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Protein

30S ribosomal protein S20

Gene

rpsT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds directly to 16S ribosomal RNA.

GO - Molecular functioni

  1. ornithine decarboxylase inhibitor activity Source: EcoCyc
  2. small ribosomal subunit rRNA binding Source: EcoCyc
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. negative regulation of catalytic activity Source: GOC
  2. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10919-MONOMER.
ECOL316407:JW0022-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S20
Gene namesi
Name:rpsT
Ordered Locus Names:b0023, JW0022
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10919. rpsT.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic small ribosomal subunit Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 878630S ribosomal protein S20PRO_0000167958Add
BLAST

Proteomic databases

PaxDbiP0A7U7.
PRIDEiP0A7U7.

Expressioni

Gene expression databases

GenevestigatoriP0A7U7.

Interactioni

Protein-protein interaction databases

DIPiDIP-35857N.
IntActiP0A7U7. 57 interactions.
STRINGi511145.b0023.

Structurei

Secondary structure

1
87
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 4134Combined sources
Helixi44 – 6421Combined sources
Turni66 – 694Combined sources
Helixi70 – 8314Combined sources
Turni84 – 863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-T3-87[»]
1P6Gelectron microscopy12.30T2-87[»]
1P87electron microscopy11.50T2-87[»]
1VS5X-ray3.46T1-87[»]
1VS7X-ray3.46T1-87[»]
2AVYX-ray3.46T2-87[»]
2AW7X-ray3.46T2-87[»]
2GY9electron microscopy15.00T5-87[»]
2GYBelectron microscopy15.00T5-87[»]
2I2PX-ray3.22T2-87[»]
2I2UX-ray3.22T2-87[»]
2QALX-ray3.21T2-87[»]
2QANX-ray3.21T2-87[»]
2QB9X-ray3.54T2-87[»]
2QBBX-ray3.54T2-87[»]
2QBDX-ray3.30T2-87[»]
2QBFX-ray3.30T2-87[»]
2QBHX-ray4.00T2-87[»]
2QBJX-ray4.00T2-87[»]
2QOUX-ray3.93T2-87[»]
2QOWX-ray3.93T2-87[»]
2QOYX-ray3.50T2-87[»]
2QP0X-ray3.50T2-87[»]
2VHPX-ray3.74T2-87[»]
2WWLelectron microscopy5.80T3-87[»]
2YKRelectron microscopy9.80T3-87[»]
2Z4KX-ray4.45T2-87[»]
2Z4MX-ray4.45T2-87[»]
3DF1X-ray3.50T2-87[»]
3DF3X-ray3.50T2-86[»]
3E1Aelectron microscopy-N1-87[»]
3E1Celectron microscopy-N1-87[»]
3FIHelectron microscopy6.70T3-87[»]
3I1MX-ray3.19T1-87[»]
3I1OX-ray3.19T1-87[»]
3I1QX-ray3.81T1-87[»]
3I1SX-ray3.81T1-87[»]
3I1ZX-ray3.71T1-87[»]
3I21X-ray3.71T1-87[»]
3IZVelectron microscopy-X1-87[»]
3IZWelectron microscopy-X1-87[»]
3J00electron microscopy-T2-87[»]
3J0Uelectron microscopy12.10W2-87[»]
3J0Velectron microscopy14.70W2-87[»]
3J0Xelectron microscopy13.50W2-87[»]
3J0Zelectron microscopy11.50W2-87[»]
3J10electron microscopy11.50W2-87[»]
3J13electron microscopy13.10V2-87[»]
3J18electron microscopy8.30T3-87[»]
3J36electron microscopy9.80T2-87[»]
3J4Velectron microscopy12.00T3-87[»]
3J4Welectron microscopy12.00T3-87[»]
3J4Yelectron microscopy17.00T3-87[»]
3J4Zelectron microscopy20.00T3-87[»]
3J53electron microscopy13.00T3-87[»]
3J55electron microscopy15.00T3-87[»]
3J57electron microscopy17.00T3-87[»]
3J59electron microscopy12.00T3-87[»]
3J5Belectron microscopy17.00T3-87[»]
3J5Delectron microscopy17.00T3-87[»]
3J5Felectron microscopy20.00T3-87[»]
3J5Helectron microscopy15.00T3-87[»]
3J5Jelectron microscopy9.00T3-87[»]
3J5Nelectron microscopy6.80T1-87[»]
3J5Telectron microscopy7.60T2-87[»]
3J5Xelectron microscopy7.60T2-87[»]
3KC4electron microscopy-T1-87[»]
3OAQX-ray3.25T3-87[»]
3OARX-ray3.25T3-87[»]
3OFAX-ray3.19T3-87[»]
3OFBX-ray3.19T3-87[»]
3OFOX-ray3.10T3-87[»]
3OFPX-ray3.10T3-87[»]
3OFXX-ray3.29T3-87[»]
3OFYX-ray3.29T3-87[»]
3OR9X-ray3.30T1-87[»]
3ORAX-ray3.30T1-87[»]
3SFSX-ray3.20T1-87[»]
3UOQX-ray3.70T1-87[»]
4A2Ielectron microscopy16.50T3-87[»]
4ADVelectron microscopy13.50T2-87[»]
4GAQX-ray3.30T1-87[»]
4GASX-ray3.30T1-87[»]
4GD1X-ray3.00T3-87[»]
4GD2X-ray3.00T3-87[»]
4KIYX-ray2.90T1-87[»]
4KJ0X-ray2.90T1-87[»]
4KJ2X-ray2.90T1-87[»]
4KJ4X-ray2.90T1-87[»]
4KJ6X-ray2.90T1-87[»]
4KJ8X-ray2.90T1-87[»]
4KJAX-ray2.90T1-87[»]
4KJCX-ray2.90T1-87[»]
4PE9X-ray2.95T3-87[»]
4PEAX-ray2.95T3-87[»]
4TOLX-ray3.00T3-87[»]
4TONX-ray3.00T3-87[»]
4TOUX-ray2.90T3-87[»]
4TOWX-ray2.90T3-87[»]
4TP0X-ray2.90T3-87[»]
4TP2X-ray2.90T3-87[»]
4TP4X-ray2.90T3-87[»]
4TP6X-ray2.90T3-87[»]
4TP8X-ray2.80T3-87[»]
4TPAX-ray2.80T3-87[»]
4TPCX-ray2.80T3-87[»]
4TPEX-ray2.80T3-87[»]
4WAOX-ray3.09T3-87[»]
4WAQX-ray3.09T3-87[»]
ProteinModelPortaliP0A7U7.
SMRiP0A7U7. Positions 3-87.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7U7.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S20P family.Curated

