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P80373

- RS4_THET8

UniProt

P80373 - RS4_THET8

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Protein

30S ribosomal protein S4

Gene

rpsD

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the body and platform of the 30S subunit. Binds mRNA in the 70S ribosome, positioning it for translation.

Cofactori

Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91ZincCurated
Metal bindingi12 – 121ZincCurated
Metal bindingi26 – 261ZincCurated
Metal bindingi31 – 311ZincCurated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 3123C4-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. rRNA binding Source: UniProtKB-HAMAP
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, RNA-binding, rRNA-binding, Zinc

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1704-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S4
Gene namesi
Name:rpsD
Synonyms:rps4
Ordered Locus Names:TTHA1665
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: 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 – 20920830S ribosomal protein S4PRO_0000132483Add
BLAST

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity.

Protein-protein interaction databases

STRINGi300852.TTHA1665.

Structurei

Secondary structure

1
209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 157
Beta strandi21 – 233
Beta strandi26 – 283
Helixi33 – 353
Turni42 – 454
Helixi53 – 6816
Helixi72 – 8413
Beta strandi85 – 873
Helixi89 – 9810
Helixi101 – 1077
Beta strandi110 – 1134
Helixi114 – 1229
Turni123 – 1253
Beta strandi126 – 1283
Beta strandi129 – 1313
Beta strandi145 – 1484
Helixi150 – 1523
Beta strandi153 – 1553
Helixi156 – 1649
Turni165 – 1673
Beta strandi174 – 1763
Turni178 – 1814
Beta strandi182 – 1843
Helixi191 – 1933
Helixi200 – 2067

