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Protein

30S ribosomal protein S21

Gene

rpsU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciEcoCyc:EG10920-MONOMER.
ECOL316407:JW3037-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
30S ribosomal protein S21
Gene namesi
Name:rpsU
Ordered Locus Names:b3065, JW3037
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10920. rpsU.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 717030S ribosomal protein S21PRO_0000178332Add
BLAST

Proteomic databases

PaxDbiP68679.
PRIDEiP68679.

Interactioni

Protein-protein interaction databases

DIPiDIP-47839N.
IntActiP68679. 23 interactions.
MINTiMINT-1281887.
STRINGi511145.b3065.

Structurei

Secondary structure

1
71
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi19 – 224Combined sources
Turni24 – 274Combined sources
Helixi28 – 325Combined sources
Beta strandi38 – 403Combined sources
Helixi41 – 455Combined sources
Turni46 – 505Combined sources
Helixi51 – 533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YKRelectron microscopy9.80U4-54[»]
3J9Yelectron microscopy3.90u1-71[»]
4A2Ielectron microscopy16.50U4-54[»]
4ADVelectron microscopy13.50U1-71[»]
4U1UX-ray2.95AU/CU4-54[»]
4U1VX-ray3.00AU/CU4-54[»]
4U20X-ray2.90AU/CU4-54[»]
4U24X-ray2.90AU/CU4-54[»]
4U25X-ray2.90AU/CU4-54[»]
4U26X-ray2.80AU/CU4-54[»]
4U27X-ray2.80AU/CU4-54[»]
4V4HX-ray3.46AU/CU1-71[»]
4V4QX-ray3.46AU/CU1-71[»]
4V50X-ray3.22AU/CU2-71[»]
4V52X-ray3.21AU/CU2-71[»]
4V53X-ray3.54AU/CU2-71[»]
4V54X-ray3.30AU/CU2-71[»]
4V55X-ray4.00AU/CU2-71[»]
4V56X-ray3.93AU/CU2-71[»]
4V57X-ray3.50AU/CU2-71[»]
4V5BX-ray3.74BU/DU1-71[»]
4V5Helectron microscopy5.80AU4-54[»]
4V5YX-ray4.45AU/CU2-71[»]
4V64X-ray3.50AU/CU1-71[»]
4V65electron microscopy9.00AQ1-71[»]
4V66electron microscopy9.00AQ1-71[»]
4V69electron microscopy6.70AU4-54[»]
4V6CX-ray3.19AU/CU1-71[»]
4V6DX-ray3.81AU/CU1-71[»]
4V6EX-ray3.71AU/CU1-71[»]
4V6Kelectron microscopy8.25BY1-71[»]
4V6Lelectron microscopy13.20AY1-71[»]
4V6Melectron microscopy7.10AU2-71[»]
4V6Nelectron microscopy12.10BX2-71[»]
4V6Oelectron microscopy14.70AX2-71[»]
4V6Pelectron microscopy13.50AX2-71[»]
4V6Qelectron microscopy11.50AX2-71[»]
4V6Relectron microscopy11.50AX2-71[»]
4V6Selectron microscopy13.10BW2-71[»]
4V6Telectron microscopy8.30AU4-54[»]
4V6Velectron microscopy9.80U2-71[»]
4V6Yelectron microscopy12.00AU4-54[»]
4V6Zelectron microscopy12.00AU4-54[»]
4V70electron microscopy17.00AU4-54[»]
4V71electron microscopy20.00AU4-54[»]
4V72electron microscopy13.00AU4-54[»]
4V73electron microscopy15.00AU4-54[»]
4V74electron microscopy17.00AU4-54[»]
4V75electron microscopy12.00AU4-54[»]
4V76electron microscopy17.00AU4-54[»]
4V77electron microscopy17.00AU4-54[»]
4V78electron microscopy20.00AU4-54[»]
4V79electron microscopy15.00AU4-54[»]
4V7Aelectron microscopy9.00AU4-54[»]
4V7Belectron microscopy6.80AU1-71[»]
4V7Celectron microscopy7.60AU2-71[»]
4V7Delectron microscopy7.60BU2-71[»]
4V7Ielectron microscopy9.60BU1-71[»]
4V7SX-ray3.25AU/CU4-54[»]
4V7TX-ray3.19AU/CU4-54[»]
4V7UX-ray3.10AU/CU4-54[»]
4V7VX-ray3.29AU/CU4-54[»]
4V85X-ray3.20U1-71[»]
4V89X-ray3.70AU1-71[»]
4V9CX-ray3.30AU/CU1-71[»]
4V9DX-ray3.00AU/BU4-54[»]
4V9OX-ray2.90BU/DU/FU/HU1-71[»]
4V9PX-ray2.90BU/DU/FU/HU1-71[»]
4WF1X-ray3.09AU/CU4-54[»]
4WWWX-ray3.10QU/XU4-54[»]
4YBBX-ray2.10AU/BU2-57[»]
5AFIelectron microscopy2.90u1-71[»]
ProteinModelPortaliP68679.
SMRiP68679. Positions 4-54.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68679.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S21P family.Curated

