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P0AG48 (RL21_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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) [Reference proteome] [HAMAP]
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-Rule 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.9

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10310350S ribosomal protein L21 HAMAP-Rule 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] [Europe PMC] [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] [Europe PMC] [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 277:1453-1462(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]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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO L20.
[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]"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
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_000913.3.
YP_491371.1. NC_007779.1.

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[»]
3J0Telectron microscopy12.10T1-103[»]
3J0Welectron microscopy14.70T1-103[»]
3J0Yelectron microscopy13.50T1-103[»]
3J11electron microscopy13.10T1-103[»]
3J12electron microscopy11.50T1-103[»]
3J14electron microscopy11.50T1-103[»]
3J19electron microscopy8.30R1-103[»]
3J37electron microscopy9.80V1-103[»]
3J4Xelectron microscopy12.00R1-103[»]
3J50electron microscopy20.00R1-103[»]
3J51electron microscopy17.00R1-103[»]
3J52electron microscopy12.00R1-103[»]
3J54electron microscopy13.00R1-103[»]
3J56electron microscopy15.00R1-103[»]
3J58electron microscopy17.00R1-103[»]
3J5Aelectron microscopy12.00R1-103[»]
3J5Celectron microscopy17.00R1-103[»]
3J5Eelectron microscopy17.00R1-103[»]
3J5Gelectron microscopy20.00R1-103[»]
3J5Ielectron microscopy15.00R1-103[»]
3J5Kelectron microscopy9.00R1-103[»]
3J5Oelectron microscopy6.80R1-103[»]
3J5Uelectron microscopy7.60T1-103[»]
3J5Welectron microscopy7.60U1-103[»]
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[»]
3SGFX-ray3.20V1-103[»]
3UOSX-ray3.70V1-103[»]
4GARX-ray3.30R1-103[»]
4GAUX-ray3.30R1-103[»]
4KIXX-ray2.90R1-103[»]
4KIZX-ray2.90R1-103[»]
4KJ1X-ray2.90R1-103[»]
4KJ3X-ray2.90R1-103[»]
4KJ5X-ray2.90R1-103[»]
4KJ7X-ray2.90R1-103[»]
4KJ9X-ray2.90R1-103[»]
4KJBX-ray2.90R1-103[»]
ProteinModelPortalP0AG48.
SMRP0AG48. Positions 1-103.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47852N.
IntActP0AG48. 81 interactions.
MINTMINT-1280768.
STRING511145.b3186.

Chemistry

ChEMBLCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP0AG48.

Proteomic databases

PaxDbP0AG48.
PRIDEP0AG48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76218; AAC76218; b3186.
BAE77230; BAE77230; BAE77230.
GeneID12932080.
949057.
KEGGecj:Y75_p3106.
eco:b3186.
PATRIC32121792. VBIEscCol129921_3280.

Organism-specific databases

EchoBASEEB4295.
EcoGeneEG50001. rplU.

Phylogenomic databases

eggNOGCOG0261.
HOGENOMHOG000036265.
KOK02888.
OMAQGHRQPF.
OrthoDBEOG6TJ84X.
ProtClustDBPRK05573.

Enzyme and pathway databases

BioCycEcoCyc:EG50001-MONOMER.
ECOL316407:JW3153-MONOMER.

Gene expression databases

GenevestigatorP0AG48.

Family and domain databases

HAMAPMF_01363. Ribosomal_L21.
InterProIPR028909. L21p-like.
IPR001787. Ribosomal_L21.
IPR018258. Ribosomal_L21_CS.
[Graphical view]
PfamPF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
SUPFAMSSF141091. SSF141091. 1 hit.
TIGRFAMsTIGR00061. L21. 1 hit.
PROSITEPS01169. RIBOSOMAL_L21. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AG48.
PROP0AG48.

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: April 16, 2014
This is version 82 of the entry and version 1 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