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P68679 (RS21_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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 S21
Gene names
Name:rpsU
Ordered Locus Names:b3065, JW3037
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length71 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein S21P family.

Mass spectrometry

Molecular mass is 8368.8 Da from positions 2 - 71. Determined by MALDI. Ref.7

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 717030S ribosomal protein S21 HAMAP-Rule MF_00358
PRO_0000178332

Secondary structure

.............. 71
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68679 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B2E8A18BFBB2F685

FASTA718,500
        10         20         30         40         50         60 
MPVIKVRENE PFDVALRRFK RSCEKAGVLA EVRRREFYEK PTTERKRAKA SAVKRHAKKL 

        70 
ARENARRTRL Y 

« Hide

References

« Hide 'large scale' references
[1]"The operon that encodes the sigma subunit of RNA polymerase also encodes ribosomal protein S21 and DNA primase in E. coli K12."
Burton Z.F., Gross C.A., Watanabe K.K., Burgess R.R.
Cell 32:335-349(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Regulation of the rpsU-dnaG-rpoD macromolecular synthesis operon and the initiation of DNA replication in Escherichia coli K-12."
Lupski J.R., Smiley B.L., Godson G.N.
Mol. Gen. Genet. 189:48-57(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[3]"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.
[4]"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.
[5]"Determination of the complete amino acid sequence of protein S21 from Escherichia coli ribosomes."
Vandekerckhove J., Rombauts W., Peeters B., Wittmann-Liebold B.
Hoppe-Seyler's Z. Physiol. Chem. 356:1955-1976(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-71.
Strain: K.
[6]"Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-35, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[7]"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.
[8]"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
J01687 Genomic DNA. Translation: AAA24599.1.
V00346 Genomic DNA. Translation: CAA23635.1.
U28379 Genomic DNA. Translation: AAA89145.1.
U00096 Genomic DNA. Translation: AAC76101.1.
AP009048 Genomic DNA. Translation: BAE77116.1.
PIRR3EC21. A02749.
RefSeqNP_417537.1. NC_000913.3.
YP_491257.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VS5X-ray3.46U1-71[»]
1VS7X-ray3.46U1-71[»]
2AVYX-ray3.46U1-71[»]
2AW7X-ray3.46U1-71[»]
2I2PX-ray3.22U2-71[»]
2I2UX-ray3.22U2-71[»]
2QALX-ray3.21U2-71[»]
2QANX-ray3.21U2-71[»]
2QB9X-ray3.54U2-71[»]
2QBBX-ray3.54U2-71[»]
2QBDX-ray3.30U2-71[»]
2QBFX-ray3.30U2-71[»]
2QBHX-ray4.00U2-71[»]
2QBJX-ray4.00U2-71[»]
2QOUX-ray3.93U2-71[»]
2QOWX-ray3.93U2-71[»]
2QOYX-ray3.50U2-71[»]
2QP0X-ray3.50U2-71[»]
2VHOX-ray3.74U1-71[»]
2VHPX-ray3.74U1-71[»]
2WWLelectron microscopy5.80U4-54[»]
2YKRelectron microscopy9.80U4-54[»]
2Z4KX-ray4.45U2-71[»]
2Z4MX-ray4.45U2-71[»]
3DF1X-ray3.50U1-71[»]
3DF3X-ray3.50U1-71[»]
3E1Aelectron microscopy-Q1-71[»]
3E1Celectron microscopy-Q1-71[»]
3FIHelectron microscopy6.70U4-54[»]
3I1MX-ray3.19U1-71[»]
