7-240[»]
4JI0X-ray3.49B1-256[»]
4JI1X-ray3.14B1-256[»]
4JI2X-ray3.64B1-256[»]
4JI3X-ray3.35B1-256[»]
4JI4X-ray3.69B1-256[»]
4JI5X-ray3.85B1-256[»]
4JI6X-ray3.55B1-256[»]
4JI7X-ray3.50B1-256[»]
4JI8X-ray3.74B1-256[»]
4JV5X-ray3.16B7-240[»]
4JYAX-ray3.10B7-240[»]
4K0KX-ray3.40B7-241[»]
4KHPX-ray3.10B7-240[»]
4L47X-ray3.22QB/XB1-256[»]
4L71X-ray3.90QB/XB1-256[»]
4LELX-ray3.90QB/XB1-256[»]
4LF4X-ray3.34B1-256[»]
4LF5X-ray3.75B1-256[»]
4LF6X-ray3.31B1-256[»]
4LF7X-ray3.15B1-256[»]
4LF8X-ray3.15B1-256[»]
4LF9X-ray3.28B1-256[»]
4LFAX-ray3.65B1-256[»]
4LFBX-ray3.01B1-256[»]
4LFCX-ray3.60B1-256[»]
4LFZX-ray3.92QB/XB1-256[»]
4LNTX-ray2.94QB/XB1-256[»]
4LSKX-ray3.48QB/XB1-256[»]
4LT8X-ray3.14QB/XB1-256[»]
4NXMX-ray3.65B1-256[»]
4NXNX-ray3.54B1-256[»]
4OX9X-ray3.80B1-256[»]
4P6FX-ray3.60QB/XB1-256[»]
4P70X-ray3.68QB/XB1-256[»]
4TUAX-ray3.60QB/XB1-256[»]
4TUBX-ray3.60QB/XB1-256[»]
4TUCX-ray3.60QB/XB1-256[»]
4TUDX-ray3.60QB/XB1-256[»]
4TUEX-ray3.50QB/XB1-256[»]
4V42X-ray5.50AE1-256[»]
4V49X-ray8.70B7-240[»]
4V4AX-ray9.50B7-240[»]
4V4PX-ray5.50BE1-256[»]
4V4RX-ray5.90AB1-256[»]
4V4SX-ray6.76AB1-256[»]
4V4TX-ray6.46AB1-256[»]
4V4XX-ray5.00AE1-256[»]
4V4YX-ray5.50AE1-256[»]
4V4ZX-ray4.51AE1-256[»]
4V51X-ray2.80AB/CB2-256[»]
4V5AX-ray3.50AB/CB2-256[»]
4V5CX-ray3.30AB/CB1-256[»]
4V5DX-ray3.50AB/CB1-256[»]
4V5EX-ray3.45AB/CB1-256[»]
4V5FX-ray3.60AB/CB1-256[»]
4V5GX-ray3.60AB/CB1-256[»]
4V5JX-ray3.10AB/CB1-256[»]
4V5KX-ray3.20AB/CB1-256[»]
4V5LX-ray3.10AB1-256[»]
4V5Melectron microscopy7.80AB1-256[»]
4V5Nelectron microscopy7.60AB1-256[»]
4V5PX-ray3.10AB/CB1-256[»]
4V5QX-ray3.10AB/CB1-256[»]
4V5RX-ray3.10AB/CB1-256[»]
4V5SX-ray3.10AB/CB1-256[»]
4V68electron microscopy6.40AB7-241[»]
4V6AX-ray3.10AB/CB1-256[»]
4V6FX-ray3.10BE/CE1-256[»]
4V6GX-ray3.50AE/CE1-256[»]
4V7JX-ray3.30Ab/Bb1-256[»]
4V7KX-ray3.60Ab/Bb1-256[»]
4V7LX-ray3.00AB/CB1-256[»]
4V7MX-ray3.45AB/CB1-256[»]
4V7WX-ray3.00AB/CB1-256[»]
4V7XX-ray3.00AB/CB1-256[»]
4V7YX-ray3.00AB/CB1-256[»]
4V7ZX-ray3.10AB/CB1-256[»]
4V87X-ray3.10BE/CE1-256[»]
4V8AX-ray3.20CB/DB1-256[»]
4V8BX-ray3.00AE/CE1-256[»]
4V8CX-ray3.30CE/DE1-256[»]
4V8DX-ray3.00AE/CE1-256[»]
4V8EX-ray3.30BE/DE1-256[»]
4V8FX-ray3.30BE/CE1-256[»]
4V8GX-ray3.00AB/CB1-256[»]
4V8HX-ray3.10AB/CB1-256[»]
4V8IX-ray2.70AB/CB1-256[»]