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00D1-209[»]
1FKAX-ray3.30D1-209[»]
1GIXX-ray5.50G1-209[»]
1HNWX-ray3.40D1-209[»]
1HNXX-ray3.40D1-209[»]
1HNZX-ray3.30D1-209[»]
1HR0X-ray3.20D1-209[»]
1I94X-ray3.20D2-209[»]
1I95X-ray4.50D2-209[»]
1I96X-ray4.20D2-209[»]
1I97X-ray4.50D2-209[»]
1IBKX-ray3.31D1-209[»]
1IBLX-ray3.11D1-209[»]
1IBMX-ray3.31D1-209[»]
1J5EX-ray3.05D2-209[»]
1JGOX-ray5.60G1-209[»]
1JGPX-ray7.00G1-209[»]
1JGQX-ray5.00G1-209[»]
1L1Umodel-D1-209[»]
1ML5electron microscopy14.00G1-209[»]
1N32X-ray3.00D2-209[»]
1N33X-ray3.35D2-209[»]
1N34X-ray3.80D2-209[»]
1N36X-ray3.65D2-209[»]
1PNSX-ray8.70D2-209[»]
1PNXX-ray9.50D2-209[»]
1QD7X-ray5.50C60-155[»]
1TWTmodel-G2-209[»]
1VVLX-ray3.22D1-209[»]
1VVNX-ray3.22D1-209[»]
1VVPX-ray3.90D1-209[»]
1VVRX-ray3.90D1-209[»]
1VVTX-ray3.90D1-209[»]
1VVVX-ray3.90D1-209[»]
1VVXX-ray3.92D1-209[»]
1VVZX-ray3.92D1-209[»]
1VX8X-ray2.94D1-209[»]
1VXIX-ray2.94D1-209[»]
1VXKX-ray3.48D1-209[»]
1VXMX-ray3.48D1-209[»]
1VXPX-ray3.14D1-209[»]
1VXSX-ray3.14D1-209[»]
1VY0X-ray3.68D1-209[»]
1VY2X-ray3.68D1-209[»]
1XMOX-ray3.25D1-209[»]
1XMQX-ray3.00D1-209[»]
1XNQX-ray3.05D1-209[»]
1XNRX-ray3.10D1-209[»]
1YL4X-ray5.50G1-209[»]
2B64X-ray5.90D1-209[»]
2B9MX-ray6.76D1-209[»]
2B9OX-ray6.46D1-209[»]
2E5LX-ray3.30D2-209[»]
2F4VX-ray3.80D1-209[»]
2HGIX-ray5.00G1-209[»]
2HGPX-ray5.50G1-209[»]
2HGRX-ray4.51G1-209[»]
2HHHX-ray3.35D1-209[»]
2J00X-ray2.80D2-209[»]
2J02X-ray2.80D2-209[»]
2OW8X-ray3.71e1-209[»]
2UU9X-ray3.10D2-209[»]
2UUAX-ray2.90D2-209[»]
2UUBX-ray2.80D2-209[»]
2UUCX-ray3.10D2-209[»]
2UXBX-ray3.10D2-209[»]
2UXCX-ray2.90D2-209[»]
2UXDX-ray3.20D2-209[»]
2V46X-ray3.50D2-209[»]
2V48X-ray3.50D2-209[»]
2VQEX-ray2.50D1-209[»]
2VQFX-ray2.90D1-209[»]
2WDGX-ray3.30D1-209[»]
2WDHX-ray3.30D1-209[»]
2WDKX-ray3.50D1-209[»]
2WDMX-ray3.50D1-209[»]
2WH1X-ray3.45D1-209[»]
2WH3X-ray3.45D1-209[»]
2WRIX-ray3.60D1-209[»]
2WRKX-ray3.60D1-209[»]
2WRNX-ray3.60D1-209[»]
2WRQX-ray3.60D1-209[»]
2X9RX-ray3.10D1-209[»]
2X9TX-ray3.10D1-209[»]
2XFZX-ray3.20D1-209[»]
2XG1X-ray3.20D1-209[»]
2XQDX-ray3.10D1-209[»]
2XSYelectron microscopy7.80D1-209[»]
2XUYelectron microscopy7.60D1-209[»]
2Y0UX-ray3.10D1-209[»]
2Y0WX-ray3.10D1-209[»]
2Y0YX-ray3.10D1-209[»]
2Y10X-ray3.10D1-209[»]
2Y12X-ray3.10D1-209[»]
2Y14X-ray3.10D1-209[»]
2Y16X-ray3.10D1-209[»]
2Y18X-ray3.10D1-209[»]
2ZKQelectron microscopy8.70d1-209[»]
2ZM6X-ray3.30D2-209[»]
3FICelectron microscopy6.40D2-209[»]
3HUWX-ray3.10D1-209[»]
3HUYX-ray3.10D1-209[»]
3I8GX-ray3.10G1-209[»]
3I8HX-ray3.10G1-209[»]
3I9BX-ray3.50G1-209[»]
3I9DX-ray3.50G1-209[»]
3KIQX-ray3.30d1-209[»]
3KISX-ray3.30d1-209[»]
3KIUX-ray3.60d1-209[»]
3KIXX-ray3.60d1-209[»]
3KNHX-ray3.00D1-209[»]
3KNJX-ray3.15D1-209[»]
3KNLX-ray3.45D1-209[»]
3KNNX-ray3.45D1-209[»]
3OGEX-ray3.00D1-209[»]
3OGYX-ray3.00D1-209[»]
3OHCX-ray3.00D1-209[»]
3OHDX-ray3.00D1-209[»]
3OHYX-ray3.00D1-209[»]
3OI0X-ray3.00D1-209[»]
3OI2X-ray3.10D1-209[»]
3OI4X-ray3.10D1-209[»]
3OTOX-ray3.69D1-209[»]
