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Protein

30S ribosomal protein S17

Gene

rpsQ

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

One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform and body of the 30S subunit by bringing together and stabilizing interactions between several different RNA helices. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
Deletion of the protein leads to an increased generation time and a temperature-sensitive phenotype.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. 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

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1722-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S17UniRule annotation
Gene namesi
Name:rpsQUniRule annotation
Ordered Locus Names:TTHA1683
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. ribosome Source: UniProtKB-KW
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10510430S ribosomal protein S17PRO_0000128492Add
BLAST

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts protein S12.

Protein-protein interaction databases

STRINGi300852.TTHA1683.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Beta strandi15 – 173Combined sources
Beta strandi18 – 2912Combined sources
Turni30 – 323Combined sources
Beta strandi33 – 4513Combined sources
Beta strandi47 – 493Combined sources
Beta strandi56 – 6611Combined sources
Beta strandi69 – 7810Combined sources
Helixi82 – 9514Combined sources
Beta strandi98 – 1014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00Q1-105[»]
1HNWX-ray3.40Q1-105[»]
1HNXX-ray3.40Q1-105[»]
1HNZX-ray3.30Q1-105[»]
1HR0X-ray3.20Q1-105[»]
1I94X-ray3.20Q2-105[»]
1I95X-ray4.50Q2-105[»]
1I96X-ray4.20Q2-105[»]
1I97X-ray4.50Q2-105[»]
1IBKX-ray3.31Q1-105[»]
1IBLX-ray3.11Q1-105[»]
1IBMX-ray3.31Q1-105[»]
1J5EX-ray3.05Q2-105[»]
1JGOX-ray5.60T1-105[»]
1JGPX-ray7.00T1-105[»]
1JGQX-ray5.00T1-105[»]
1L1Umodel-Q1-105[»]
1ML5electron microscopy14.00T1-105[»]
1N32X-ray3.00Q2-105[»]
1N33X-ray3.35Q2-105[»]
1N34X-ray3.80Q2-105[»]
1N36X-ray3.65Q2-105[»]
1VVJX-ray3.44QQ/XQ1-105[»]
1VY4X-ray2.60AQ/CQ1-105[»]
1VY5X-ray2.55AQ/CQ1-105[»]
1VY6X-ray2.90AQ/CQ1-105[»]
1VY7X-ray2.80AQ/CQ1-105[»]