4V8JX-ray3.90AB/CB1-256[»]
4V8NX-ray3.10AB/CB1-256[»]
4V8OX-ray3.80AB1-256[»]
4V8QX-ray3.10BB1-256[»]
4V8UX-ray3.70AB/CB1-256[»]
4V8XX-ray3.35AB/CB1-256[»]
4V90X-ray2.95AB1-256[»]
4V95X-ray3.20AB/CB1-256[»]
4V97X-ray3.52AB/CB1-256[»]
4V9AX-ray3.30AE/CE1-256[»]
4V9BX-ray3.10AE/CE1-256[»]
4V9HX-ray2.86AB7-240[»]
4V9IX-ray3.30AB/CB7-240[»]
4V9RX-ray3.00AB/CB1-256[»]
4V9SX-ray3.10AB/CB1-256[»]
4W2EX-ray2.90b1-256[»]
4W2FX-ray2.40AB/CB1-256[»]
4W2GX-ray2.55AB/CB1-256[»]
4W2HX-ray2.70AB/CB1-256[»]
4W2IX-ray2.70AB/CB1-256[»]
4WPOX-ray2.80BB/DB1-256[»]
4WQFX-ray2.80BB/DB1-256[»]
4WQUX-ray2.80BB/DB1-256[»]
4WQYX-ray2.80BB/DB1-256[»]
4WT8X-ray3.40A7-240[»]
4WUSX-ray3.40A7-240[»]
4Y4OX-ray2.301b/2b1-256[»]
4Y4PX-ray2.501b/2b1-256[»]
4YHHX-ray3.42B3-228[»]
ProteinModelPortaliP80371.
SMRiP80371. Positions 2-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80371.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili104 – 14946Add
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S2P family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0052.
HOGENOMiHOG000071892.
KOiK02967.
OMAiLEFAYNI.
OrthoDBiEOG6XWV6P.
PhylomeDBiP80371.

Family and domain databases

HAMAPiMF_00291_B. Ribosomal_S2_B.
InterProiIPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR12534. PTHR12534. 1 hit.
PfamiPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01011. rpsB_bact. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P80371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVEITVKEL LEAGVHFGHE RKRWNPKFAR YIYAERNGIH IIDLQKTMEE
60 70 80 90 100
LERTFRFIED LAMRGGTILF VGTKKQAQDI VRMEAERAGM PYVNQRWLGG
110 120 130 140 150
MLTNFKTISQ RVHRLEELEA LFASPEIEER PKKEQVRLKH ELERLQKYLS
160 170 180 190 200
GFRLLKRLPD AIFVVDPTKE AIAVREARKL FIPVIALADT DSDPDLVDYI
210 220 230 240 250
IPGNDDAIRS IQLILSRAVD LIIQARGGVV EPSPSYALVQ EAEATETPEG

ESEVEA
Length:256
Mass (Da):29,277
Last modified:January 23, 2007 - v4
Checksum:i65D7958336911CE5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191H → N AA sequence (PubMed:7957245).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70684.1.
X83598 Genomic DNA. Translation: CAA58577.1.
PIRiS51053.
RefSeqiWP_011172954.1. NC_006461.1.
YP_144127.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70684; BAD70684; BAD70684.