3I1OX-ray3.19U1-71[»]
3I1QX-ray3.81U1-71[»]
3I1SX-ray3.81U1-71[»]
3I1ZX-ray3.71U1-71[»]
3I21X-ray3.71U1-71[»]
3IZVelectron microscopy-Y1-71[»]
3IZWelectron microscopy-Y1-71[»]
3J00electron microscopy-U2-71[»]
3J0Uelectron microscopy12.10X2-71[»]
3J0Velectron microscopy14.70X2-71[»]
3J0Xelectron microscopy13.50X2-71[»]
3J0Zelectron microscopy11.50X2-71[»]
3J10electron microscopy11.50X2-71[»]
3J13electron microscopy13.10W2-71[»]
3J18electron microscopy8.30U4-54[»]
3J36electron microscopy9.80U2-71[»]
3J4Velectron microscopy12.00U4-54[»]
3J4Welectron microscopy12.00U4-54[»]
3J4Yelectron microscopy17.00U4-54[»]
3J4Zelectron microscopy20.00U4-54[»]
3J53electron microscopy13.00U4-54[»]
3J55electron microscopy15.00U4-54[»]
3J57electron microscopy17.00U4-54[»]
3J59electron microscopy12.00U4-54[»]
3J5Belectron microscopy17.00U4-54[»]
3J5Delectron microscopy17.00U4-54[»]
3J5Felectron microscopy20.00U4-54[»]
3J5Helectron microscopy15.00U4-54[»]
3J5Jelectron microscopy9.00U4-54[»]
3J5Nelectron microscopy6.80U1-71[»]
3J5Telectron microscopy7.60U2-71[»]
3J5Xelectron microscopy7.60U2-71[»]
3KC4electron microscopy-U1-71[»]
3OAQX-ray3.25U4-54[»]
3OARX-ray3.25U4-54[»]
3OFAX-ray3.19U4-54[»]
3OFBX-ray3.19U4-54[»]
3OFOX-ray3.10U4-54[»]
3OFPX-ray3.10U4-54[»]
3OFXX-ray3.29U4-54[»]
3OFYX-ray3.29U4-54[»]
3OR9X-ray3.30U1-71[»]
3ORAX-ray3.30U1-71[»]
3SFSX-ray3.20U1-71[»]
3UOQX-ray3.70U1-71[»]
4A2Ielectron microscopy16.50U4-54[»]
4ADVelectron microscopy13.50U1-71[»]
4GAQX-ray3.30U1-71[»]
4GASX-ray3.30U1-71[»]
4GD1X-ray3.00U4-54[»]
4GD2X-ray3.00U4-54[»]
4KIYX-ray2.90U1-71[»]
4KJ0X-ray2.90U1-71[»]
4KJ2X-ray2.90U1-71[»]
4KJ4X-ray2.90U1-71[»]
4KJ6X-ray2.90U1-71[»]
4KJ8X-ray2.90U1-71[»]
4KJAX-ray2.90U1-71[»]
4KJCX-ray2.90U1-71[»]
ProteinModelPortalP68679.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47839N.
IntActP68679. 23 interactions.
MINTMINT-1281887.
STRING511145.b3065.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP68679.
PRIDEP68679.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76101; AAC76101; b3065.
BAE77116; BAE77116; BAE77116.
GeneID12933220.
947577.
KEGGecj:Y75_p2991.
eco:b3065.
PATRIC32121544. VBIEscCol129921_3159.

Organism-specific databases

EchoBASEEB0913.
EcoGeneEG10920. rpsU.

Phylogenomic databases

eggNOGCOG0828.
HOGENOMHOG000157460.
KOK02970.
OMARNCAKAG.
OrthoDBEOG6FBX3Z.
PhylomeDBP68679.

Enzyme and pathway databases

BioCycEcoCyc:EG10920-MONOMER.
ECOL316407:JW3037-MONOMER.

Gene expression databases

GenevestigatorP68679.

Family and domain databases

HAMAPMF_00358. Ribosomal_S21.
InterProIPR001911. Ribosomal_S21.
IPR018278. Ribosomal_S21_CS.
[Graphical view]
PfamPF01165. Ribosomal_S21. 1 hit.
[Graphical view]
PRINTSPR00976. RIBOSOMALS21.
ProDomPD005521. Ribosomal_S21. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00030. S21p. 1 hit.
PROSITEPS01181. RIBOSOMAL_S21. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP68679.
PROP68679.

Entry information

Entry nameRS21_ECOLI
AccessionPrimary (citable) accession number: P68679
Secondary accession number(s): P02379, Q2M9E0, Q8ZI69
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 97 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