1XMOX-ray3.25Q1-105[»]
1XMQX-ray3.00Q1-105[»]
1XNQX-ray3.05Q1-105[»]
1XNRX-ray3.10Q1-105[»]
2E5LX-ray3.30Q2-105[»]
2F4VX-ray3.80Q1-105[»]
2HHHX-ray3.35Q1-105[»]
2UU9X-ray3.10Q2-105[»]
2UUAX-ray2.90Q2-105[»]
2UUBX-ray2.80Q2-105[»]
2UUCX-ray3.10Q2-105[»]
2UXBX-ray3.10Q2-105[»]
2UXCX-ray2.90Q2-105[»]
2UXDX-ray3.20Q2-105[»]
2ZM6X-ray3.30Q2-105[»]
3OTOX-ray3.69Q1-105[»]
3T1HX-ray3.11Q1-105[»]
3T1YX-ray2.80Q1-105[»]
4AQYX-ray3.50Q2-105[»]
4B3MX-ray2.90Q2-105[»]
4B3RX-ray3.00Q2-105[»]
4B3SX-ray3.15Q2-105[»]
4B3TX-ray3.00Q2-105[»]
4DR1X-ray3.60Q1-105[»]
4DR2X-ray3.25Q1-105[»]
4DR3X-ray3.35Q1-105[»]
4DR4X-ray3.97Q1-105[»]
4DR5X-ray3.45Q1-105[»]
4DR6X-ray3.30Q1-105[»]
4DR7X-ray3.75Q1-105[»]
4DUYX-ray3.39Q1-105[»]
4DUZX-ray3.65Q1-105[»]
4DV0X-ray3.85Q1-105[»]
4DV1X-ray3.85Q1-105[»]
4DV2X-ray3.65Q1-105[»]
4DV3X-ray3.55Q1-105[»]
4DV4X-ray3.65Q1-105[»]
4DV5X-ray3.68Q1-105[»]
4DV6X-ray3.30Q1-105[»]
4DV7X-ray3.29Q1-105[»]
4GKJX-ray3.30Q2-105[»]
4GKKX-ray3.20Q2-105[»]
4JI0X-ray3.49Q1-105[»]
4JI1X-ray3.14Q1-105[»]
4JI2X-ray3.64Q1-105[»]
4JI3X-ray3.35Q1-105[»]
4JI4X-ray3.69Q1-105[»]
4JI5X-ray3.85Q1-105[»]
4JI6X-ray3.55Q1-105[»]
4JI7X-ray3.50Q1-105[»]
4JI8X-ray3.74Q1-105[»]
4JV5X-ray3.16Q2-100[»]
4JYAX-ray3.10Q2-100[»]
4K0KX-ray3.40Q2-101[»]
4KHPX-ray3.10Q2-100[»]
4L47X-ray3.22QQ/XQ1-105[»]
4L71X-ray3.90QQ/XQ1-105[»]
4LELX-ray3.90QQ/XQ1-105[»]
4LF4X-ray3.34Q1-105[»]
4LF5X-ray3.75Q1-105[»]
4LF6X-ray3.31Q1-105[»]
4LF7X-ray3.15Q1-105[»]
4LF8X-ray3.15Q1-105[»]
4LF9X-ray3.28Q1-105[»]
4LFAX-ray3.65Q1-105[»]
4LFBX-ray3.01Q1-105[»]
4LFCX-ray3.60Q1-105[»]
4LFZX-ray3.92QQ/XQ1-105[»]
4LNTX-ray2.94QQ/XQ1-105[»]
4LSKX-ray3.48QQ/XQ1-105[»]
4LT8X-ray3.14QQ/XQ1-105[»]
4NXMX-ray3.65Q1-105[»]
4NXNX-ray3.54Q1-105[»]
4OX9X-ray3.80Q2-105[»]
4P6FX-ray3.60QQ/XQ1-105[»]
4P70X-ray3.68QQ/XQ1-105[»]
4V42X-ray5.50T1-105[»]
4V49X-ray8.70Q2-105[»]
4V4GX-ray11.50Q2-105[»]
4V4IX-ray3.71r1-105[»]
4V4PX-ray5.50BT1-105[»]
4V4RX-ray5.90Q1-105[»]
4V4SX-ray6.76Q1-105[»]
4V4TX-ray6.46Q1-105[»]
4V4XX-ray5.00T1-105[»]
4V4YX-ray5.50T1-105[»]
4V4ZX-ray4.51T1-105[»]
4V51X-ray2.80AQ/CQ2-105[»]
4V5AX-ray3.50AQ/CQ2-105[»]
4V5CX-ray3.30AQ/CQ1-105[»]
4V5DX-ray3.50AQ/CQ1-105[»]
4V5EX-ray3.45AQ/CQ1-105[»]