GeneIDi3170121.
KEGGittj:TTHA0861.
PATRICi23956704. VBITheThe93045_0855.

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: BAD70684.1.
X83598 Genomic DNA. Translation: CAA58577.1.
PIRiS51053.
RefSeqiWP_011172954.1. NC_006461.1.
YP_144127.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00B1-256[»]
1HNWX-ray3.40B1-256[»]
1HNXX-ray3.40B1-256[»]
1HNZX-ray3.30B1-256[»]
1HR0X-ray3.20B1-256[»]
1I94X-ray3.20B2-256[»]
1I95X-ray4.50B2-256[»]
1I96X-ray4.20B2-256[»]
1I97X-ray4.50B2-256[»]
1IBKX-ray3.31B1-256[»]
1IBLX-ray3.11B1-256[»]
1IBMX-ray3.31B1-256[»]
1J5EX-ray3.05B1-256[»]
1JGOX-ray5.60E1-256[»]
1JGPX-ray7.00E1-256[»]
1JGQX-ray5.00E1-256[»]
1L1Umodel-B7-240[»]
1ML5electron microscopy14.00E1-256[»]
1N32X-ray3.00B1-256[»]
1N33X-ray3.35B1-256[»]
1N34X-ray3.80B1-256[»]
1N36X-ray3.65B1-256[»]
1VVJX-ray3.44QB/XB1-256[»]
1VY4X-ray2.60AB/CB1-256[»]
1VY5X-ray2.55AB/CB1-256[»]
1VY6X-ray2.90AB/CB1-256[»]
1VY7X-ray2.80AB/CB1-256[»]
1X18electron microscopy13.50E7-240[»]
1XMOX-ray3.25B1-256[»]
1XMQX-ray3.00B1-256[»]
1XNQX-ray3.05B1-256[»]
1XNRX-ray3.10B1-256[»]
2E5LX-ray3.30B2-228[»]
2F4VX-ray3.80B1-256[»]
2HHHX-ray3.35B1-256[»]
2OM7electron microscopy7.30N1-256[»]
2UU9X-ray3.10B2-256[»]
2UUAX-ray2.90B2-256[»]
2UUBX-ray2.80B2-256[»]
2UUCX-ray3.10B2-256[»]
2UXBX-ray3.10B2-256[»]
2UXCX-ray2.90B2-256[»]
2UXDX-ray3.20B2-256[»]
2VQEX-ray2.50B1-256[»]
2VQFX-ray2.90B1-256[»]
2ZM6X-ray3.30B2-256[»]
3OTOX-ray3.69B1-256[»]
3T1HX-ray3.11B1-256[»]
3T1YX-ray2.80B1-256[»]
4AQYX-ray3.50B1-256[»]
4B3MX-ray2.90B1-256[»]
4B3RX-ray3.00B1-256[»]
4B3SX-ray3.15B1-256[»]
4B3TX-ray3.00B1-256[»]
4DR1X-ray3.60B1-256[»]
4DR2X-ray3.25B1-256[»]
4DR3X-ray3.35B1-256[»]
4DR4X-ray3.97B1-256[»]
4DR5X-ray3.45B1-256[»]
4DR6X-ray3.30B1-256[»]
4DR7X-ray3.75B1-256[»]
4DUYX-ray3.39B1-256[»]
4DUZX-ray3.65B1-256[»]
4DV0X-ray3.85B1-256[»]
4DV1X-ray3.85B1-256[»]
4DV2X-ray3.65B1-256[»]
4DV3X-ray3.55B1-256[»]
4DV4X-ray3.65B1-256[»]
4DV5X-ray3.68B1-256[»]
4DV6X-ray3.30B1-256[»]
4DV7X-ray3.29B1-256[»]
4GKJX-ray3.30B7-240[»]
4GKKX-ray3.20B7-240[»]
4JI0X-ray3.49B1-256[»]
4JI1X-ray3.14B1-256[»]
4JI2X-ray3.64B1-256[»]
4JI3X-ray3.35B1-256[»]
4JI4X-ray3.69B1-256[»]
4JI5X-ray3.85B1-256[»]
4JI6X-ray3.55B1-256[»]
4JI7X-ray3.50B1-256[»]
4JI8X-ray3.74B1-256[»]
4JV5X-ray3.16B7-240[»]
4JYAX-ray3.10B7-240[»]
4K0KX-ray3.40B7-241[»]
4KHPX-ray3.10B7-240[»]