3T1HX-ray3.11D1-209[»]
3T1YX-ray2.80D1-209[»]
3TVFX-ray3.10G2-209[»]
3TVGX-ray3.10G2-209[»]
3UXSX-ray3.20D1-209[»]
3UXTX-ray3.20D1-209[»]
3UYDX-ray3.00G2-209[»]
3UYFX-ray3.00G2-209[»]
3UZ3X-ray3.30G2-209[»]
3UZ4X-ray3.30G2-209[»]
3UZ6X-ray3.00G2-209[»]
3UZ7X-ray3.00G2-209[»]
3UZGX-ray3.30G2-209[»]
3UZIX-ray3.30G2-209[»]
3UZLX-ray3.30G2-209[»]
3UZMX-ray3.30G2-209[»]
3V22X-ray3.00D1-209[»]
3V24X-ray3.00D1-209[»]
3V26X-ray3.10D1-209[»]
3V28X-ray3.10D1-209[»]
3V2CX-ray2.70D1-209[»]
3V2EX-ray2.70D1-209[»]
3V6UX-ray3.90D1-209[»]
3V6VX-ray3.90D1-209[»]
3ZN7X-ray3.10D1-209[»]
3ZNDX-ray3.10D1-209[»]
3ZVOX-ray3.80D1-209[»]
4ABRX-ray3.10D1-209[»]
4AQYX-ray3.50D2-209[»]
4B3MX-ray2.90D2-209[»]
4B3RX-ray3.00D2-209[»]
4B3SX-ray3.15D2-209[»]
4B3TX-ray3.00D2-209[»]
4B8FX-ray3.70D1-209[»]
4B8HX-ray3.70D1-209[»]
4BYBX-ray3.35D1-209[»]
4BYDX-ray3.35D1-209[»]
4CR1X-ray2.95D1-209[»]
4DH9X-ray3.20D1-209[»]
4DHBX-ray3.20D1-209[»]
4DR1X-ray3.60D1-209[»]
4DR2X-ray3.25D1-209[»]
4DR3X-ray3.35D1-209[»]
4DR4X-ray3.97D1-209[»]
4DR5X-ray3.45D1-209[»]
4DR6X-ray3.30D1-209[»]
4DR7X-ray3.75D1-209[»]
4DUYX-ray3.39D1-209[»]
4DUZX-ray3.65D1-209[»]
4DV0X-ray3.85D1-209[»]
4DV1X-ray3.85D1-209[»]
4DV2X-ray3.65D1-209[»]
4DV3X-ray3.55D1-209[»]
4DV4X-ray3.65D1-209[»]
4DV5X-ray3.68D1-209[»]
4DV6X-ray3.30D1-209[»]
4DV7X-ray3.29D1-209[»]
4EJ9X-ray3.52D1-209[»]
4EJAX-ray3.52D1-209[»]
4G5KX-ray3.30G2-209[»]
4G5MX-ray3.30G2-209[»]
4G5TX-ray3.10G2-209[»]
4G5VX-ray3.10G2-209[»]
4GKJX-ray3.30D2-209[»]
4GKKX-ray3.20D2-209[»]
4JI0X-ray3.49D1-209[»]
4JI1X-ray3.14D1-209[»]
4JI2X-ray3.64D1-209[»]
4JI3X-ray3.35D1-209[»]
4JI4X-ray3.69D1-209[»]
4JI5X-ray3.85D1-209[»]
4JI6X-ray3.55D1-209[»]
4JI7X-ray3.50D1-209[»]
4JI8X-ray3.74D1-209[»]
4JUWX-ray2.86D2-209[»]
4JV5X-ray3.16D2-209[»]
4JYAX-ray3.10D2-209[»]
4K0KX-ray3.40D2-209[»]
4K0LX-ray3.30D2-209[»]
4K0PX-ray3.30D2-209[»]
4KHPX-ray3.10D2-209[»]
4KWZX-ray3.44D1-209[»]
4KX1X-ray3.44D1-209[»]
4LF4X-ray3.34D1-209[»]
4LF5X-ray3.75D1-209[»]
4LF6X-ray3.31D1-209[»]
4LF7X-ray3.15D1-209[»]
4LF8X-ray3.15D1-209[»]
4LF9X-ray3.28D1-209[»]
4LFAX-ray3.65D1-209[»]
4LFBX-ray3.01D1-209[»]
4LFCX-ray3.60D1-209[»]
4NVUX-ray3.00D1-209[»]
4NVWX-ray3.00D1-209[»]
4NVYX-ray3.10D1-209[»]
4NW0X-ray3.10D1-209[»]
4NXMX-ray3.65D1-209[»]
4NXNX-ray3.54D1-209[»]
4OX9X-ray3.80D2-209[»]
4QCMX-ray2.60D1-209[»]
4QCOX-ray2.60D1-209[»]
4QCQX-ray2.55D1-209[»]
4QCSX-ray2.55D1-209[»]
4QCUX-ray2.90D1-209[»]
4QCWX-ray2.90D1-209[»]
4QCYX-ray2.80D1-209[»]
4QD0X-ray2.80D1-209[»]
ProteinModelPortaliP80373.
SMRiP80373. Positions 2-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80373.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 16163S4 RNA-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S4P family.Curated
Contains 1 S4 RNA-binding domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri9 – 3123C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG0522.
HOGENOMiHOG000221004.
KOiK02986.
OMAiTCKLSRR.
OrthoDBiEOG6N3CXM.
PhylomeDBiP80373.