4V5FX-ray3.60AQ/CQ1-105[»]
4V5GX-ray3.60AQ/CQ1-105[»]
4V5JX-ray3.10AQ/CQ1-105[»]
4V5KX-ray3.20AQ/CQ1-105[»]
4V5LX-ray3.10AQ1-105[»]
4V5Melectron microscopy7.80AQ1-105[»]
4V5Nelectron microscopy7.60AQ1-105[»]
4V5PX-ray3.10AQ/CQ1-105[»]
4V5QX-ray3.10AQ/CQ1-105[»]
4V5RX-ray3.10AQ/CQ1-105[»]
4V5SX-ray3.10AQ/CQ1-105[»]
4V68electron microscopy6.40AQ2-101[»]
4V6AX-ray3.10AQ/CQ1-105[»]
4V6FX-ray3.10BT/CT1-105[»]
4V6GX-ray3.50AT/CT1-105[»]
4V7JX-ray3.30Aq/Bq1-105[»]
4V7KX-ray3.60Aq/Bq1-105[»]
4V7LX-ray3.00AQ/CQ1-105[»]
4V7MX-ray3.45AQ/CQ1-105[»]
4V7WX-ray3.00AQ/CQ1-105[»]
4V7XX-ray3.00AQ/CQ1-105[»]
4V7YX-ray3.00AQ/CQ1-105[»]
4V7ZX-ray3.10AQ/CQ1-105[»]
4V87X-ray3.10BT/CT1-105[»]
4V8AX-ray3.20CQ/DQ1-105[»]
4V8BX-ray3.00AT/CT1-105[»]
4V8CX-ray3.30CT/DT1-105[»]
4V8DX-ray3.00AT/CT1-105[»]
4V8EX-ray3.30BT/DT1-105[»]
4V8FX-ray3.30BT/CT1-105[»]
4V8GX-ray3.00AQ/CQ1-105[»]
4V8HX-ray3.10AQ/CQ1-105[»]
4V8IX-ray2.70AQ/CQ1-105[»]
4V8JX-ray3.90AQ/CQ1-105[»]
4V8NX-ray3.10AQ/CQ1-105[»]
4V8OX-ray3.80AQ1-105[»]
4V8QX-ray3.10BQ1-105[»]
4V8UX-ray3.70AQ/CQ1-105[»]
4V8XX-ray3.35AQ/CQ1-105[»]
4V90X-ray2.95AQ1-105[»]
4V95X-ray3.20AQ/CQ1-105[»]
4V97X-ray3.52AQ/CQ1-105[»]
4V9AX-ray3.30AT/CT1-105[»]
4V9BX-ray3.10AT/CT1-105[»]
4V9HX-ray2.86AQ2-100[»]
4V9IX-ray3.30AQ/CQ2-100[»]
4V9RX-ray3.00AQ/CQ1-105[»]
4V9SX-ray3.10AQ/CQ1-105[»]
4W2EX-ray2.90q1-105[»]
4W2FX-ray2.40AQ/CQ1-105[»]
4W2GX-ray2.55AQ/CQ1-105[»]
4W2HX-ray2.70AQ/CQ1-105[»]
4W2IX-ray2.70AQ/CQ1-105[»]
ProteinModelPortaliQ5SHP7.
SMRiQ5SHP7. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHP7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0186.
HOGENOMiHOG000231339.
KOiK02961.
OMAiWIVVKDS.
OrthoDBiEOG63JRH2.
PhylomeDBiQ5SHP7.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
IPR019984. Ribosomal_S17_bac-type.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
[Graphical view]
PRINTSiPR00973. RIBOSOMALS17.
ProDomiPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR03635. S17_bact. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5SHP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKKVLTGVV VSDKMQKTVT VLVERQFPHP LYGKVIKRSK KYLAHDPEEK
60 70 80 90 100
YKLGDVVEII ESRPISKRKR FRVLRLVESG RMDLVEKYLI RRQNYESLSK