4L47X-ray3.22QB/XB1-256[»]
4L71X-ray3.90QB/XB1-256[»]
4LELX-ray3.90QB/XB1-256[»]
4LF4X-ray3.34B1-256[»]
4LF5X-ray3.75B1-256[»]
4LF6X-ray3.31B1-256[»]
4LF7X-ray3.15B1-256[»]
4LF8X-ray3.15B1-256[»]
4LF9X-ray3.28B1-256[»]
4LFAX-ray3.65B1-256[»]
4LFBX-ray3.01B1-256[»]
4LFCX-ray3.60B1-256[»]
4LFZX-ray3.92QB/XB1-256[»]
4LNTX-ray2.94QB/XB1-256[»]
4LSKX-ray3.48QB/XB1-256[»]
4LT8X-ray3.14QB/XB1-256[»]
4NXMX-ray3.65B1-256[»]
4NXNX-ray3.54B1-256[»]
4OX9X-ray3.80B1-256[»]
4P6FX-ray3.60QB/XB1-256[»]
4P70X-ray3.68QB/XB1-256[»]
4TUAX-ray3.60QB/XB1-256[»]
4TUBX-ray3.60QB/XB1-256[»]
4TUCX-ray3.60QB/XB1-256[»]
4TUDX-ray3.60QB/XB1-256[»]
4TUEX-ray3.50QB/XB1-256[»]
4V42X-ray5.50AE1-256[»]
4V49X-ray8.70B7-240[»]
4V4AX-ray9.50B7-240[»]
4V4PX-ray5.50BE1-256[»]
4V4RX-ray5.90AB1-256[»]
4V4SX-ray6.76AB1-256[»]
4V4TX-ray6.46AB1-256[»]
4V4XX-ray5.00AE1-256[»]
4V4YX-ray5.50AE1-256[»]
4V4ZX-ray4.51AE1-256[»]
4V51X-ray2.80AB/CB2-256[»]
4V5AX-ray3.50AB/CB2-256[»]
4V5CX-ray3.30AB/CB1-256[»]
4V5DX-ray3.50AB/CB1-256[»]
4V5EX-ray3.45AB/CB1-256[»]
4V5FX-ray3.60AB/CB1-256[»]
4V5GX-ray3.60AB/CB1-256[»]
4V5JX-ray3.10AB/CB1-256[»]
4V5KX-ray3.20AB/CB1-256[»]
4V5LX-ray3.10AB1-256[»]
4V5Melectron microscopy7.80AB1-256[»]
4V5Nelectron microscopy7.60AB1-256[»]
4V5PX-ray3.10AB/CB1-256[»]
4V5QX-ray3.10AB/CB1-256[»]
4V5RX-ray3.10AB/CB1-256[»]
4V5SX-ray3.10AB/CB1-256[»]
4V68electron microscopy6.40AB7-241[»]
4V6AX-ray3.10AB/CB1-256[»]
4V6FX-ray3.10BE/CE1-256[»]
4V6GX-ray3.50AE/CE1-256[»]
4V7JX-ray3.30Ab/Bb1-256[»]
4V7KX-ray3.60Ab/Bb1-256[»]
4V7LX-ray3.00AB/CB1-256[»]
4V7MX-ray3.45AB/CB1-256[»]
4V7WX-ray3.00AB/CB1-256[»]
4V7XX-ray3.00AB/CB1-256[»]
4V7YX-ray3.00AB/CB1-256[»]
4V7ZX-ray3.10AB/CB1-256[»]
4V87X-ray3.10BE/CE1-256[»]
4V8AX-ray3.20CB/DB1-256[»]
4V8BX-ray3.00AE/CE1-256[»]
4V8CX-ray3.30CE/DE1-256[»]
4V8DX-ray3.00AE/CE1-256[»]
4V8EX-ray3.30BE/DE1-256[»]
4V8FX-ray3.30BE/CE1-256[»]
4V8GX-ray3.00AB/CB1-256[»]
4V8HX-ray3.10AB/CB1-256[»]
4V8IX-ray2.70AB/CB1-256[»]
4V8JX-ray3.90AB/CB1-256[»]
4V8NX-ray3.10AB/CB1-256[»]
4V8OX-ray3.80AB1-256[»]
4V8QX-ray3.10BB1-256[»]
4V8UX-ray3.70AB/CB1-256[»]
4V8XX-ray3.35AB/CB1-256[»]
4V90X-ray2.95AB1-256[»]
4V95X-ray3.20AB/CB1-256[»]
4V97X-ray3.52AB/CB1-256[»]
4V9AX-ray3.30AE/CE1-256[»]
4V9BX-ray3.10AE/CE1-256[»]
4V9HX-ray2.86AB7-240[»]
4V9IX-ray3.30AB/CB7-240[»]
4V9RX-ray3.00AB/CB1-256[»]
4V9SX-ray3.10AB/CB1-256[»]