Family and domain databases

Gene3Di1.10.1050.10. 1 hit.
3.10.290.10. 1 hit.
HAMAPiMF_01306_B. Ribosomal_S4_B.
InterProiIPR022801. Ribosomal_S4/S9.
IPR001912. Ribosomal_S4/S9_N.
IPR005709. Ribosomal_S4_bac-type.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01017. rpsD_bact. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P80373-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRYIGPVCR LCRREGVKLY LKGERCYSPK CAMERRPYPP GQHGQKRARR
60 70 80 90 100
PSDYAVRLRE KQKLRRIYGI SERQFRNLFE EASKKKGVTG SVFLGLLESR
110 120 130 140 150
LDNVVYRLGF AVSRRQARQL VRHGHITVNG RRVDLPSYRV RPGDEIAVAE
160 170 180 190 200
KSRNLELIRQ NLEAMKGRKV GPWLSLDVEG MKGKFLRLPD REDLALPVNE

QLVIEFYSR
Length:209
Mass (Da):24,324
Last modified:January 23, 2007 - v3
Checksum:i0FF3911816971236
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121C → S AA sequence (PubMed:7957245)Curated
Sequence conflicti26 – 261C → D AA sequence (PubMed:7957245)Curated

Mass spectrometryi

Molecular mass is 24192 Da from positions 2 - 209. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB024328 Genomic DNA. Translation: BAA75548.1.
AP008226 Genomic DNA. Translation: BAD71488.1.
RefSeqiWP_011173699.1. NC_006461.1.
YP_144931.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71488; BAD71488; BAD71488.
GeneIDi3168006.
KEGGittj:TTHA1665.
PATRICi23958285. VBITheThe93045_1635.