Phylogenomic databases

eggNOGiCOG0268.
HOGENOMiHOG000097048.
InParanoidiP0A7U7.
KOiK02968.
OMAiGLVHKNA.
OrthoDBiEOG6HMXNQ.
PhylomeDBiP0A7U7.

Family and domain databases

Gene3Di1.20.58.110. 1 hit.
HAMAPiMF_00500. Ribosomal_S20.
InterProiIPR002583. Ribosomal_S20.
[Graphical view]
PfamiPF01649. Ribosomal_S20p. 1 hit.
[Graphical view]
ProDomiPD004231. Ribosomal_S20. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381A → R in AAA24604. (PubMed:2985604)Curated

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.
YP_488329.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73134; AAC73134; b0023.
BAB96593; BAB96593; BAB96593.
GeneIDi12931850.
944759.
KEGGiecj:Y75_p0023.
eco:b0023.
PATRICi32115137. VBIEscCol129921_0020.

Cross-referencesi

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.
YP_488329.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5Gmodel-T3-87[»]
1P6Gelectron microscopy12.30T2-87[»]
1P87electron microscopy11.50T2-87[»]
1VS5X-ray3.46T1-87[»]
1VS7X-ray3.46T1-87[»]
2AVYX-ray3.46T2-87[»]
2AW7X-ray3.46T2-87[»]
2GY9electron microscopy15.00T5-87[»]
2GYBelectron microscopy15.00T5-87[»]
2I2PX-ray3.22T2-87[»]
2I2UX-ray3.22T2-87[»]
2QALX-ray3.21T2-87[»]
2QANX-ray3.21T2-87[»]
2QB9X-ray3.54T2-87[»]
2QBBX-ray3.54T2-87[»]
2QBDX-ray3.30T2-87[»]
2QBFX-ray3.30T2-87[»]
2QBHX-ray4.00T2-87[»]
2QBJX-ray4.00T2-87[»]
2QOUX-ray3.93T2-87[»]
2QOWX-ray3.93T2-87[»]
2QOYX-ray3.50T2-87[»]
2QP0X-ray3.50T2-87[»]
2VHPX-ray3.74T2-87[»]
2WWLelectron microscopy5.80T3-87[»]
2YKRelectron microscopy9.80T3-87[»]
2Z4KX-ray4.45T2-87[»]
2Z4MX-ray4.45T2-87[»]
3DF1X-ray3.50T2-87[»]
3DF3X-ray3.50T2-86[»]
3E1Aelectron microscopy-N1-87[»]
3E1Celectron microscopy-N1-87[»]
3FIHelectron microscopy6.70T3-87[»]
3I1MX-ray3.19T1-87[»]
3I1OX-ray3.19T1-87[»]
3I1QX-ray3.81T1-87[»]
3I1SX-ray3.81T1-87[»]
3I1ZX-ray3.71T1-87[»]
3I21X-ray3.71T1-87[»]
3IZVelectron microscopy-X1-87[»]
3IZWelectron microscopy-X1-87[»]
3J00electron microscopy-T2-87[»]
3J0Uelectron microscopy12.10W2-87[»]
3J0Velectron microscopy14.70W2-87[»]
3J0Xelectron microscopy13.50W2-87[»]
3J0Zelectron microscopy11.50W2-87[»]
3J10electron microscopy11.50W2-87[»]
3J13electron microscopy13.10V2-87[»]
3J18electron microscopy8.30T3-87[»]
3J36electron microscopy9.80T2-87[»]
3J4Velectron microscopy12.00T3-87[»]
3J4Welectron microscopy12.00T3-87[»]
3J4Yelectron microscopy17.00T3-87[»]
3J4Zelectron microscopy20.00T3-87[»]
3J53electron microscopy13.00T3-87[»]
3J55electron microscopy15.00T3-87[»]
3J57electron microscopy17.00T3-87[»]
3J59electron microscopy12.00T3-87[»]
3J5Belectron microscopy17.00T3-87[»]
3J5Delectron microscopy17.00T3-87[»]
3J5Felectron microscopy20.00T3-87[»]
3J5Helectron microscopy15.00T3-87[»]
3J5Jelectron microscopy9.00T3-87[»]
3J5Nelectron microscopy6.80T1-87[»]
3J5Telectron microscopy7.60T2-87[»]
3J5Xelectron microscopy7.60T2-87[»]
3KC4electron microscopy-T1-87[»]
3OAQX-ray3.25T3-87[»]
3OARX-ray3.25T3-87[»]
3OFAX-ray3.19T3-87[»]
3OFBX-ray3.19T3-87[»]
3OFOX-ray3.10T3-87[»]
3OFPX-ray3.10T3-87[»]
3OFXX-ray3.29T3-87[»]
3OFYX-ray3.29T3-87[»]
3OR9X-ray3.30T1-87[»]
3ORAX-ray3.30T1-87[»]
3SFSX-ray3.20T1-87[»]
3UOQX-ray3.70T1-87[»]
4A2Ielectron microscopy16.50T3-87[»]
4ADVelectron microscopy13.50T2-87[»]
4GAQX-ray3.30T1-87[»]
4GASX-ray3.30T1-87[»]
4GD1X-ray3.00T3-87[»]
4GD2X-ray3.00T3-87[»]
4KIYX-ray2.90T1-87[»]
4KJ0X-ray2.90T1-87[»]
4KJ2X-ray2.90T1-87[»]
4KJ4X-ray2.90T1-87[»]
4KJ6X-ray2.90T1-87[»]
4KJ8X-ray2.90T1-87[»]
4KJAX-ray2.90T1-87[»]
4KJCX-ray2.90T1-87[»]
4PE9X-ray2.95T3-87[»]
4PEAX-ray2.95T3-87[»]
4TOLX-ray3.00T3-87[»]
4TONX-ray3.00T3-87[»]
4TOUX-ray2.90T3-87[»]
4TOWX-ray2.90T3-87[»]
4TP0X-ray2.90T3-87[»]
4TP2X-ray2.90T3-87[»]
4TP4X-ray2.90T3-87[»]
4TP6X-ray2.90T3-87[»]
4TP8X-ray2.80T3-87[»]
4TPAX-ray2.80T3-87[»]
4TPCX-ray2.80T3-87[»]
4TPEX-ray2.80T3-87[»]
4WAOX-ray3.09T3-87[»]
4WAQX-ray3.09T3-87[»]
ProteinModelPortaliP0A7U7.
SMRiP0A7U7. Positions 3-87.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35857N.
IntActiP0A7U7. 57 interactions.
STRINGi511145.b0023.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP0A7U7.
PRIDEiP0A7U7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73134; AAC73134; b0023.
BAB96593; BAB96593; BAB96593.
GeneIDi12931850.
944759.
KEGGiecj:Y75_p0023.
eco:b0023.
PATRICi32115137. VBIEscCol129921_0020.

