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P68679

- RS21_ECOLI

UniProt

P68679 - RS21_ECOLI

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Protein

30S ribosomal protein S21

Gene

rpsU

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

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
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: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10920. rpsU.

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 – 717030S ribosomal protein S21PRO_0000178332Add
BLAST

Proteomic databases

PaxDbiP68679.
PRIDEiP68679.

Expressioni

Gene expression databases

GenevestigatoriP68679.

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
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[»]
4PE9X-ray2.95U4-54[»]
4PEAX-ray2.95U4-54[»]
4TOLX-ray3.00U4-54[»]
4TONX-ray3.00U4-54[»]
4TOUX-ray2.90U4-54[»]
4TOWX-ray2.90U4-54[»]
4TP0X-ray2.90U4-54[»]
4TP2X-ray2.90U4-54[»]
4TP4X-ray2.90U4-54[»]
4TP6X-ray2.90U4-54[»]
4TP8X-ray2.80U4-54[»]
4TPAX-ray2.80U4-54[»]
4TPCX-ray2.80U4-54[»]
4TPEX-ray2.80U4-54[»]
ProteinModelPortaliP68679.
SMRiP68679. Positions 2-71.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68679.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S21P family.Curated

Phylogenomic databases

eggNOGiCOG0828.
HOGENOMiHOG000157460.
InParanoidiP68679.
KOiK02970.
OMAiRNCAKAG.
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.
YP_491257.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76101; AAC76101; b3065.
BAE77116; BAE77116; BAE77116.
GeneIDi12933220.
947577.
KEGGiecj:Y75_p2991.
eco: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 .
PIRi A02749. R3EC21.
RefSeqi NP_417537.1. NC_000913.3.
YP_491257.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VS5 X-ray 3.46 U 1-71 [» ]
1VS7 X-ray 3.46 U 1-71 [» ]
2AVY X-ray 3.46 U 1-71 [» ]
2AW7 X-ray 3.46 U 1-71 [» ]
2I2P X-ray 3.22 U 2-71 [» ]
2I2U X-ray 3.22 U 2-71 [» ]
2QAL X-ray 3.21 U 2-71 [» ]
2QAN X-ray 3.21 U 2-71 [» ]
2QB9 X-ray 3.54 U 2-71 [» ]
2QBB X-ray 3.54 U 2-71 [» ]
2QBD X-ray 3.30 U 2-71 [» ]
2QBF X-ray 3.30 U 2-71 [» ]
2QBH X-ray 4.00 U 2-71 [» ]
2QBJ X-ray 4.00 U 2-71 [» ]
2QOU X-ray 3.93 U 2-71 [» ]
2QOW X-ray 3.93 U 2-71 [» ]
2QOY X-ray 3.50 U 2-71 [» ]
2QP0 X-ray 3.50 U 2-71 [» ]
2VHO X-ray 3.74 U 1-71 [» ]
2VHP X-ray 3.74 U 1-71 [» ]
2WWL electron microscopy 5.80 U 4-54 [» ]
2YKR electron microscopy 9.80 U 4-54 [» ]
2Z4K X-ray 4.45 U 2-71 [» ]
2Z4M X-ray 4.45 U 2-71 [» ]
3DF1 X-ray 3.50 U 1-71 [» ]
3DF3 X-ray 3.50 U 1-71 [» ]
3E1A electron microscopy - Q 1-71 [» ]
3E1C electron microscopy - Q 1-71 [» ]
3FIH electron microscopy 6.70 U 4-54 [» ]
3I1M X-ray 3.19 U 1-71 [» ]
3I1O X-ray 3.19 U 1-71 [» ]
3I1Q X-ray 3.81 U 1-71 [» ]
3I1S X-ray 3.81 U 1-71 [» ]
3I1Z X-ray 3.71 U 1-71 [» ]
3I21 X-ray 3.71 U 1-71 [» ]
3IZV electron microscopy - Y 1-71 [» ]
3IZW electron microscopy - Y 1-71 [» ]
3J00 electron microscopy - U 2-71 [» ]
3J0U electron microscopy 12.10 X 2-71 [» ]
3J0V electron microscopy 14.70 X 2-71 [» ]
3J0X electron microscopy 13.50 X 2-71 [» ]
3J0Z electron microscopy 11.50 X 2-71 [» ]
3J10 electron microscopy 11.50 X 2-71 [» ]
3J13 electron microscopy 13.10 W 2-71 [» ]
3J18 electron microscopy 8.30 U 4-54 [» ]
3J36 electron microscopy 9.80 U 2-71 [» ]
