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Protein

30S ribosomal protein S9

Gene

rpsI

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

Part of the top of the head of the 30S subunit. The C-terminal region penetrates the head emerging in the P-site where it contacts tRNA.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S9
Gene namesi
Name:rpsI
Synonyms:rps9
Ordered Locus Names:TTHA1464
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Chemistry databases

DrugBankiDB08185. 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001114311 – 12830S ribosomal protein S9Add BLAST128

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit. Contacts proteins S7 and S10.

Protein-protein interaction databases

STRINGi300852.TTHA1464.

Structurei

Secondary structure

1128
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi9 – 12Combined sources4
Beta strandi14 – 23Combined sources10
Beta strandi26 – 31Combined sources6
Helixi33 – 36Combined sources4
Beta strandi37 – 39Combined sources3
Helixi43 – 47Combined sources5
Helixi48 – 52Combined sources5
Turni56 – 58Combined sources3
Beta strandi59 – 68Combined sources10
Helixi70 – 88Combined sources19
Helixi90 – 92Combined sources3
Helixi93 – 96Combined sources4
Helixi97 – 99Combined sources3
Turni100 – 102Combined sources3
Beta strandi116 – 118Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FJGX-ray3.00I1-128[»]
1HNWX-ray3.40I1-128[»]
1HNXX-ray3.40I1-128[»]
1HNZX-ray3.30I1-128[»]
1HR0X-ray3.20I1-128[»]
1I94X-ray3.20I1-128[»]
1I95X-ray4.50I1-128[»]
1I96X-ray4.20I1-128[»]
1I97X-ray4.50I1-128[»]
1IBKX-ray3.31I1-128[»]
1IBLX-ray3.11I1-128[»]
1IBMX-ray3.31I1-128[»]
1J5EX-ray3.05I1-128[»]
1JGOX-ray5.60L1-128[»]
1JGPX-ray7.00L1-128[»]
1JGQX-ray5.00L1-128[»]
1L1Umodel-I2-128[»]
1ML5electron microscopy14.00L1-128[»]
1N32X-ray3.00I1-128[»]
1N33X-ray3.35I1-128[»]
1N34X-ray3.80I1-128[»]
1N36X-ray3.65I1-128[»]
1VVJX-ray3.44QI/XI1-128[»]
1VY4X-ray2.60AI/CI1-128[»]
1VY5X-ray2.55AI/CI1-128[»]
1VY6X-ray2.90AI/CI1-128[»]
1VY7X-ray2.80AI/CI1-128[»]
1XMOX-ray3.25I1-128[»]
1XMQX-ray3.00I1-128[»]
1XNQX-ray3.05I1-128[»]
1XNRX-ray3.10I1-128[»]
2E5LX-ray3.30I1-128[»]
2F4VX-ray3.80I1-128[»]
2HHHX-ray3.35I1-128[»]
2UU9X-ray3.10I1-128[»]
2UUAX-ray2.90I1-128[»]
2UUBX-ray2.90I1-128[»]
2UUCX-ray3.10I1-128[»]
2ZM6X-ray3.30I1-128[»]
3OTOX-ray3.69I1-128[»]
4AQYX-ray3.50I1-128[»]
4B3MX-ray2.90I1-128[»]
4B3RX-ray3.00I1-128[»]
4B3SX-ray3.15I1-128[»]
4B3TX-ray3.00I1-128[»]
4DR1X-ray3.60I1-128[»]
4DR2X-ray3.25I1-128[»]
4DR3X-ray3.35I1-128[»]
4DR4X-ray3.97I1-128[»]
4DR5X-ray3.45I1-128[»]
4DR6X-ray3.30I1-128[»]
4DR7X-ray3.75I1-128[»]
4DUYX-ray3.39I1-128[»]
4DUZX-ray3.65I1-128[»]
4DV0X-ray3.85I1-128[»]
4DV1X-ray3.85I1-128[»]
4DV2X-ray3.65I1-128[»]
4DV3X-ray3.55I1-128[»]
4DV4X-ray3.65I1-128[»]
4DV5X-ray3.68I1-128[»]
4DV6X-ray3.30I1-128[»]
4DV7X-ray3.29I1-128[»]
4GKJX-ray3.30I2-128[»]
4GKKX-ray3.20I2-128[»]
4JI0X-ray3.49I1-128[»]
4JI1X-ray3.14I1-128[»]
4JI2X-ray3.64I1-128[»]
4JI3X-ray3.35I1-128[»]
4JI4X-ray3.69I1-128[»]
4JI5X-ray3.85I1-128[»]
4JI6X-ray3.55I1-128[»]
4JI7X-ray3.50I1-128[»]
4JI8X-ray3.74I1-128[»]
4JV5X-ray3.16I2-128[»]
4JYAX-ray3.10I2-128[»]
4K0KX-ray3.40I2-128[»]
4KHPX-ray3.10I2-128[»]
4L47X-ray3.22QI/XI1-128[»]
4L71X-ray3.90QI/XI1-128[»]
4LELX-ray3.90QI/XI1-128[»]
4LF4X-ray3.34I1-128[»]
4LF5X-ray3.75I1-128[»]
4LF6X-ray3.31I1-128[»]
4LF7X-ray3.15I1-128[»]
4LF8X-ray3.15I1-128[»]
4LF9X-ray3.28I1-128[»]
4LFAX-ray3.65I1-128[»]
4LFBX-ray3.01I1-128[»]
4LFCX-ray3.60I1-128[»]
4LFZX-ray3.92QI/XI1-128[»]
4LNTX-ray2.94QI/XI1-128[»]
4LSKX-ray3.48QI/XI1-128[»]
4LT8X-ray3.14QI/XI1-128[»]
4NXMX-ray3.65I1-128[»]
4NXNX-ray3.54I1-128[»]
4OX9X-ray3.80I1-128[»]
4P6FX-ray3.60QI/XI1-128[»]
4P70X-ray3.68QI/XI1-128[»]
4TUAX-ray3.60QI/XI1-128[»]
4TUBX-ray3.60QI/XI1-128[»]
4TUCX-ray3.60QI/XI1-128[»]
4TUDX-ray3.60QI/XI1-128[»]
4TUEX-ray3.50QI/XI1-128[»]
4V42X-ray5.50AL1-128[»]
4V49X-ray8.70I2-128[»]
4V4AX-ray9.50I2-128[»]
4V4IX-ray3.71j1-128[»]
4V4PX-ray5.50BL1-128[»]
4V4RX-ray5.90AI1-128[»]
4V4SX-ray6.76AI1-128[»]
4V4TX-ray6.46AI1-128[»]
4V4XX-ray5.00AL1-128[»]
4V4YX-ray5.50AL1-128[»]
4V4ZX-ray4.51AL1-128[»]
4V5EX-ray3.45AI/CI1-128[»]
4V5FX-ray3.60AI/CI1-128[»]
4V5GX-ray3.60AI/CI1-128[»]
4V5JX-ray3.10AI/CI1-128[»]
4V5KX-ray3.20AI/CI1-128[»]
4V5LX-ray3.10AI1-128[»]
4V5Melectron microscopy7.80AI1-128[»]
4V5Nelectron microscopy7.60AI1-128[»]
4V5PX-ray3.10AI/CI1-128[»]
4V5QX-ray3.10AI/CI1-128[»]
4V5RX-ray3.10AI/CI1-128[»]
4V5SX-ray3.10AI/CI1-128[»]
4V68electron microscopy6.40AI2-128[»]
4V6AX-ray3.10AI/CI1-128[»]
4V6FX-ray3.10BL/CL1-128[»]
4V6GX-ray3.50AL/CL1-128[»]
4V7JX-ray3.30Ai/Bi1-128[»]
4V7KX-ray3.60Ai/Bi1-128[»]
4V7LX-ray3.00AI/CI1-128[»]
4V7MX-ray3.45AI/CI1-128[»]
4V7WX-ray3.00AI/CI1-128[»]
4V7XX-ray3.00AI/CI1-128[»]
4V7YX-ray3.00AI/CI1-128[»]
