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P60422 (RL2_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L2
Gene names
Name:rplB
Ordered Locus Names:b3317, JW3279
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial. HAMAP-Rule MF_01320_B

In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, Ref.15); these contacts are broken in the model with bound EF-G. HAMAP-Rule MF_01320_B

Subunit structure

Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Interacts weakly with S6 in one of the 3.5 A resolved structures. Ref.6 Ref.11 Ref.15

Miscellaneous

This protein can be partially replaced in vivo by its H.marismortui (HmaL2) or human (L8, from the 60S cytoplasmic ribosome) homolog.

Sequence similarities

Belongs to the ribosomal protein L2P family.

Mass spectrometry

Molecular mass is 29732.3 Da from positions 2 - 273. Determined by MALDI. Ref.12

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 27327250S ribosomal protein L2 HAMAP-Rule MF_01320_B
PRO_0000129559

Amino acid modifications

Modified residue2421N6-acetyllysine Ref.13

Experimental info

Mutagenesis2301H → Q: Loss of peptidyltransferase activity in reconstituted ribosomes. No change in rRNA binding or assembly into ribosomes. Ref.7 Ref.10
Sequence conflict232 – 2354HGGG → GGGH AA sequence Ref.4

Secondary structure

.................................................................................. 273
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60422 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 1010BDE8D8C68B9B

FASTA27329,860
        10         20         30         40         50         60 
MAVVKCKPTS PGRRHVVKVV NPELHKGKPF APLLEKNSKS GGRNNNGRIT TRHIGGGHKQ 

        70         80         90        100        110        120 
AYRIVDFKRN KDGIPAVVER LEYDPNRSAN IALVLYKDGE RRYILAPKGL KAGDQIQSGV 

       130        140        150        160        170        180 
DAAIKPGNTL PMRNIPVGST VHNVEMKPGK GGQLARSAGT YVQIVARDGA YVTLRLRSGE 

       190        200        210        220        230        240 
MRKVEADCRA TLGEVGNAEH MLRVLGKAGA ARWRGVRPTV RGTAMNPVDH PHGGGEGRNF 

