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P0A7U7 (RS20_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
30S ribosomal protein S20
Gene names
Name:rpsT
Ordered Locus Names:b0023, JW0022
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length87 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds directly to 16S ribosomal RNA. HAMAP-Rule MF_00500

Sequence similarities

Belongs to the ribosomal protein S20P family.

Mass spectrometry

Molecular mass is 9553.6 Da from positions 2 - 87. Determined by MALDI. Ref.9

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 878630S ribosomal protein S20 HAMAP-Rule MF_00500
PRO_0000167958

Experimental info

Sequence conflict381A → R in AAA24604. Ref.2

Secondary structure

.......... 87
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7U7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F02154BE2D1E22D9

FASTA879,684
        10         20         30         40         50         60 
MANIKSAKKR AIQSEKARKH NASRRSMMRT FIKKVYAAIE AGDKAAAQKA FNEMQPIVDR 

        70         80 
QAAKGLIHKN KAARHKANLT AQINKLA 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Structures of the bacterial ribosome at 3.5 A resolution."
Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D.
Science 310:827-834(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
Strain: MRE-600.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M10428 Genomic DNA. Translation: AAA24604.1.
X04382 Genomic DNA. Translation: CAA27968.1.
U00096 Genomic DNA. Translation: AAC73134.1.
AP009048 Genomic DNA. Translation: BAB96593.1.
PIRR3EC20. A30425.
RefSeqNP_414564.1. NC_000913.3.
YP_488329.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0A7U7.
SMRP0A7U7. Positions 3-87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35857N.
IntActP0A7U7. 57 interactions.
STRING511145.b0023.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7U7.
PRIDEP0A7U7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73134; AAC73134; b0023.
BAB96593; BAB96593; BAB96593.
GeneID12931850.
944759.
KEGGecj:Y75_p0023.
eco:b0023.
PATRIC32115137. VBIEscCol129921_0020.

Organism-specific databases

EchoBASEEB0912.
EcoGeneEG10919. rpsT.

Phylogenomic databases

eggNOGCOG0268.
HOGENOMHOG000097048.
KOK02968.
OMARHKSNLT.
OrthoDBEOG6HMXNQ.
PhylomeDBP0A7U7.

Enzyme and pathway databases

BioCycEcoCyc:EG10919-MONOMER.
ECOL316407:JW0022-MONOMER.

Gene expression databases

GenevestigatorP0A7U7.

Family and domain databases

Gene3D1.20.58.110. 1 hit.
HAMAPMF_00500. Ribosomal_S20.
InterProIPR002583. Ribosomal_S20.
[Graphical view]
PfamPF01649. Ribosomal_S20p. 1 hit.
[Graphical view]
ProDomPD004231. Ribosomal_S20. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF46992. SSF46992. 1 hit.
TIGRFAMsTIGR00029. S20. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A7U7.
PROP0A7U7.

Entry information

Entry nameRS20_ECOLI
AccessionPrimary (citable) accession number: P0A7U7
Secondary accession number(s): P02378
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene