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Reviewed, UniProtKB/Swiss-Prot P0ADZ0 (RL23_ECOLI)

Last modified June 16, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    50S ribosomal protein L23
Gene names
Name: rplW
Ordered Locus Names: b3318, JW3280
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

One of the early assembly protein, it binds 23S rRNA; is essential for growth. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (Ref.8) for Ffh binding to the ribosome (SRP54, Ref.9 and Ref.10) and to nascent polypeptide chains (Ref.9). HAMAP MF_01369

Subunit structure

Part of the 50S ribosomal subunit. Contacts protein L29 and trigger factor. Ref.6

Sequence similarities

Belongs to the ribosomal protein L23P family.

Mass spectrometry

Molecular mass is 11198.0 Da from positions 1 - 100. Determined by MALDI. Ref.11

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10010050S ribosomal protein L23 HAMAP MF_01369
PRO_0000129407

Experimental info

Mutagenesis16 – 183VSE → AAA: Strongly reduces trigger factor binding. Ref.8
Mutagenesis181E → A: Binds normally to ribosomes; strongly reduces trigger factor binding. Ref.8
Mutagenesis181E → Q: Strongly reduces trigger factor binding. Ref.8
Mutagenesis51 – 533FEV → AAA: No effect on trigger factor binding. Ref.8
Mutagenesis521E → K: No effect on trigger factor binding. Ref.8
Sequence conflict801Missing AA sequence Ref.1

Secondary structure

............. 100
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ADZ0-1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 30CD1D77CC7CF9EB

FASTA10011,199
        10         20         30         40         50         60 
MIREERLLKV LRAPHVSEKA STAMEKSNTI VLKVAKDATK AEIKAAVQKL FEVEVEVVNT 

        70         80         90        100 
LVVKGKVKRH GQRIGRRSDW KKAYVTLKEG QNLDFVGGAE 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of protein L23 from the Escherichia coli ribosome."
Wittmann-Liebold B., Greuer B.
FEBS Lett. 108:69-74(1979) [PubMed: 391594] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: K12.
[2]"Structure of the Escherichia coli S10 ribosomal protein operon."
Zurawski G., Zurawski S.M.
Nucleic Acids Res. 13:4521-4526(1985) [PubMed: 3892488] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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]"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.
[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: 3298242] [Abstract]
Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
Strain: K12.
[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 L29.
[8]"L23 protein functions as a chaperone docking site on the ribosome."
Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B.
Nature 419:171-174(2002) [PubMed: 12226666] [Abstract]
Cited for: BINDING TO TRIGGER FACTOR, MUTAGENESIS OF 16-VAL--GLU-18; GLU-18; 51-PHE--VAL-53 AND GLU-52.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[9]"Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome."
Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J.
J. Cell Biol. 161:679-684(2003) [PubMed: 12756233] [Abstract]
Cited for: CROSS-LINKS TO FFH (SRP54); TRIGGER FACTOR AND TO NASCENT PROTEIN CHAINS.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[10]"The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome."
Gu S.-Q., Peske F., Wieden H.-J., Rodnina M.V., Wintermeyer W.
RNA 9:566-573(2003) [PubMed: 12702815] [Abstract]
Cited for: IDENTIFICATION OF RIBOSOMAL PROTEIN L23 AS THE DOCKING SITE FOR SIGNAL RECOGNITION PARTICLE.
Strain: MRE-600.
[11]"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.
[12]"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: 12809609] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
Strain: MRE-600.
[13]"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

X02613 Genomic DNA. Translation: CAA26462.1.
U18997 Genomic DNA. Translation: AAA58115.1.
U00096 Genomic DNA. Translation: AAC76343.1.
AP009048 Genomic DNA. Translation: BAE77973.1.
PIRR5EC23. A65125.
RefSeqAP_004472.1.
NP_417777.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30R1-100[»]
1P86electron microscopy11.50R1-100[»]
1VS6X-ray3.46T1-100[»]
1VS8X-ray3.46T1-100[»]
2AW4X-ray3.46T1-100[»]
2AWBX-ray3.46T1-100[»]
2GYAelectron microscopy2.00R7-98[»]
2GYCelectron microscopy-R7-98[»]
2I2TX-ray3.22T1-100[»]
2I2VX-ray3.22T1-100[»]
2J28electron microscopy8.00T1-99[»]
2QAMX-ray3.21T1-100[»]
2QAOX-ray3.21T1-100[»]
2QBAX-ray3.54T1-100[»]
2QBCX-ray3.54T1-100[»]
2QBEX-ray3.30T1-100[»]
2QBGX-ray3.30T1-100[»]
2QBIX-ray4.00T1-100[»]
2QBKX-ray4.00T1-100[»]
2QOVX-ray3.93T1-100[»]
2QOXX-ray3.93T1-100[»]
2QOZX-ray3.50T1-100[»]
2QP1X-ray3.50T1-100[»]
2RDOelectron microscopy9.10T1-100[»]
2Z4LX-ray4.45T1-100[»]
2Z4NX-ray4.45T1-100[»]
3BBXelectron microscopy-T1-100[»]
3FIKelectron microscopy-T1-93[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP0ADZ0. 73 interactions.

2-D gel databases

ECO2DBASEI013.0. 6TH EDITION.

Genome annotation databases

GeneID947819.
GenomeReviewsGene locus JW3280 in contig AP009048_GR.
Gene locus b3318 in contig U00096_GR.
KEGGecj:JW3280.
eco:b3318.

Organism-specific databases

EchoBASEEB0876.
EcoGeneEG10883. rplW.
CMRSearch...

Phylogenomic databases

HOGENOMP0ADZ0.
OMAP0ADZ0. VSEKATM.

Enzyme and pathway databases

BioCycEcoCyc:EG10883-MON.

Family and domain databases

HAMAPMF_01369.
[Tree]
InterProIPR012677. a_b_plait_nuc_bd.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
PfamPF00276. Ribosomal_L23. 1 hit.
[Graphical view]
ProDomPD001141. Ribosomal_L23. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRL23_ECOLI
AccessionPrimary (citable) accession number: P0ADZ0
Secondary accession number(s): P02424, Q2M6Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 6, 2005
Last modified: June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents