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P0AG48 (RL21_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. 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:
50S ribosomal protein L21
Gene names
Name:rplU
Ordered Locus Names:b3186, JW3153
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length103 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein binds to 23S rRNA in the presence of protein L20. HAMAP MF_01363

Subunit structure

Part of the 50S ribosomal subunit. Contacts protein L20.

Sequence similarities

Belongs to the ribosomal protein L21P family.

Mass spectrometry

Molecular mass is 11562.7 Da from positions 1 - 103. Determined by MALDI. Ref.8

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10310350S ribosomal protein L21 HAMAP MF_01363
PRO_0000181000

Secondary structure

......... 103
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AG48 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 9221F104EC9C8CDB

FASTA10311,564
        10         20         30         40         50         60 
MYAVFQSGGK QHRVSEGQTV RLEKLDIATG ETVEFAEVLM IANGEEVKIG VPFVDGGVIK 

        70         80         90        100 
AEVVAHGRGE KVKIVKFRRR KHYRKQQGHR QWFTDVKITG ISA 

« Hide

References

« Hide 'large scale' references
[1]"Amino acid sequence of the ribosomal protein L21 of Escherichia coli."
Heiland I., Wittmann-Liebold B.
Biochemistry 18:4605-4612(1979) [PubMed: 387076] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli."
Jeong J.H., Kitakawa M.S., Isono S., Isono K.
DNA Seq. 4:59-67(1993) [PubMed: 8312607] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.
Submitted (SEP-1994) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-13.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29."
Wower I., Wower J., Meinke M., Brimacombe R.
Nucleic Acids Res. 9:4285-4302(1981) [PubMed: 6170935] [Abstract]
Cited for: CROSS-LINKING TO 23S RRNA.
Strain: MRE-600.
[7]"Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
Biochemistry 28:4099-4105(1989) [PubMed: 2665813] [Abstract]
Cited for: CROSS-LINKING TO L20.
[8]"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: 10094780] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[9]"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: 16272117] [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
D13267 Genomic DNA. Translation: BAA02525.1.
U18997 Genomic DNA. Translation: AAA57987.1.
U00096 Genomic DNA. Translation: AAC76218.1.
AP009048 Genomic DNA. Translation: BAE77230.1.
PIRR5EC21. JS0766.
RefSeqNP_417653.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VS6X-ray3.46R1-103[»]
1VS8X-ray3.46R1-103[»]
1VT2X-ray3.30R1-103[»]
2AW4X-ray3.46R1-103[»]
2AWBX-ray3.46R1-103[»]
2I2TX-ray3.22R1-103[»]
2I2VX-ray3.22R1-103[»]
2J28electron microscopy8.00R1-103[»]
2QAMX-ray3.21R1-103[»]
2QAOX-ray3.21R1-103[»]
2QBAX-ray3.54R1-103[»]
2QBCX-ray3.54R1-103[»]
2QBEX-ray3.30R1-103[»]
2QBGX-ray3.30R1-103[»]
2QBIX-ray4.00R1-103[»]
2QBKX-ray4.00R1-103[»]
2QOVX-ray3.93R1-103[»]
2QOXX-ray3.93R1-103[»]
2QOZX-ray3.50R1-103[»]
2QP1X-ray3.50R1-103[»]
2RDOelectron microscopy9.10R1-103[»]
2WWQelectron microscopy5.80R1-103[»]
2Z4LX-ray4.45R1-103[»]
2Z4NX-ray4.45R1-103[»]
3BBXelectron microscopy10.00R1-103[»]
3E1Belectron microscopy-K1-103[»]
3E1Delectron microscopy-K1-103[»]
3FIKelectron microscopy6.70R1-103[»]
3I1NX-ray3.19R1-103[»]
3I1PX-ray3.19R1-103[»]
3I1RX-ray3.81R1-103[»]
3I1TX-ray3.81R1-103[»]
3I20X-ray3.71R1-103[»]
3I22X-ray3.71R1-103[»]
3IZTelectron microscopy-S1-103[»]
3IZUelectron microscopy-S1-103[»]
3J01electron microscopy-R1-103[»]
3KCRelectron microscopy-R1-103[»]
3OASX-ray3.25R1-103[»]
3OATX-ray3.25R1-103[»]
3OFCX-ray3.19R1-103[»]
3OFDX-ray3.19R1-103[»]
3OFQX-ray3.10R1-103[»]
3OFRX-ray3.10R1-103[»]
3OFZX-ray3.29R1-103[»]
3OG0X-ray3.29R1-103[»]
3ORBX-ray3.30R1-103[»]
3R8SX-ray3.00R1-103[»]
3R8TX-ray3.00R1-103[»]
ProteinModelPortalP0AG48.
SMRP0AG48. Positions 1-103.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47852N.
IntActP0AG48. 80 interactions.
MINTMINT-1280768.

2D gel databases

SWISS-2DPAGEP0AG48.
ECO2DBASEI013.2. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000003884; EBESCP00000003884; EBESCG00000003176.
EBESCT00000017503; EBESCP00000016794; EBESCG00000016559.
GeneID949057.
GenomeReviewsGene locus JW3153 in contig AP009048_GR.
Gene locus b3186 in contig U00096_GR.
KEGGecj:JW3153.
eco:b3186.
PATRIC32121792. VBIEscCol129921_3280.

Organism-specific databases

EchoBASEEB4295.
EcoGeneEG50001. rplU.

Phylogenomic databases

eggNOGCOG0261.
GeneTreeEBGT00050000010507.
HOGENOMHBG706775.
OMAIKVEQIA.
PhylomeDBP0AG48.
ProtClustDBPRK05573.

Enzyme and pathway databases

BioCycEcoCyc:EG50001-MONOMER.

Gene expression databases

GenevestigatorP0AG48.

Family and domain databases

HAMAPMF_01363. Ribosomal_L21.
[Tree]
InterProIPR001787. Ribosomal_L21.
IPR018258. Ribosomal_L21_CS.
[Graphical view]
KOK02888.
PANTHERPTHR21349. Ribosomal_L21p. 1 hit.
PfamPF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
TIGRFAMsTIGR00061. L21. 1 hit.
PROSITEPS01169. RIBOSOMAL_L21. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRL21_ECOLI
AccessionPrimary (citable) accession number: P0AG48
Secondary accession number(s): P02422, Q2M926
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 25, 2012
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families