Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

30S ribosomal protein S20

Gene

rpsT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Binds directly to 16S ribosomal RNA.

GO - Molecular functioni

  • ornithine decarboxylase inhibitor activity Source: EcoCyc
  • small ribosomal subunit rRNA binding Source: EcoCyc
  • structural constituent of ribosome Source: CAFA

GO - Biological processi

  • ribosomal small subunit assembly Source: CAFA
  • translation Source: InterPro

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:EG10919-MONOMER
MetaCyc:EG10919-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S20
Alternative name(s):
Small ribosomal subunit protein bS201 Publication
Gene namesi
Name:rpsT
Ordered Locus Names:b0023, JW0022
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10919 rpsT

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • cytosolic small ribosomal subunit Source: CAFA

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001679582 – 8730S ribosomal protein S20Add BLAST86

Proteomic databases

EPDiP0A7U7
PaxDbiP0A7U7
PRIDEiP0A7U7

Interactioni

Subunit structurei

Part of the 30S ribosomal subunit (PubMed:786731, PubMed:10094780, PubMed:12244297, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:27906160, PubMed:27906161).8 Publications

Protein-protein interaction databases

BioGridi4260844, 67 interactors
DIPiDIP-35857N
IntActiP0A7U7, 70 interactors
STRINGi316385.ECDH10B_0024

Structurei

Secondary structure

187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 41Combined sources34
Helixi44 – 64Combined sources21
Turni66 – 69Combined sources4
Helixi70 – 83Combined sources14
Turni84 – 86Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-T3-87[»]
2YKRelectron microscopy9.80T3-87[»]
3J9Yelectron microscopy3.90t1-87[»]
3J9Zelectron microscopy3.60ST2-87[»]
3JA1electron microscopy3.60ST2-87[»]
3JBUelectron microscopy3.64T1-87[»]
3JBVelectron microscopy3.32T1-87[»]
3JCDelectron microscopy3.70t1-87[»]
3JCEelectron microscopy3.20t1-87[»]
3JCJelectron microscopy3.7031-87[»]
3JCNelectron microscopy4.60x1-87[»]
4A2Ielectron microscopy16.50T3-87[»]
4ADVelectron microscopy13.50T2-87[»]
4U1UX-ray2.95AT/CT3-87[»]
4U1VX-ray3.00AT/CT3-87[»]
4U20X-ray2.90AT/CT3-87[»]
4U24X-ray2.90AT/CT3-87[»]
4U25X-ray2.90AT/CT3-87[»]
4U26X-ray2.80AT/CT3-87[»]
4U27X-ray2.80AT/CT3-87[»]
4V47electron microscopy12.30BT2-87[»]
4V48electron microscopy11.50BT2-87[»]
4V4HX-ray3.46AT/CT1-87[»]
4V4QX-ray3.46AT/CT2-87[»]
4V4Velectron microscopy15.00AT5-87[»]
4V4Welectron microscopy15.00AT5-87[»]
4V50X-ray3.22AT/CT2-87[»]
4V52X-ray3.21AT/CT2-87[»]
4V53X-ray3.54AT/CT2-87[»]
4V54X-ray3.30AT/CT2-87[»]
4V55X-ray4.00AT/CT2-87[»]
4V56X-ray3.93AT/CT2-87[»]
4V57X-ray3.50AT/CT2-87[»]
4V5BX-ray3.74BT/DT2-87[»]
4V5Helectron microscopy5.80AT3-87[»]
4V5YX-ray4.45AT/CT2-87[»]
4V64X-ray3.50AT/CT2-87[»]
4V65electron microscopy9.00AN1-87[»]
4V66electron microscopy9.00AN1-87[»]
4V69electron microscopy6.70AT3-87[»]
4V6CX-ray3.19AT/CT1-87[»]
4V6DX-ray3.81AT/CT1-87[»]
4V6EX-ray3.71AT/CT1-87[»]
4V6Kelectron microscopy8.25BX1-87[»]
4V6Lelectron microscopy13.20AX1-87[»]
4V6Melectron microscopy7.10AT2-87[»]
4V6Nelectron microscopy12.10BW2-87[»]
4V6Oelectron microscopy14.70AW2-87[»]
4V6Pelectron microscopy13.50AW2-87[»]
4V6Qelectron microscopy11.50AW2-87[»]
4V6Relectron microscopy11.50AW2-87[»]
4V6Selectron microscopy13.10BV2-87[»]
4V6Telectron microscopy8.30AT3-87[»]
4V6Velectron microscopy9.80AT2-87[»]
4V6Yelectron microscopy12.00AT3-87[»]
4V6Zelectron microscopy12.00AT3-87[»]
4V70electron microscopy17.00AT3-87[»]
4V71electron microscopy20.00AT3-87[»]
4V72electron microscopy13.00AT3-87[»]
4V73electron microscopy15.00AT3-87[»]
4V74electron microscopy17.00AT3-87[»]
4V75electron microscopy12.00AT3-87[»]
4V76electron microscopy17.00AT3-87[»]
4V77electron microscopy17.00AT3-87[»]
4V78electron microscopy20.00AT3-87[»]
4V79electron microscopy15.00AT3-87[»]
4V7Aelectron microscopy9.00AT3-87[»]
4V7Belectron microscopy6.80AT1-87[»]
4V7Celectron microscopy7.60AT2-87[»]
4V7Delectron microscopy7.60BT2-87[»]
4V7Ielectron microscopy9.60BT1-87[»]
4V7SX-ray3.25AT/CT3-87[»]
4V7TX-ray3.19AT/CT3-87[»]
4V7UX-ray3.10AT/CT3-87[»]
4V7VX-ray3.29AT/CT3-87[»]
4V85X-ray3.20AT1-87[»]
4V89X-ray3.70AT1-87[»]
4V9CX-ray3.30AT/CT1-87[»]
4V9DX-ray3.00AT/BT3-87[»]
4V9OX-ray2.90BT/DT/FT/HT1-87[»]
4V9PX-ray2.90BT/DT/FT/HT1-87[»]
4WF1X-ray3.09AT/CT3-87[»]
4WOIX-ray3.00AT/DT1-87[»]
4WWWX-ray3.10QT/XT3-87[»]
4YBBX-ray2.10AT/BT2-87[»]
5AFIelectron microscopy2.90t1-87[»]
5H5Uelectron microscopy3.0012-87[»]
5IQRelectron microscopy3.00y1-87[»]
5IT8X-ray3.12AT/BT2-87[»]
5J5BX-ray2.80AT/BT2-87[»]
5J7LX-ray3.00AT/BT2-87[»]
5J88X-ray3.32AT/BT2-87[»]
5J8AX-ray3.10AT/BT2-87[»]
5J91X-ray2.96AT/BT2-87[»]
5JC9X-ray3.03AT/BT2-87[»]
5JTEelectron microscopy3.60AT1-87[»]
5JU8electron microscopy3.60AT1-87[»]
5KCRelectron microscopy3.601t1-87[»]
5KCSelectron microscopy3.901t1-87[»]
5KPSelectron microscopy3.90251-87[»]
5KPVelectron microscopy4.10241-87[»]
5KPWelectron microscopy3.90241-87[»]
5KPXelectron microscopy3.90241-87[»]
5L3Pelectron microscopy3.70t1-87[»]
5LZAelectron microscopy3.60t3-87[»]
5LZBelectron microscopy5.30t3-87[»]
5LZCelectron microscopy4.80t3-87[»]
5LZDelectron microscopy3.40t3-87[»]
5LZEelectron microscopy3.50t3-87[»]
5LZFelectron microscopy4.60t3-87[»]
5MDVelectron microscopy2.97y1-87[»]
5MDWelectron microscopy3.06y1-87[»]
5MDYelectron microscopy3.35y1-87[»]
5MDZelectron microscopy3.10y1-87[»]
5ME0electron microscopy13.50T1-87[»]
5ME1electron microscopy13.50T1-87[»]
5MGPelectron microscopy3.10t3-87[»]
5MY1electron microscopy7.60T2-87[»]
5NO2electron microscopy5.16T2-87[»]
5NO3electron microscopy5.16T2-87[»]
5NO4electron microscopy5.16T2-87[»]
5NP6electron microscopy3.60W3-87[»]
5NWYelectron microscopy2.93J1-87[»]
5O2Relectron microscopy3.40t3-87[»]
5U4Ielectron microscopy3.50t2-87[»]
5U9Felectron microscopy3.20T1-87[»]
5U9Gelectron microscopy3.20T1-87[»]
5UYKelectron microscopy3.90T3-87[»]
5UYLelectron microscopy3.60T3-87[»]
5UYMelectron microscopy3.20T3-87[»]
5UYNelectron microscopy4.00T3-87[»]
5UYPelectron microscopy3.90T3-87[»]
5UYQelectron microscopy3.80T3-87[»]
5UZ4electron microscopy5.80T1-87[»]
6BU8electron microscopy3.50T3-87[»]
6C4Ielectron microscopy3.24t1-87[»]
6ENFelectron microscopy3.20t3-87[»]
6ENJelectron microscopy3.70t3-87[»]
6ENUelectron microscopy3.10t3-87[»]
ProteinModelPortaliP0A7U7
SMRiP0A7U7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7U7