Phylogenomic databases

eggNOGiCOG0828.
HOGENOMiHOG000157460.
InParanoidiP68679.
KOiK02970.
OMAiKRHFKRL.
OrthoDBiEOG6FBX3Z.
PhylomeDBiP68679.

Family and domain databases

HAMAPiMF_00358. Ribosomal_S21.
InterProiIPR001911. Ribosomal_S21.
IPR018278. Ribosomal_S21_CS.
[Graphical view]
PfamiPF01165. Ribosomal_S21. 1 hit.
[Graphical view]
PRINTSiPR00976. RIBOSOMALS21.
ProDomiPD005521. Ribosomal_S21. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR00030. S21p. 1 hit.
PROSITEiPS01181. RIBOSOMAL_S21. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P68679-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVIKVRENE PFDVALRRFK RSCEKAGVLA EVRRREFYEK PTTERKRAKA
60 70
SAVKRHAKKL ARENARRTRL Y
Length:71
Mass (Da):8,500
Last modified:January 23, 2007 - v2
Checksum:iB2E8A18BFBB2F685
GO

Mass spectrometryi

Molecular mass is 8368.8 Da from positions 2 - 71. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA02749. R3EC21.
RefSeqiNP_417537.1. NC_000913.3.
WP_001144069.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC76101; AAC76101; b3065.
BAE77116; BAE77116; BAE77116.
GeneIDi947577.
9732014.
KEGGieco:b3065.
PATRICi32121544. VBIEscCol129921_3159.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA02749. R3EC21.
RefSeqiNP_417537.1. NC_000913.3.
WP_001144069.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YKRelectron microscopy9.80U4-54[»]
3J9Yelectron microscopy3.90u1-71[»]
4A2Ielectron microscopy16.50U4-54[»]
4ADVelectron microscopy13.50U1-71[»]
4U1UX-ray2.95AU/CU4-54[»]
4U1VX-ray3.00AU/CU4-54[»]
4U20X-ray2.90AU/CU4-54[»]
4U24X-ray2.90AU/CU4-54[»]
4U25X-ray2.90AU/CU4-54[»]
4U26X-ray2.80AU/CU4-54[»]
4U27X-ray2.80AU/CU4-54[»]
4V4HX-ray3.46AU/CU1-71[»]
4V4QX-ray3.46AU/CU1-71[»]
4V50X-ray3.22AU/CU2-71[»]
4V52X-ray3.21AU/CU2-71[»]
4V53X-ray3.54AU/CU2-71[»]
4V54X-ray3.30AU/CU2-71[»]
4V55X-ray4.00AU/CU2-71[»]
4V56X-ray3.93AU/CU2-71[»]
4V57X-ray3.50AU/CU2-71[»]
4V5BX-ray3.74BU/DU1-71[»]
4V5Helectron microscopy5.80AU4-54[»]
4V5YX-ray4.45AU/CU2-71[»]
4V64X-ray3.50AU/CU1-71[»]
4V65electron microscopy9.00AQ1-71[»]
4V66electron microscopy9.00AQ1-71[»]
4V69electron microscopy6.70AU4-54[»]
4V6CX-ray3.19AU/CU1-71[»]
4V6DX-ray3.81AU/CU1-71[»]
4V6EX-ray3.71AU/CU1-71[»]
4V6Kelectron microscopy8.25BY1-71[»]
4V6Lelectron microscopy13.20AY1-71[»]
4V6Melectron microscopy7.10AU2-71[»]
4V6Nelectron microscopy12.10BX2-71[»]
4V6Oelectron microscopy14.70AX2-71[»]
4V6Pelectron microscopy13.50AX2-71[»]
4V6Qelectron microscopy11.50AX2-71[»]
4V6Relectron microscopy11.50AX2-71[»]
4V6Selectron microscopy13.10BW2-71[»]