       250        260        270 
GKHPVTPWGV QTKGKKTRSN KRTDKFIVRR RSK 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the Escherichia coli S10 ribosomal protein operon."
Zurawski G., Zurawski S.M.
Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[3]"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.
[4]"The primary structure of protein L2 from the Escherichia coli ribosome."
Kimura M., Mende L., Wittmann-Liebold B.
FEBS Lett. 149:304-312(1982)
Cited for: PROTEIN SEQUENCE OF 2-273.
[5]"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 60-71 AND 200-208, CROSS-LINKING TO RRNA.
Strain: MRE-600.
[6]"Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
Herold M., Nierhaus K.H.
J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
Strain: K12.
[7]"Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity."
Cooperman B.S., Wooten T., Romero D.P., Traut R.R.
Biochem. Cell Biol. 73:1087-1094(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-230.
[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]"Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies."
Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.
Biochem. J. 331:423-430(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN REPLACEMENT STUDIES.
[10]"Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer."
Diedrich G., Spahn C.M.T., Stelzl U., Schaefer M.A., Wooten T., Bochkariov D.E., Cooperman B.S., Traut R.R., Nierhaus K.H.
EMBO J. 19:5241-5250(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REQUIREMENT FOR 70S RIBOSOME FORMATION, TRNA-BINDING, MUTAGENESIS OF CONSERVED RESIDUES.
[11]"Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome."
Willumeit R., Forthmann S., Beckmann J., Diedrich G., Ratering R., Stuhrmann H.B., Nierhaus K.H.
J. Mol. Biol. 305:167-177(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: POSITION IN THE 50S SUBUNIT AND 70S RIBOSOME.
Strain: MRE-600.
[12]"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.
[13]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-242, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[14]"The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[15]"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), INTERSUBUNIT BRIDGE FORMATION.
Strain: MRE-600.
[16]"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
X02613 Genomic DNA. Translation: CAA26463.1.
U18997 Genomic DNA. Translation: AAA58114.1.
U00096 Genomic DNA. Translation: AAC76342.1.
AP009048 Genomic DNA. Translation: BAE77974.1.
PIRR5EC2. E23129.
RefSeqNP_417776.1. NC_000913.3.
YP_492115.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30A2-273[»]
1P86electron microscopy11.50A2-273[»]
1VS6X-ray3.46C1-273[»]
1VS8X-ray3.46C1-273[»]
1VT2X-ray3.30C1-273[»]
2AW4X-ray3.46C1-273[»]
2AWBX-ray3.46C1-273[»]
2GYAelectron microscopy15.00A39-264[»]
2GYCelectron microscopy15.00A39-265[»]
2I2TX-ray3.22C2-272[»]
2I2VX-ray3.22C2-272[»]
2J28electron microscopy8.00C4-270[»]
2QAMX-ray3.21C2-273[»]
2QAOX-ray3.21C2-273[»]
2QBAX-ray3.54C2-273[»]
2QBCX-ray3.54C2-273[»]
2QBEX-ray3.30C2-273[»]
2QBGX-ray3.30C2-273[»]
2QBIX-ray4.00C2-273[»]
2QBKX-ray4.00C2-273[»]
2QOVX-ray3.93C2-273[»]
2QOXX-ray3.93C2-273[»]
2QOZX-ray3.50C2-273[»]
2QP1X-ray3.50C2-273[»]
2RDOelectron microscopy9.10C2-273[»]
2VHMX-ray3.74C1-273[»]
2VHNX-ray3.74C1-273[»]
2WWQelectron microscopy5.80C2-272[»]
2Z4LX-ray4.45C2-273[»]
2Z4NX-ray4.45C2-273[»]
3BBXelectron microscopy10.00C1-273[»]
3DF2X-ray3.50C1-273[»]
3DF4X-ray3.50C1-273[»]
3E1Belectron microscopy-N1-270[»]
3E1Delectron microscopy-N1-270[»]
3FIKelectron microscopy6.70C2-272[»]
3I1NX-ray3.19C1-273[»]
3I1PX-ray3.19C1-273[»]
3I1RX-ray3.81C1-273[»]
3I1TX-ray3.81C1-273[»]
3I20X-ray3.71C1-273[»]
3I22X-ray3.71C1-273[»]
3IZTelectron microscopy-D1-273[»]
3IZUelectron microscopy-D1-273[»]
3J01electron microscopy-62-273[»]
3J0Telectron microscopy12.10D2-272[»]
3J0Welectron microscopy14.70D2-272[»]
3J0Yelectron microscopy13.50D2-272[»]
3J11electron microscopy13.10D2-272[»]
3J12electron microscopy11.50D2-272[»]
3J14electron microscopy11.50D2-272[»]
3J19electron microscopy8.30C2-272[»]
3J37electron microscopy9.80D2-273[»]
3J4Xelectron microscopy12.00C1-272[»]
3J50electron microscopy20.00C1-272[»]
3J51electron microscopy17.00C1-272[»]
3J52electron microscopy12.00C1-272[»]
3J54electron microscopy13.00C1-272[»]
3J56electron microscopy15.00C1-272[»]
3J58electron microscopy17.00C1-272[»]
3J5Aelectron microscopy12.00C1-272[»]
3J5Celectron microscopy17.00C1-272[»]
3J5Eelectron microscopy17.00C1-272[»]
3J5Gelectron microscopy20.00C1-272[»]
3J5Ielectron microscopy15.00C1-272[»]
3J5Kelectron microscopy9.00C1-272[»]
3J5Oelectron microscopy6.80C1-273[»]
3J5Uelectron microscopy7.60D2-273[»]
3J5Welectron microscopy7.60D2-273[»]
3KCRelectron microscopy-61-273[»]
3OASX-ray3.25C2-272[»]
3OATX-ray3.25C2-272[»]
3OFCX-ray3.19C2-272[»]
3OFDX-ray3.19C2-272[»]
3OFQX-ray3.10C2-272[»]
3OFRX-ray3.10C2-272[»]
3OFZX-ray3.29C2-272[»]
3OG0X-ray3.29C2-272[»]
3ORBX-ray3.30C1-273[»]
3R8SX-ray3.00C2-272[»]
3R8TX-ray3.00C2-272[»]
3SGFX-ray3.20C1-273[»]
3UOSX-ray3.70C1-273[»]
487Delectron microscopy7.50I62-172[»]
4GARX-ray3.30C1-273[»]
4GAUX-ray3.30C1-273[»]
4KIXX-ray2.90C1-273[»]
4KIZX-ray2.90C1-273[»]
4KJ1X-ray2.90C1-273[»]
4KJ3X-ray2.90C1-273[»]
4KJ5X-ray2.90C1-273[»]
4KJ7X-ray2.90C1-273[»]
4KJ9X-ray2.90C1-273[»]
4KJBX-ray2.90C1-273[»]
ProteinModelPortalP60422.
SMRP60422. Positions 2-272.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid852132. 1 interaction.
DIPDIP-35747N.
IntActP60422. 362 interactions.
MINTMINT-1322809.
STRING511145.b3317.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP60422.
PRIDEP60422.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76342; AAC76342; b3317.
BAE77974; BAE77974; BAE77974.
GeneID12932295.
947820.
KEGGecj:Y75_p3859.
eco:b3317.
PATRIC32122066. VBIEscCol129921_3410.

Organism-specific databases

EchoBASEEB0858.
EcoGeneEG10865. rplB.

Phylogenomic databases

eggNOGCOG0090.
HOGENOMHOG000232982.
KOK02886.
OMANNLPIRN.
OrthoDBEOG6TR0J1.
PhylomeDBP60422.
ProtClustDBPRK09374.

Enzyme and pathway databases

BioCycEcoCyc:EG10865-MONOMER.
ECOL316407:JW3279-MONOMER.

Gene expression databases

GenevestigatorP60422.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPMF_01320_B. Ribosomal_L2_B.
InterProIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR13691. PTHR13691. 1 hit.
PTHR13691:SF5. PTHR13691:SF5. 1 hit.
PfamPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR01171. rplB_bact. 1 hit.
PROSITEPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60422.
PROP60422.

Entry information

Entry nameRL2_ECOLI
AccessionPrimary (citable) accession number: P60422
Secondary accession number(s): P02387, Q2M6Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 122 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