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105KQV Bacteria
COG0268 LUCA
HOGENOMiHOG000097048
InParanoidiP0A7U7
KOiK02968
OMAiANKKSAM
PhylomeDBiP0A7U7

Family and domain databases

Gene3Di1.20.58.110, 1 hit
HAMAPiMF_00500 Ribosomal_S20, 1 hit
InterProiView protein in InterPro
IPR002583 Ribosomal_S20
IPR036510 Ribosomal_S20_sf
PANTHERiPTHR33398 PTHR33398, 1 hit
PfamiView protein in Pfam
PF01649 Ribosomal_S20p, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD004231 Ribosomal_S20, 1 hit
SUPFAMiSSF46992 SSF46992, 1 hit
TIGRFAMsiTIGR00029 S20, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0A7U7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANIKSAKKR AIQSEKARKH NASRRSMMRT FIKKVYAAIE AGDKAAAQKA
60 70 80
FNEMQPIVDR QAAKGLIHKN KAARHKANLT AQINKLA
Length:87
Mass (Da):9,684
Last modified:January 23, 2007 - v2
Checksum:iF02154BE2D1E22D9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38A → R in AAA24604 (PubMed:2985604).Curated1

Mass spectrometryi

Molecular mass is 9553.6 Da from positions 2 - 87. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10428 Genomic DNA Translation: AAA24604.1
X04382 Genomic DNA Translation: CAA27968.1
U00096 Genomic DNA Translation: AAC73134.1
AP009048 Genomic DNA Translation: BAB96593.1
PIRiA30425 R3EC20
RefSeqiNP_414564.1, NC_000913.3
WP_001274021.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73134; AAC73134; b0023
BAB96593; BAB96593; BAB96593
GeneIDi944759
KEGGiecj:JW0022
eco:b0023
PATRICifig|1411691.4.peg.2261

Similar proteinsi

Entry informationi

Entry nameiRS20_ECOLI
AccessioniPrimary (citable) accession number: P0A7U7
Secondary accession number(s): P02378
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 129 of the entry and version 2 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health