Organism-specific databases

EchoBASEiEB0912.
EcoGeneiEG10919. rpsT.

Phylogenomic databases

eggNOGiCOG0268.
HOGENOMiHOG000097048.
InParanoidiP0A7U7.
KOiK02968.
OMAiGLVHKNA.
OrthoDBiEOG6HMXNQ.
PhylomeDBiP0A7U7.

Enzyme and pathway databases

BioCyciEcoCyc:EG10919-MONOMER.
ECOL316407:JW0022-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7U7.
PROiP0A7U7.

Gene expression databases

GenevestigatoriP0A7U7.

Family and domain databases

Gene3Di1.20.58.110. 1 hit.
HAMAPiMF_00500. Ribosomal_S20.
InterProiIPR002583. Ribosomal_S20.
[Graphical view]
PfamiPF01649. Ribosomal_S20p. 1 hit.
[Graphical view]
ProDomiPD004231. Ribosomal_S20. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46992. SSF46992. 1 hit.
TIGRFAMsiTIGR00029. S20. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the gene for ribosomal protein S20 and its flanking regions."
    Mackie G.A.
    J. Biol. Chem. 256:8177-8182(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon."
    Kamio Y., Lin C.-K., Regue M., Wu H.C.
    J. Biol. Chem. 260:5616-5620(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure of the DNA distal to the gene for ribosomal protein S20 in Escherichia coli K12: presence of a strong terminator and an IS1 element."
    Mackie G.A.
    Nucleic Acids Res. 14:6965-6981(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Primary structure of protein S20 from the small ribosomal subunit of Escherichia coli."
    Wittmann-Liebold B., Marzinzig E., Lehmann A.
    FEBS Lett. 68:110-114(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-87.
    Strain: K.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  10. "All-atom homology model of the Escherichia coli 30S ribosomal subunit."
    Tung C.-S., Joseph S., Sanbonmatsu K.Y.
    Nat. Struct. Biol. 9:750-755(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  11. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
    Strain: MRE-600.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS20_ECOLI
AccessioniPrimary (citable) accession number: P0A7U7
Secondary accession number(s): P02378
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 100 of the entry and version 2 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. 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

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.