RGGKA
Length:105
Mass (Da):12,298
Last modified:January 23, 2007 - v3
Checksum:i60981D6D57478FBD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501K → R in CAA39893 (PubMed:2029902).Curated
Sequence conflicti53 – 531L → V in CAA39893 (PubMed:2029902).Curated
Sequence conflicti62 – 621S → A in CAA39893 (PubMed:2029902).Curated
Sequence conflicti79 – 791S → E in CAA39893 (PubMed:2029902).Curated
Sequence conflicti82 – 821M → L in CAA39893 (PubMed:2029902).Curated
Sequence conflicti90 – 901I → V in CAA39893 (PubMed:2029902).Curated
Sequence conflicti96 – 961E → A in CAA39893 (PubMed:2029902).Curated

Mass spectrometryi

Molecular mass is 12167 Da from positions 2 - 105. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56552 Genomic DNA. Translation: CAA39893.1.
AP008226 Genomic DNA. Translation: BAD71506.1.
RefSeqiYP_144949.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71506; BAD71506; BAD71506.
GeneIDi3169831.
KEGGittj:TTHA1683.
PATRICi23958321. VBITheThe93045_1653.

Cross-referencesi

Web resourcesi

T.thermophilus ribosome structure and function

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56552 Genomic DNA. Translation: CAA39893.1.
AP008226 Genomic DNA. Translation: BAD71506.1.
RefSeqiYP_144949.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00Q1-105[»]
1HNWX-ray3.40Q1-105[»]
1HNXX-ray3.40Q1-105[»]
1HNZX-ray3.30Q1-105[»]
1HR0X-ray3.20Q1-105[»]
1I94X-ray3.20Q2-105[»]
1I95X-ray4.50Q2-105[»]
1I96X-ray4.20Q2-105[»]
1I97X-ray4.50Q2-105[»]
1IBKX-ray3.31Q1-105[»]
1IBLX-ray3.11Q1-105[»]
1IBMX-ray3.31Q1-105[»]
1J5EX-ray3.05Q2-105[»]
1JGOX-ray5.60T1-105[»]
1JGPX-ray7.00T1-105[»]
1JGQX-ray5.00T1-105[»]
1L1Umodel-Q1-105[»]
1ML5electron microscopy14.00T1-105[»]
1N32X-ray3.00Q2-105[»]
1N33X-ray3.35Q2-105[»]
1N34X-ray3.80Q2-105[»]
1N36X-ray3.65Q2-105[»]
1VVJX-ray3.44QQ/XQ1-105[»]
1VY4X-ray2.60AQ/CQ1-105[»]
1VY5X-ray2.55AQ/CQ1-105[»]
1VY6X-ray2.90AQ/CQ1-105[»]
1VY7X-ray2.80AQ/CQ1-105[»]
1XMOX-ray3.25Q1-105[»]
1XMQX-ray3.00Q1-105[»]
1XNQX-ray3.05Q1-105[»]
1XNRX-ray3.10Q1-105[»]
2E5LX-ray3.30Q2-105[»]
2F4VX-ray3.80Q1-105[»]
2HHHX-ray3.35Q1-105[»]
2UU9X-ray3.10Q2-105[»]
2UUAX-ray2.90Q2-105[»]
2UUBX-ray2.80Q2-105[»]
2UUCX-ray3.10Q2-105[»]
2UXBX-ray3.10Q2-105[»]
2UXCX-ray2.90Q2-105[»]
2UXDX-ray3.20Q2-105[»]
2ZM6X-ray3.30Q2-105[»]
3OTOX-ray3.69Q1-105[»]
3T1HX-ray3.11Q1-105[»]
3T1YX-ray2.80Q1-105[»]
4AQYX-ray3.50Q2-105[»]
4B3MX-ray2.90Q2-105[»]
4B3RX-ray3.00Q2-105[»]
4B3SX-ray3.15Q2-105[»]
4B3TX-ray3.00Q2-105[»]
4DR1X-ray3.60Q1-105[»]
4DR2X-ray3.25Q1-105[»]
4DR3X-ray3.35Q1-105[»]
4DR4X-ray3.97Q1-105[»]
4DR5X-ray3.45Q1-105[»]
4DR6X-ray3.30Q1-105[»]
4DR7X-ray3.75Q1-105[»]
4DUYX-ray3.39Q1-105[»]
4DUZX-ray3.65Q1-105[»]
4DV0X-ray3.85Q1-105[»]
4DV1X-ray3.85Q1-105[»]
4DV2X-ray3.65Q1-105[»]
4DV3X-ray3.55Q1-105[»]
4DV4X-ray3.65Q1-105[»]
4DV5X-ray3.68Q1-105[»]
4DV6X-ray3.30Q1-105[»]
4DV7X-ray3.29Q1-105[»]
4GKJX-ray3.30Q2-105[»]
4GKKX-ray3.20Q2-105[»]
4JI0X-ray3.49Q1-105[»]
4JI1X-ray3.14Q1-105[»]
4JI2X-ray3.64Q1-105[»]
4JI3X-ray3.35Q1-105[»]
4JI4X-ray3.69Q1-105[»]
4JI5X-ray3.85Q1-105[»]
4JI6X-ray3.55Q1-105[»]
4JI7X-ray3.50Q1-105[»]
4JI8X-ray3.74Q1-105[»]
4JV5X-ray3.16Q2-100[»]
4JYAX-ray3.10Q2-100[»]
4K0KX-ray3.40Q2-101[»]
4KHPX-ray3.10Q2-100[»]
4L47X-ray3.22QQ/XQ1-105[»]
4L71X-ray3.90QQ/XQ1-105[»]
4LELX-ray3.90QQ/XQ1-105[»]
4LF4X-ray3.34Q1-105[»]
4LF5X-ray3.75Q1-105[»]
4LF6X-ray3.31Q1-105[»]
4LF7X-ray3.15Q1-105[»]
4LF8X-ray3.15Q1-105[»]
4LF9X-ray3.28Q1-105[»]
4LFAX-ray3.65Q1-105[»]
4LFBX-ray3.01Q1-105[»]
4LFCX-ray3.60Q1-105[»]
4LFZX-ray3.92QQ/XQ1-105[»]
4LNTX-ray2.94QQ/XQ1-105[»]
4LSKX-ray3.48QQ/XQ1-105[»]
4LT8X-ray3.14QQ/XQ1-105[»]
4NXMX-ray3.65Q1-105[»]
4NXNX-ray3.54Q1-105[»]
4OX9X-ray3.80Q2-105[»]
4P6FX-ray3.60QQ/XQ1-105[»]
4P70X-ray3.68QQ/XQ1-105[»]
4V42X-ray5.50T1-105[»]
4V49X-ray8.70Q2-105[»]
4V4GX-ray11.50Q2-105[»]
4V4IX-ray3.71r1-105[»]
4V4PX-ray5.50BT1-105[»]
4V4RX-ray5.90Q1-105[»]
4V4SX-ray6.76Q1-105[»]
4V4TX-ray6.46Q1-105[»]
4V4XX-ray5.00T1-105[»]
4V4YX-ray5.50T1-105[»]
4V4ZX-ray4.51T1-105[»]
4V51X-ray2.80AQ/CQ2-105[»]
4V5AX-ray3.50AQ/CQ2-105[»]
4V5CX-ray3.30AQ/CQ1-105[»]
4V5DX-ray3.50AQ/CQ1-105[»]
4V5EX-ray3.45AQ/CQ1-105[»]
4V5FX-ray3.60AQ/CQ1-105[»]
4V5GX-ray3.60AQ/CQ1-105[»]
4V5JX-ray3.10AQ/CQ1-105[»]
4V5KX-ray3.20AQ/CQ1-105[»]
4V5LX-ray3.10AQ1-105[»]
4V5Melectron microscopy7.80AQ1-105[»]
4V5Nelectron microscopy7.60AQ1-105[»]
4V5PX-ray3.10AQ/CQ1-105[»]
4V5QX-ray3.10AQ/CQ1-105[»]
4V5RX-ray3.10AQ/CQ1-105[»]
4V5SX-ray3.10AQ/CQ1-105[»]
4V68electron microscopy6.40AQ2-101[»]
4V6AX-ray3.10AQ/CQ1-105[»]
4V6FX-ray3.10BT/CT1-105[»]
4V6GX-ray3.50AT/CT1-105[»]
4V7JX-ray3.30Aq/Bq1-105[»]
4V7KX-ray3.60Aq/Bq1-105[»]
4V7LX-ray3.00AQ/CQ1-105[»]
4V7MX-ray3.45AQ/CQ1-105[»]
4V7WX-ray3.00AQ/CQ1-105[»]
4V7XX-ray3.00AQ/CQ1-105[»]
4V7YX-ray3.00AQ/CQ1-105[»]
4V7ZX-ray3.10AQ/CQ1-105[»]
4V87X-ray3.10BT/CT1-105[»]
4V8AX-ray3.20CQ/DQ1-105[»]
4V8BX-ray3.00AT/CT1-105[»]
4V8CX-ray3.30CT/DT1-105[»]
4V8DX-ray3.00AT/CT1-105[»]
4V8EX-ray3.30BT/DT1-105[»]
4V8FX-ray3.30BT/CT1-105[»]
4V8GX-ray3.00AQ/CQ1-105[»]
4V8HX-ray3.10AQ/CQ1-105[»]
4V8IX-ray2.70AQ/CQ1-105[»]
4V8JX-ray3.90AQ/CQ1-105[»]
