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P0A7U7

- RS20_ECOLI

UniProt

P0A7U7 - RS20_ECOLI

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Protein

30S ribosomal protein S20

Gene
rpsT, b0023, JW0022
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Binds directly to 16S ribosomal RNA.UniRule annotation

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: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 878630S ribosomal protein S20UniRule annotationPRO_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
Helixi6 – 83
Helixi9 – 4133
Helixi44 – 6421
Turni66 – 694
Helixi70 – 8314
Turni84 – 863

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliP0A7U7.
SMRiP0A7U7. Positions 3-87.

Miscellaneous databases

EvolutionaryTraceiP0A7U7.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0268.
HOGENOMiHOG000097048.
KOiK02968.
OMAiRHKSNLT.
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

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

Mass spectrometryi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381A → R in AAA24604. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A30425. R3EC20.
RefSeqi NP_414564.1. NC_000913.3.
YP_488329.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M5G model - T 3-87 [» ]
1P6G electron microscopy 12.30 T 2-87 [» ]
1P87 electron microscopy 11.50 T 2-87 [» ]
1VS5 X-ray 3.46 T 1-87 [» ]
1VS7 X-ray 3.46 T 1-87 [» ]
2AVY X-ray 3.46 T 2-87 [» ]
2AW7 X-ray 3.46 T 2-87 [» ]
2GY9 electron microscopy 15.00 T 5-87 [» ]
2GYB electron microscopy 15.00 T 5-87 [» ]
2I2P X-ray 3.22 T 2-87 [» ]
2I2U X-ray 3.22 T 2-87 [» ]
2QAL X-ray 3.21 T 2-87 [» ]
2QAN X-ray 3.21 T 2-87 [» ]
2QB9 X-ray 3.54 T 2-87 [» ]
2QBB X-ray 3.54 T 2-87 [» ]
2QBD X-ray 3.30 T 2-87 [» ]
2QBF X-ray 3.30 T 2-87 [» ]
2QBH X-ray 4.00 T 2-87 [» ]
2QBJ X-ray 4.00 T 2-87 [» ]
2QOU X-ray 3.93 T 2-87 [» ]
2QOW X-ray 3.93 T 2-87 [» ]
2QOY X-ray 3.50 T 2-87 [» ]
2QP0 X-ray 3.50 T 2-87 [» ]
2VHP X-ray 3.74 T 2-87 [» ]
2WWL electron microscopy 5.80 T 3-87 [» ]
2YKR electron microscopy 9.80 T 3-87 [» ]
2Z4K X-ray 4.45 T 2-87 [» ]
2Z4M X-ray 4.45 T 2-87 [» ]
3DF1 X-ray 3.50 T 2-87 [» ]
3DF3 X-ray 3.50 T 2-86 [» ]
3E1A electron microscopy - N 1-87 [» ]
3E1C electron microscopy - N 1-87 [» ]
3FIH electron microscopy 6.70 T 3-87 [» ]
3I1M X-ray 3.19 T 1-87 [» ]
3I1O X-ray 3.19 T 1-87 [» ]
3I1Q X-ray 3.81 T 1-87 [» ]
3I1S X-ray 3.81 T 1-87 [» ]
3I1Z X-ray 3.71 T 1-87 [» ]
3I21 X-ray 3.71 T 1-87 [» ]
3IZV electron microscopy - X 1-87 [» ]
3IZW electron microscopy - X 1-87 [» ]
3J00 electron microscopy - T 2-87 [» ]
3J0U electron microscopy 12.10 W 2-87 [» ]
3J0V electron microscopy 14.70 W 2-87 [» ]
3J0X electron microscopy 13.50 W 2-87 [» ]
3J0Z electron microscopy 11.50 W 2-87 [» ]
3J10 electron microscopy 11.50 W 2-87 [» ]
3J13 electron microscopy 13.10 V 2-87 [» ]