4V6Telectron microscopy8.30AU4-54[»]
4V6Velectron microscopy9.80U2-71[»]
4V6Yelectron microscopy12.00AU4-54[»]
4V6Zelectron microscopy12.00AU4-54[»]
4V70electron microscopy17.00AU4-54[»]
4V71electron microscopy20.00AU4-54[»]
4V72electron microscopy13.00AU4-54[»]
4V73electron microscopy15.00AU4-54[»]
4V74electron microscopy17.00AU4-54[»]
4V75electron microscopy12.00AU4-54[»]
4V76electron microscopy17.00AU4-54[»]
4V77electron microscopy17.00AU4-54[»]
4V78electron microscopy20.00AU4-54[»]
4V79electron microscopy15.00AU4-54[»]
4V7Aelectron microscopy9.00AU4-54[»]
4V7Belectron microscopy6.80AU1-71[»]
4V7Celectron microscopy7.60AU2-71[»]
4V7Delectron microscopy7.60BU2-71[»]
4V7Ielectron microscopy9.60BU1-71[»]
4V7SX-ray3.25AU/CU4-54[»]
4V7TX-ray3.19AU/CU4-54[»]
4V7UX-ray3.10AU/CU4-54[»]
4V7VX-ray3.29AU/CU4-54[»]
4V85X-ray3.20U1-71[»]
4V89X-ray3.70AU1-71[»]
4V9CX-ray3.30AU/CU1-71[»]
4V9DX-ray3.00AU/BU4-54[»]
4V9OX-ray2.90BU/DU/FU/HU1-71[»]
4V9PX-ray2.90BU/DU/FU/HU1-71[»]
4WF1X-ray3.09AU/CU4-54[»]
4WWWX-ray3.10QU/XU4-54[»]
4YBBX-ray2.10AU/BU2-57[»]
5AFIelectron microscopy2.90u1-71[»]
ProteinModelPortaliP68679.
SMRiP68679. Positions 4-54.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47839N.
IntActiP68679. 23 interactions.
MINTiMINT-1281887.
STRINGi511145.b3065.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP68679.
PRIDEiP68679.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76101; AAC76101; b3065.
BAE77116; BAE77116; BAE77116.
GeneIDi947577.
9732014.
KEGGieco:b3065.
PATRICi32121544. VBIEscCol129921_3159.

Organism-specific databases

EchoBASEiEB0913.
EcoGeneiEG10920. rpsU.

Phylogenomic databases

eggNOGiCOG0828.
HOGENOMiHOG000157460.
InParanoidiP68679.
KOiK02970.
OMAiKRHFKRL.
OrthoDBiEOG6FBX3Z.
PhylomeDBiP68679.

Enzyme and pathway databases

BioCyciEcoCyc:EG10920-MONOMER.
ECOL316407:JW3037-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP68679.
PROiP68679.

Family and domain databases

HAMAPiMF_00358. Ribosomal_S21.
InterProiIPR001911. Ribosomal_S21.
IPR018278. Ribosomal_S21_CS.
[Graphical view]
PfamiPF01165. Ribosomal_S21. 1 hit.
[Graphical view]
PRINTSiPR00976. RIBOSOMALS21.
ProDomiPD005521. Ribosomal_S21. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsiTIGR00030. S21p. 1 hit.
PROSITEiPS01181. RIBOSOMAL_S21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRS21_ECOLI
AccessioniPrimary (citable) accession number: P68679
Secondary accession number(s): P02379, Q2M9E0, Q8ZI69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 108 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.