4V8NX-ray3.10AQ/CQ1-105[»]
4V8OX-ray3.80AQ1-105[»]
4V8QX-ray3.10BQ1-105[»]
4V8UX-ray3.70AQ/CQ1-105[»]
4V8XX-ray3.35AQ/CQ1-105[»]
4V90X-ray2.95AQ1-105[»]
4V95X-ray3.20AQ/CQ1-105[»]
4V97X-ray3.52AQ/CQ1-105[»]
4V9AX-ray3.30AT/CT1-105[»]
4V9BX-ray3.10AT/CT1-105[»]
4V9HX-ray2.86AQ2-100[»]
4V9IX-ray3.30AQ/CQ2-100[»]
4V9RX-ray3.00AQ/CQ1-105[»]
4V9SX-ray3.10AQ/CQ1-105[»]
4W2EX-ray2.90q1-105[»]
4W2FX-ray2.40AQ/CQ1-105[»]
4W2GX-ray2.55AQ/CQ1-105[»]
4W2HX-ray2.70AQ/CQ1-105[»]
4W2IX-ray2.70AQ/CQ1-105[»]
ProteinModelPortaliQ5SHP7.
SMRiQ5SHP7. Positions 2-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1683.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71506; BAD71506; BAD71506.
GeneIDi3169831.
KEGGittj:TTHA1683.
PATRICi23958321. VBITheThe93045_1653.

Phylogenomic databases

eggNOGiCOG0186.
HOGENOMiHOG000231339.
KOiK02961.
OMAiWIVVKDS.
OrthoDBiEOG63JRH2.
PhylomeDBiQ5SHP7.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-1722-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SHP7.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
IPR019984. Ribosomal_S17_bac-type.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
[Graphical view]
PRINTSiPR00973. RIBOSOMALS17.
ProDomiPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR03635. S17_bact. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the spc ribosomal protein operon of Thermus aquaticus."
    Jahn O., Hartmann R.K., Erdmann V.A.
    Eur. J. Biochem. 197:733-740(1990) [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 (OCT-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(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-14.
  4. "Ribosomal gene disruption in the extreme thermophile Thermus thermophilus HB8. Generation of a mutant lacking ribosomal protein S17."
    Simitsopoulou M., Avila H., Franceschi F.
    Eur. J. Biochem. 266:524-532(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DELETION OF THE GENE.
  5. "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.
  6. "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.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF THE 30S SUBUNIT.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
  15. "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.
  16. "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 nameiRS17_THET8
AccessioniPrimary (citable) accession number: Q5SHP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: April 1, 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

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.