3J18 electron microscopy 8.30 T 3-87 [» ]
3J36 electron microscopy 9.80 T 2-87 [» ]
3J4V electron microscopy 12.00 T 3-87 [» ]
3J4W electron microscopy 12.00 T 3-87 [» ]
3J4Y electron microscopy 17.00 T 3-87 [» ]
3J4Z electron microscopy 20.00 T 3-87 [» ]
3J53 electron microscopy 13.00 T 3-87 [» ]
3J55 electron microscopy 15.00 T 3-87 [» ]
3J57 electron microscopy 17.00 T 3-87 [» ]
3J59 electron microscopy 12.00 T 3-87 [» ]
3J5B electron microscopy 17.00 T 3-87 [» ]
3J5D electron microscopy 17.00 T 3-87 [» ]
3J5F electron microscopy 20.00 T 3-87 [» ]
3J5H electron microscopy 15.00 T 3-87 [» ]
3J5J electron microscopy 9.00 T 3-87 [» ]
3J5N electron microscopy 6.80 T 1-87 [» ]
3J5T electron microscopy 7.60 T 2-87 [» ]
3J5X electron microscopy 7.60 T 2-87 [» ]
3KC4 electron microscopy - T 1-87 [» ]
3OAQ X-ray 3.25 T 3-87 [» ]
3OAR X-ray 3.25 T 3-87 [» ]
3OFA X-ray 3.19 T 3-87 [» ]
3OFB X-ray 3.19 T 3-87 [» ]
3OFO X-ray 3.10 T 3-87 [» ]
3OFP X-ray 3.10 T 3-87 [» ]
3OFX X-ray 3.29 T 3-87 [» ]
3OFY X-ray 3.29 T 3-87 [» ]
3OR9 X-ray 3.30 T 1-87 [» ]
3ORA X-ray 3.30 T 1-87 [» ]
3SFS X-ray 3.20 T 1-87 [» ]
3UOQ X-ray 3.70 T 1-87 [» ]
4A2I electron microscopy 16.50 T 3-87 [» ]
4ADV electron microscopy 13.50 T 2-87 [» ]
4GAQ X-ray 3.30 T 1-87 [» ]
4GAS X-ray 3.30 T 1-87 [» ]
4GD1 X-ray 3.00 T 3-87 [» ]
4GD2 X-ray 3.00 T 3-87 [» ]
4KIY X-ray 2.90 T 1-87 [» ]
4KJ0 X-ray 2.90 T 1-87 [» ]
4KJ2 X-ray 2.90 T 1-87 [» ]
4KJ4 X-ray 2.90 T 1-87 [» ]
4KJ6 X-ray 2.90 T 1-87 [» ]
4KJ8 X-ray 2.90 T 1-87 [» ]
4KJA X-ray 2.90 T 1-87 [» ]
4KJC X-ray 2.90 T 1-87 [» ]
ProteinModelPortali P0A7U7.
SMRi P0A7U7. Positions 3-87.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35857N.
IntActi P0A7U7. 57 interactions.
STRINGi 511145.b0023.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7U7.
PRIDEi P0A7U7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73134 ; AAC73134 ; b0023 .
BAB96593 ; BAB96593 ; BAB96593 .
GeneIDi 12931850.
944759.
KEGGi ecj:Y75_p0023.
eco:b0023.
PATRICi 32115137. VBIEscCol129921_0020.

Organism-specific databases

EchoBASEi EB0912.
EcoGenei EG10919. rpsT.

Phylogenomic databases

eggNOGi COG0268.
HOGENOMi HOG000097048.
KOi K02968.
OMAi RHKSNLT.
OrthoDBi EOG6HMXNQ.
PhylomeDBi P0A7U7.

Enzyme and pathway databases

BioCyci EcoCyc:EG10919-MONOMER.
ECOL316407:JW0022-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7U7.
PROi P0A7U7.

Gene expression databases

Genevestigatori P0A7U7.

Family and domain databases

Gene3Di 1.20.58.110. 1 hit.
HAMAPi MF_00500. Ribosomal_S20.
InterProi IPR002583. Ribosomal_S20.
[Graphical view ]
Pfami PF01649. Ribosomal_S20p. 1 hit.
[Graphical view ]
ProDomi PD004231. Ribosomal_S20. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF46992. SSF46992. 1 hit.
TIGRFAMsi TIGR00029. S20. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 96 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