Cross-referencesi

Web resourcesi

T.thermophilus ribosome structure and function

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB024328 Genomic DNA. Translation: BAA75548.1 .
AP008226 Genomic DNA. Translation: BAD71488.1 .
RefSeqi WP_011173699.1. NC_006461.1.
YP_144931.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FJG X-ray 3.00 D 1-209 [» ]
1FKA X-ray 3.30 D 1-209 [» ]
1GIX X-ray 5.50 G 1-209 [» ]
1HNW X-ray 3.40 D 1-209 [» ]
1HNX X-ray 3.40 D 1-209 [» ]
1HNZ X-ray 3.30 D 1-209 [» ]
1HR0 X-ray 3.20 D 1-209 [» ]
1I94 X-ray 3.20 D 2-209 [» ]
1I95 X-ray 4.50 D 2-209 [» ]
1I96 X-ray 4.20 D 2-209 [» ]
1I97 X-ray 4.50 D 2-209 [» ]
1IBK X-ray 3.31 D 1-209 [» ]
1IBL X-ray 3.11 D 1-209 [» ]
1IBM X-ray 3.31 D 1-209 [» ]
1J5E X-ray 3.05 D 2-209 [» ]
1JGO X-ray 5.60 G 1-209 [» ]
1JGP X-ray 7.00 G 1-209 [» ]
1JGQ X-ray 5.00 G 1-209 [» ]
1L1U model - D 1-209 [» ]
1ML5 electron microscopy 14.00 G 1-209 [» ]
1N32 X-ray 3.00 D 2-209 [» ]
1N33 X-ray 3.35 D 2-209 [» ]
1N34 X-ray 3.80 D 2-209 [» ]
1N36 X-ray 3.65 D 2-209 [» ]
1PNS X-ray 8.70 D 2-209 [» ]
1PNX X-ray 9.50 D 2-209 [» ]
1QD7 X-ray 5.50 C 60-155 [» ]
1TWT model - G 2-209 [» ]
1VVL X-ray 3.22 D 1-209 [» ]
1VVN X-ray 3.22 D 1-209 [» ]
1VVP X-ray 3.90 D 1-209 [» ]
1VVR X-ray 3.90 D 1-209 [» ]
1VVT X-ray 3.90 D 1-209 [» ]
1VVV X-ray 3.90 D 1-209 [» ]
1VVX X-ray 3.92 D 1-209 [» ]
1VVZ X-ray 3.92 D 1-209 [» ]
1VX8 X-ray 2.94 D 1-209 [» ]
1VXI X-ray 2.94 D 1-209 [» ]
1VXK X-ray 3.48 D 1-209 [» ]
1VXM X-ray 3.48 D 1-209 [» ]
1VXP X-ray 3.14 D 1-209 [» ]
1VXS X-ray 3.14 D 1-209 [» ]
1VY0 X-ray 3.68 D 1-209 [» ]
1VY2 X-ray 3.68 D 1-209 [» ]
1XMO X-ray 3.25 D 1-209 [» ]
1XMQ X-ray 3.00 D 1-209 [» ]
1XNQ X-ray 3.05 D 1-209 [» ]
1XNR X-ray 3.10 D 1-209 [» ]
1YL4 X-ray 5.50 G 1-209 [» ]
2B64 X-ray 5.90 D 1-209 [» ]
2B9M X-ray 6.76 D 1-209 [» ]
2B9O X-ray 6.46 D 1-209 [» ]
2E5L X-ray 3.30 D 2-209 [» ]
2F4V X-ray 3.80 D 1-209 [» ]
2HGI X-ray 5.00 G 1-209 [» ]
2HGP X-ray 5.50 G 1-209 [» ]
2HGR X-ray 4.51 G 1-209 [» ]
2HHH X-ray 3.35 D 1-209 [» ]
2J00 X-ray 2.80 D 2-209 [» ]
2J02 X-ray 2.80 D 2-209 [» ]
2OW8 X-ray 3.71 e 1-209 [» ]
2UU9 X-ray 3.10 D 2-209 [» ]
2UUA X-ray 2.90 D 2-209 [» ]
2UUB X-ray 2.80 D 2-209 [» ]
2UUC X-ray 3.10 D 2-209 [» ]
2UXB X-ray 3.10 D 2-209 [» ]
2UXC X-ray 2.90 D 2-209 [» ]
2UXD X-ray 3.20 D 2-209 [» ]
2V46 X-ray 3.50 D 2-209 [» ]
2V48 X-ray 3.50 D 2-209 [» ]
2VQE X-ray 2.50 D 1-209 [» ]
2VQF X-ray 2.90 D 1-209 [» ]
2WDG X-ray 3.30 D 1-209 [» ]
2WDH X-ray 3.30 D 1-209 [» ]
2WDK X-ray 3.50 D 1-209 [» ]
2WDM X-ray 3.50 D 1-209 [» ]
2WH1 X-ray 3.45 D 1-209 [» ]
2WH3 X-ray 3.45 D 1-209 [» ]
2WRI X-ray 3.60 D 1-209 [» ]
2WRK X-ray 3.60 D 1-209 [» ]
2WRN X-ray 3.60 D 1-209 [» ]
2WRQ X-ray 3.60 D 1-209 [» ]
2X9R X-ray 3.10 D 1-209 [» ]
2X9T X-ray 3.10 D 1-209 [» ]
2XFZ X-ray 3.20 D 1-209 [» ]
2XG1 X-ray 3.20 D 1-209 [» ]
2XQD X-ray 3.10 D 1-209 [» ]
2XSY electron microscopy 7.80 D 1-209 [» ]
2XUY electron microscopy 7.60 D 1-209 [» ]
2Y0U X-ray 3.10 D 1-209 [» ]
2Y0W X-ray 3.10 D 1-209 [» ]
2Y0Y X-ray 3.10 D 1-209 [» ]
2Y10 X-ray 3.10 D 1-209 [» ]
2Y12 X-ray 3.10 D 1-209 [» ]
2Y14 X-ray 3.10 D 1-209 [» ]
2Y16 X-ray 3.10 D 1-209 [» ]
2Y18 X-ray 3.10 D 1-209 [» ]
2ZKQ electron microscopy 8.70 d 1-209 [» ]
2ZM6 X-ray 3.30 D 2-209 [» ]
3FIC electron microscopy 6.40 D 2-209 [» ]
3HUW X-ray 3.10 D 1-209 [» ]
3HUY X-ray 3.10 D 1-209 [» ]
3I8G X-ray 3.10 G 1-209 [» ]
3I8H X-ray 3.10 G 1-209 [» ]
3I9B X-ray 3.50 G 1-209 [» ]
3I9D X-ray 3.50 G 1-209 [» ]
3KIQ X-ray 3.30 d 1-209 [» ]
3KIS X-ray 3.30 d 1-209 [» ]
3KIU X-ray 3.60 d 1-209 [» ]
3KIX X-ray 3.60 d 1-209 [» ]
3KNH X-ray 3.00 D 1-209 [» ]
3KNJ X-ray 3.15 D 1-209 [» ]
3KNL X-ray 3.45 D 1-209 [» ]