4W2EX-ray2.90b1-256[»]
4W2FX-ray2.40AB/CB1-256[»]
4W2GX-ray2.55AB/CB1-256[»]
4W2HX-ray2.70AB/CB1-256[»]
4W2IX-ray2.70AB/CB1-256[»]
4WPOX-ray2.80BB/DB1-256[»]
4WQFX-ray2.80BB/DB1-256[»]
4WQUX-ray2.80BB/DB1-256[»]
4WQYX-ray2.80BB/DB1-256[»]
4WT8X-ray3.40A7-240[»]
4WUSX-ray3.40A7-240[»]
4Y4OX-ray2.301b/2b1-256[»]
4Y4PX-ray2.501b/2b1-256[»]
4YHHX-ray3.42B3-228[»]
ProteinModelPortaliP80371.
SMRiP80371. Positions 2-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70684; BAD70684; BAD70684.
GeneIDi3170121.
KEGGittj:TTHA0861.
PATRICi23956704. VBITheThe93045_0855.

Phylogenomic databases

eggNOGiCOG0052.
HOGENOMiHOG000071892.
KOiK02967.
OMAiLEFAYNI.
OrthoDBiEOG6XWV6P.
PhylomeDBiP80371.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-893-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP80371.

Family and domain databases

HAMAPiMF_00291_B. Ribosomal_S2_B.
InterProiIPR001865. Ribosomal_S2.
IPR005706. Ribosomal_S2_bac/mit/plastid.
IPR018130. Ribosomal_S2_CS.
IPR023591. Ribosomal_S2_flav_dom.
[Graphical view]
PANTHERiPTHR12534. PTHR12534. 1 hit.
PfamiPF00318. Ribosomal_S2. 1 hit.
[Graphical view]
PRINTSiPR00395. RIBOSOMALS2.
SUPFAMiSSF52313. SSF52313. 1 hit.
TIGRFAMsiTIGR01011. rpsB_bact. 1 hit.
PROSITEiPS00962. RIBOSOMAL_S2_1. 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. "Elongation factor Ts from Thermus thermophilus -- overproduction in Escherichia coli, quaternary structure and interaction with elongation factor Tu."
    Blank J., Nock S., Kreutzer R., Sprinzl M.
    Eur. J. Biochem. 236:222-227(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-256.
  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. "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.
  9. "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.
  10. "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.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
  12. "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.
  13. "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.
  14. "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 nameiRS2_THET8
AccessioniPrimary (citable) accession number: P80371
Secondary accession number(s): Q5SJZ1, Q9ACK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 144 of the entry and version 4 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.