3J4V electron microscopy 12.00 U 4-54 [» ]
3J4W electron microscopy 12.00 U 4-54 [» ]
3J4Y electron microscopy 17.00 U 4-54 [» ]
3J4Z electron microscopy 20.00 U 4-54 [» ]
3J53 electron microscopy 13.00 U 4-54 [» ]
3J55 electron microscopy 15.00 U 4-54 [» ]
3J57 electron microscopy 17.00 U 4-54 [» ]
3J59 electron microscopy 12.00 U 4-54 [» ]
3J5B electron microscopy 17.00 U 4-54 [» ]
3J5D electron microscopy 17.00 U 4-54 [» ]
3J5F electron microscopy 20.00 U 4-54 [» ]
3J5H electron microscopy 15.00 U 4-54 [» ]
3J5J electron microscopy 9.00 U 4-54 [» ]
3J5N electron microscopy 6.80 U 1-71 [» ]
3J5T electron microscopy 7.60 U 2-71 [» ]
3J5X electron microscopy 7.60 U 2-71 [» ]
3KC4 electron microscopy - U 1-71 [» ]
3OAQ X-ray 3.25 U 4-54 [» ]
3OAR X-ray 3.25 U 4-54 [» ]
3OFA X-ray 3.19 U 4-54 [» ]
3OFB X-ray 3.19 U 4-54 [» ]
3OFO X-ray 3.10 U 4-54 [» ]
3OFP X-ray 3.10 U 4-54 [» ]
3OFX X-ray 3.29 U 4-54 [» ]
3OFY X-ray 3.29 U 4-54 [» ]
3OR9 X-ray 3.30 U 1-71 [» ]
3ORA X-ray 3.30 U 1-71 [» ]
3SFS X-ray 3.20 U 1-71 [» ]
3UOQ X-ray 3.70 U 1-71 [» ]
4A2I electron microscopy 16.50 U 4-54 [» ]
4ADV electron microscopy 13.50 U 1-71 [» ]
4GAQ X-ray 3.30 U 1-71 [» ]
4GAS X-ray 3.30 U 1-71 [» ]
4GD1 X-ray 3.00 U 4-54 [» ]
4GD2 X-ray 3.00 U 4-54 [» ]
4KIY X-ray 2.90 U 1-71 [» ]
4KJ0 X-ray 2.90 U 1-71 [» ]
4KJ2 X-ray 2.90 U 1-71 [» ]
4KJ4 X-ray 2.90 U 1-71 [» ]
4KJ6 X-ray 2.90 U 1-71 [» ]
4KJ8 X-ray 2.90 U 1-71 [» ]
4KJA X-ray 2.90 U 1-71 [» ]
4KJC X-ray 2.90 U 1-71 [» ]
4PE9 X-ray 2.95 U 4-54 [» ]
4PEA X-ray 2.95 U 4-54 [» ]
4TOL X-ray 3.00 U 4-54 [» ]
4TON X-ray 3.00 U 4-54 [» ]
4TOU X-ray 2.90 U 4-54 [» ]
4TOW X-ray 2.90 U 4-54 [» ]
4TP0 X-ray 2.90 U 4-54 [» ]
4TP2 X-ray 2.90 U 4-54 [» ]
4TP4 X-ray 2.90 U 4-54 [» ]
4TP6 X-ray 2.90 U 4-54 [» ]
4TP8 X-ray 2.80 U 4-54 [» ]
4TPA X-ray 2.80 U 4-54 [» ]
4TPC X-ray 2.80 U 4-54 [» ]
4TPE X-ray 2.80 U 4-54 [» ]
ProteinModelPortali P68679.
SMRi P68679. Positions 2-71.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47839N.
IntActi P68679. 23 interactions.
MINTi MINT-1281887.
STRINGi 511145.b3065.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P68679.
PRIDEi P68679.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76101 ; AAC76101 ; b3065 .
BAE77116 ; BAE77116 ; BAE77116 .
GeneIDi 12933220.
947577.
KEGGi ecj:Y75_p2991.
eco:b3065.
PATRICi 32121544. VBIEscCol129921_3159.

Organism-specific databases

EchoBASEi EB0913.
EcoGenei EG10920. rpsU.

Phylogenomic databases

eggNOGi COG0828.
HOGENOMi HOG000157460.
InParanoidi P68679.
KOi K02970.
OMAi RNCAKAG.
OrthoDBi EOG6FBX3Z.
PhylomeDBi P68679.

Enzyme and pathway databases

BioCyci EcoCyc:EG10920-MONOMER.
ECOL316407:JW3037-MONOMER.

Miscellaneous databases

EvolutionaryTracei P68679.
PROi P68679.

Gene expression databases

Genevestigatori P68679.

Family and domain databases

HAMAPi MF_00358. Ribosomal_S21.
InterProi IPR001911. Ribosomal_S21.
IPR018278. Ribosomal_S21_CS.
[Graphical view ]
Pfami PF01165. Ribosomal_S21. 1 hit.
[Graphical view ]
PRINTSi PR00976. RIBOSOMALS21.
ProDomi PD005521. Ribosomal_S21. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
TIGRFAMsi TIGR00030. S21p. 1 hit.
PROSITEi PS01181. RIBOSOMAL_S21. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
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