3KNN X-ray 3.45 D 1-209 [» ]
3OGE X-ray 3.00 D 1-209 [» ]
3OGY X-ray 3.00 D 1-209 [» ]
3OHC X-ray 3.00 D 1-209 [» ]
3OHD X-ray 3.00 D 1-209 [» ]
3OHY X-ray 3.00 D 1-209 [» ]
3OI0 X-ray 3.00 D 1-209 [» ]
3OI2 X-ray 3.10 D 1-209 [» ]
3OI4 X-ray 3.10 D 1-209 [» ]
3OTO X-ray 3.69 D 1-209 [» ]
3T1H X-ray 3.11 D 1-209 [» ]
3T1Y X-ray 2.80 D 1-209 [» ]
3TVF X-ray 3.10 G 2-209 [» ]
3TVG X-ray 3.10 G 2-209 [» ]
3UXS X-ray 3.20 D 1-209 [» ]
3UXT X-ray 3.20 D 1-209 [» ]
3UYD X-ray 3.00 G 2-209 [» ]
3UYF X-ray 3.00 G 2-209 [» ]
3UZ3 X-ray 3.30 G 2-209 [» ]
3UZ4 X-ray 3.30 G 2-209 [» ]
3UZ6 X-ray 3.00 G 2-209 [» ]
3UZ7 X-ray 3.00 G 2-209 [» ]
3UZG X-ray 3.30 G 2-209 [» ]
3UZI X-ray 3.30 G 2-209 [» ]
3UZL X-ray 3.30 G 2-209 [» ]
3UZM X-ray 3.30 G 2-209 [» ]
3V22 X-ray 3.00 D 1-209 [» ]
3V24 X-ray 3.00 D 1-209 [» ]
3V26 X-ray 3.10 D 1-209 [» ]
3V28 X-ray 3.10 D 1-209 [» ]
3V2C X-ray 2.70 D 1-209 [» ]
3V2E X-ray 2.70 D 1-209 [» ]
3V6U X-ray 3.90 D 1-209 [» ]
3V6V X-ray 3.90 D 1-209 [» ]
3ZN7 X-ray 3.10 D 1-209 [» ]
3ZND X-ray 3.10 D 1-209 [» ]
3ZVO X-ray 3.80 D 1-209 [» ]
4ABR X-ray 3.10 D 1-209 [» ]
4AQY X-ray 3.50 D 2-209 [» ]
4B3M X-ray 2.90 D 2-209 [» ]
4B3R X-ray 3.00 D 2-209 [» ]
4B3S X-ray 3.15 D 2-209 [» ]
4B3T X-ray 3.00 D 2-209 [» ]
4B8F X-ray 3.70 D 1-209 [» ]
4B8H X-ray 3.70 D 1-209 [» ]
4BYB X-ray 3.35 D 1-209 [» ]
4BYD X-ray 3.35 D 1-209 [» ]
4CR1 X-ray 2.95 D 1-209 [» ]
4DH9 X-ray 3.20 D 1-209 [» ]
4DHB X-ray 3.20 D 1-209 [» ]
4DR1 X-ray 3.60 D 1-209 [» ]
4DR2 X-ray 3.25 D 1-209 [» ]
4DR3 X-ray 3.35 D 1-209 [» ]
4DR4 X-ray 3.97 D 1-209 [» ]
4DR5 X-ray 3.45 D 1-209 [» ]
4DR6 X-ray 3.30 D 1-209 [» ]
4DR7 X-ray 3.75 D 1-209 [» ]
4DUY X-ray 3.39 D 1-209 [» ]
4DUZ X-ray 3.65 D 1-209 [» ]
4DV0 X-ray 3.85 D 1-209 [» ]
4DV1 X-ray 3.85 D 1-209 [» ]
4DV2 X-ray 3.65 D 1-209 [» ]
4DV3 X-ray 3.55 D 1-209 [» ]
4DV4 X-ray 3.65 D 1-209 [» ]
4DV5 X-ray 3.68 D 1-209 [» ]
4DV6 X-ray 3.30 D 1-209 [» ]
4DV7 X-ray 3.29 D 1-209 [» ]
4EJ9 X-ray 3.52 D 1-209 [» ]
4EJA X-ray 3.52 D 1-209 [» ]
4G5K X-ray 3.30 G 2-209 [» ]
4G5M X-ray 3.30 G 2-209 [» ]
4G5T X-ray 3.10 G 2-209 [» ]
4G5V X-ray 3.10 G 2-209 [» ]
4GKJ X-ray 3.30 D 2-209 [» ]
4GKK X-ray 3.20 D 2-209 [» ]
4JI0 X-ray 3.49 D 1-209 [» ]
4JI1 X-ray 3.14 D 1-209 [» ]
4JI2 X-ray 3.64 D 1-209 [» ]
4JI3 X-ray 3.35 D 1-209 [» ]
4JI4 X-ray 3.69 D 1-209 [» ]
4JI5 X-ray 3.85 D 1-209 [» ]
4JI6 X-ray 3.55 D 1-209 [» ]
4JI7 X-ray 3.50 D 1-209 [» ]
4JI8 X-ray 3.74 D 1-209 [» ]
4JUW X-ray 2.86 D 2-209 [» ]
4JV5 X-ray 3.16 D 2-209 [» ]
4JYA X-ray 3.10 D 2-209 [» ]
4K0K X-ray 3.40 D 2-209 [» ]
4K0L X-ray 3.30 D 2-209 [» ]
4K0P X-ray 3.30 D 2-209 [» ]
4KHP X-ray 3.10 D 2-209 [» ]
4KWZ X-ray 3.44 D 1-209 [» ]
4KX1 X-ray 3.44 D 1-209 [» ]
4LF4 X-ray 3.34 D 1-209 [» ]
4LF5 X-ray 3.75 D 1-209 [» ]
4LF6 X-ray 3.31 D 1-209 [» ]
4LF7 X-ray 3.15 D 1-209 [» ]
4LF8 X-ray 3.15 D 1-209 [» ]
4LF9 X-ray 3.28 D 1-209 [» ]
4LFA X-ray 3.65 D 1-209 [» ]
4LFB X-ray 3.01 D 1-209 [» ]
4LFC X-ray 3.60 D 1-209 [» ]
4NVU X-ray 3.00 D 1-209 [» ]
4NVW X-ray 3.00 D 1-209 [» ]
4NVY X-ray 3.10 D 1-209 [» ]
4NW0 X-ray 3.10 D 1-209 [» ]
4NXM X-ray 3.65 D 1-209 [» ]
4NXN X-ray 3.54 D 1-209 [» ]
4OX9 X-ray 3.80 D 2-209 [» ]
4QCM X-ray 2.60 D 1-209 [» ]
4QCO X-ray 2.60 D 1-209 [» ]
4QCQ X-ray 2.55 D 1-209 [» ]
4QCS X-ray 2.55 D 1-209 [» ]
4QCU X-ray 2.90 D 1-209 [» ]
4QCW X-ray 2.90 D 1-209 [» ]
4QCY X-ray 2.80 D 1-209 [» ]
4QD0 X-ray 2.80 D 1-209 [» ]
ProteinModelPortali P80373.
SMRi P80373. Positions 2-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA1665.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD71488 ; BAD71488 ; BAD71488 .
GeneIDi 3168006.
KEGGi ttj:TTHA1665.
PATRICi 23958285. VBITheThe93045_1635.