4V7ZX-ray3.10AI/CI1-128[»]
4V87X-ray3.10BL/CL1-128[»]
4V8AX-ray3.20CI/DI1-128[»]
4V8BX-ray3.00AL/CL1-128[»]
4V8CX-ray3.30CL/DL1-128[»]
4V8DX-ray3.00AL/CL1-128[»]
4V8EX-ray3.30BL/DL1-128[»]
4V8FX-ray3.30BL/CL1-128[»]
4V8GX-ray3.00AI/CI1-128[»]
4V8HX-ray3.10AI/CI1-128[»]
4V8IX-ray2.70AI/CI1-128[»]
4V8JX-ray3.90AI/CI1-128[»]
4V8NX-ray3.10AI/CI1-128[»]
4V8OX-ray3.80AI1-128[»]
4V8QX-ray3.10BI1-128[»]
4V8UX-ray3.70AI/CI1-128[»]
4V8XX-ray3.35AI/CI1-128[»]
4V90X-ray2.95AI1-128[»]
4V95X-ray3.20AI/CI1-128[»]
4V97X-ray3.52AI/CI1-128[»]
4V9AX-ray3.30AL/CL1-128[»]
4V9BX-ray3.10AL/CL1-128[»]
4V9HX-ray2.86AI2-128[»]
4V9IX-ray3.30AI/CI2-128[»]
4V9RX-ray3.00AI/CI1-128[»]
4V9SX-ray3.10AI/CI1-128[»]
4W2EX-ray2.90i1-128[»]
4W2FX-ray2.40AI/CI1-128[»]
4W2GX-ray2.55AI/CI1-128[»]
4W2HX-ray2.70AI/CI1-128[»]
4W2IX-ray2.70AI/CI1-128[»]
4W4GX-ray3.30QI/XI1-128[»]
4WPOX-ray2.80BI/DI1-128[»]
4WQ1X-ray3.1082/8E1-128[»]
4WQFX-ray2.80BI/DI1-128[»]
4WQRX-ray3.1582/8E1-128[»]
4WQUX-ray2.80BI/DI1-128[»]
4WQYX-ray2.80BI/DI1-128[»]
4WR6X-ray3.0582/8E1-128[»]
4WRAX-ray3.0582/8E1-128[»]
4WROX-ray3.058E1-128[»]
4WSDX-ray2.9582/8E1-128[»]
4WSMX-ray3.3082/8E1-128[»]
4WT1X-ray3.0582/8E1-128[»]
4WT8X-ray3.40AI/BI2-128[»]
4WU1X-ray3.2082/8E1-128[»]
4WZDX-ray3.1082/8E1-128[»]
4WZOX-ray3.3082/8E1-128[»]
4X62X-ray3.45I2-128[»]
4X64X-ray3.35I2-128[»]
4X65X-ray3.35I2-128[»]
4X66X-ray3.45I2-128[»]
4Y4OX-ray2.301i/2i1-128[»]
4Y4PX-ray2.501i/2i1-128[»]
4YHHX-ray3.42I2-128[»]
4YPBX-ray3.40QI/XI1-128[»]
4YY3X-ray3.60I1-128[»]
4YZVX-ray3.10QI/XI1-128[»]
4Z3SX-ray2.651i/2i1-128[»]
4Z8CX-ray2.901i/2i1-128[»]
4ZERX-ray3.101i/2i2-128[»]
4ZSNX-ray3.60QI/XI1-128[»]
5A9Zelectron microscopy4.70BM2-128[»]
5AA0electron microscopy5.00BM2-128[»]
5BR8X-ray3.40I1-128[»]
5CZPX-ray3.30QI/XI1-128[»]
5D8BX-ray3.63FC/JA1-128[»]
5DFEX-ray3.10QI/XI1-128[»]
5DOXX-ray3.101i/2i1-128[»]
5DOYX-ray2.601i/2i1-128[»]
5E7KX-ray3.2082/8E1-128[»]
5E81X-ray2.9582/8E1-128[»]
5EL4X-ray3.1582/8E1-128[»]
5EL5X-ray3.1582/8E1-128[»]
5EL6X-ray3.1082/8E1-128[»]
5EL7X-ray3.1582/8E1-128[»]
5F8KX-ray2.801i/2i2-128[»]
5FDUX-ray2.901i/2i2-128[»]
5FDVX-ray2.801i/2i2-128[»]
5HAUX-ray3.001i/2i1-128[»]
5HCPX-ray2.891i/2i1-128[»]
5HCQX-ray2.801i/2i1-128[»]
5HCRX-ray2.801i/2i1-128[»]
5HD1X-ray2.701i/2i1-128[»]
5IB7X-ray2.9982/8E1-128[»]
5IB8X-ray3.1382/8E1-128[»]
5IBBX-ray2.9682/8E1-128[»]
5IMQelectron microscopy3.80M1-128[»]