Phylogenomic databases

eggNOGi COG0522.
HOGENOMi HOG000221004.
KOi K02986.
OMAi TCKLSRR.
OrthoDBi EOG6N3CXM.
PhylomeDBi P80373.

Enzyme and pathway databases

BioCyci TTHE300852:GH8R-1704-MONOMER.

Miscellaneous databases

EvolutionaryTracei P80373.

Family and domain databases

Gene3Di 1.10.1050.10. 1 hit.
3.10.290.10. 1 hit.
HAMAPi MF_01306_B. Ribosomal_S4_B.
InterProi IPR022801. Ribosomal_S4/S9.
IPR001912. Ribosomal_S4/S9_N.
IPR005709. Ribosomal_S4_bac-type.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view ]
PANTHERi PTHR11831. PTHR11831. 1 hit.
Pfami PF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view ]
SMARTi SM00363. S4. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01017. rpsD_bact. 1 hit.
PROSITEi PS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view ]
ProtoNeti Search...

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 2-27.
  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. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE 30S SUBUNIT.
  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(2000) [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(2000) [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(2000) [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(2001) [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(2001) [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(2001) [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(2001) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.

Entry informationi

Entry nameiRS4_THET8
AccessioniPrimary (citable) accession number: P80373
Secondary accession number(s): Q5SHR5, Q9Z9H7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: October 29, 2014
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