5IMRelectron microscopy-M1-128[»]
5IWAX-ray3.50I2-128[»]
5J30X-ray3.20QI/XI1-128[»]
5J3CX-ray3.04QI/XI1-128[»]
5J4BX-ray2.601i/2i1-128[»]
5J4CX-ray2.801i/2i1-128[»]
5J8BX-ray2.60i1-128[»]
5LMNelectron microscopy3.55I1-128[»]
5LMOelectron microscopy4.30I1-128[»]
5LMPelectron microscopy5.35I1-128[»]
5LMQelectron microscopy4.20I1-128[»]
5LMRelectron microscopy4.45I1-128[»]
5LMSelectron microscopy5.10I1-128[»]
5LMTelectron microscopy4.15I1-128[»]
5LMUelectron microscopy4.00I1-128[»]
5LMVelectron microscopy4.90I1-128[»]
ProteinModelPortaliP80374.
SMRiP80374.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80374.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108UJD. Bacteria.
COG0103. LUCA.
HOGENOMiHOG000019802.
KOiK02996.
OMAiMVERKKF.
PhylomeDBiP80374.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
HAMAPiMF_00532_B. Ribosomal_S9_B. 1 hit.
InterProiView protein in InterPro
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR023035. Ribosomal_S9_bac/plastid.
IPR020574. Ribosomal_S9_CS.
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiView protein in Pfam
PF00380. Ribosomal_S9. 1 hit.
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiView protein in PROSITE
PS00360. RIBOSOMAL_S9. 1 hit.

Sequencei

Sequence statusi: Complete.

P80374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQYYGTGRR KEAVARVFLR PGNGKVTVNG QDFNEYFQGL VRAVAALEPL
60 70 80 90 100
RAVDALGHFD AYITVRGGGK SGQIDAIKLG IARALVQYNP DYRAKLKPLG
110 120
FLTRDARVVE RKKYGKHKAR RAPQYSKR
Length:128
Mass (Da):14,383
Last modified:May 10, 2005 - v3
Checksum:iFA9A4ED2CC5D8CC1
GO

Mass spectrometryi

Molecular mass is 14384 Da from positions 1 - 128. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71287.1.
RefSeqiWP_011228699.1. NC_006461.1.
YP_144730.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71287; BAD71287; BAD71287.
GeneIDi3169752.
KEGGittj:TTHA1464.
PATRICifig|300852.9.peg.1438.

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 one 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.

Entry informationi

Entry nameiRS9_THET8
AccessioniPrimary (citable) accession number: P80374
Secondary accession number(s): Q5SIB0, Q9ACJ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 10, 2005
Last modified: June 7, 2017
This is version 155 of the entry and version 3 of the sequence. See 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