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P0ADZ0 (RL23_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. 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 L23
Gene names
Name:rplW
Ordered Locus Names:b3318, JW3280
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length100 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (Ref.9) for Ffh binding to the ribosome (SRP54, Ref.10 and Ref.11) and to nascent polypeptide chains (Ref.10). HAMAP-Rule MF_01369

Subunit structure

Part of the 50S ribosomal subunit. Contacts protein L29 and trigger factor. Might also contact SecE and probably does contact SecG and SecY when the SecYEG translocation complex is docked with the ribosome. 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.12

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rpsEP0A7W12EBI-542264,EBI-543949

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10010050S ribosomal protein L23 HAMAP-Rule MF_01369
PRO_0000129407

Experimental info

Mutagenesis16 – 183VSE → AAA: Strongly reduces trigger factor binding. Ref.9
Mutagenesis181E → A: Binds normally to ribosomes; strongly reduces trigger factor binding. Ref.9
Mutagenesis181E → Q: Strongly reduces trigger factor binding. Ref.9
Mutagenesis51 – 533FEV → AAA: No effect on trigger factor binding. Ref.9
Mutagenesis521E → K: No effect on trigger factor binding. Ref.9
Sequence conflict801Missing AA sequence Ref.1

Secondary structure

...................... 100
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ADZ0 [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] [Europe PMC] [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] [Europe PMC] [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 277:1453-1462(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]"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.
[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]"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 L29.
[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]"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] [Europe PMC] [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.
[10]"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] [Europe PMC] [Abstract]
Cited for: CROSS-LINKS TO FFH (SRP54); TRIGGER FACTOR AND TO NASCENT PROTEIN CHAINS.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RIBOSOMAL PROTEIN L23 AS THE DOCKING SITE FOR SIGNAL RECOGNITION PARTICLE.
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]"Structure of the E. coli protein-conducting channel bound to a translating ribosome."
Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX.
Strain: MRE-600.
[14]"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).
Strain: MRE-600.
[15]"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.
[16]"Cryo-EM structure of the ribosome-SecYE complex in the membrane environment."
Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R.
Nat. Struct. Mol. Biol. 18:614-621(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH SECYE AND A NASCENT POLYPEPTIDE CHAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_417777.1. NC_000913.3.
YP_492114.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00t2-85[»]
1P85electron microscopy12.30R1-100[»]
1P86electron microscopy11.50R1-100[»]
1VS6X-ray3.46T1-100[»]
1VS8X-ray3.46T1-100[»]
1VT2X-ray3.30T1-100[»]
2AW4X-ray3.46T1-100[»]
2AWBX-ray3.46T1-100[»]
2GYAelectron microscopy15.00R7-98[»]
2GYCelectron microscopy15.00R7-98[»]
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[»]
2VRHelectron microscopy19.00B1-100[»]
2WWQelectron microscopy5.80T1-93[»]
2Z4LX-ray4.45T1-100[»]
2Z4NX-ray4.45T1-100[»]
3BBXelectron microscopy10.00T1-100[»]
3E1Belectron microscopy-M1-99[»]
3E1Delectron microscopy-M1-99[»]
3FIKelectron microscopy6.70T1-93[»]
3I1NX-ray3.19T1-100[»]
3I1PX-ray3.19T1-100[»]
3I1RX-ray3.81T1-100[»]
3I1TX-ray3.81T1-100[»]
3I20X-ray3.71T1-100[»]
3I22X-ray3.71T1-100[»]
3IY9electron microscopy14.10T1-99[»]
3IZTelectron microscopy-U1-100[»]
3IZUelectron microscopy-U1-100[»]
3J01electron microscopy-T1-100[»]
3J0Telectron microscopy12.10V1-100[»]
3J0Welectron microscopy14.70V1-100[»]
3J0Yelectron microscopy13.50V1-100[»]
3J11electron microscopy13.10V1-100[»]
3J12electron microscopy11.50V1-100[»]
3J14electron microscopy11.50V1-100[»]
3J19electron microscopy8.30T1-93[»]
3J37electron microscopy9.80X1-100[»]
3J45electron microscopy9.50T1-100[»]
3J46electron microscopy10.10T1-100[»]
3J4Xelectron microscopy12.00T1-93[»]
3J50electron microscopy20.00T1-93[»]
3J51electron microscopy17.00T1-93[»]
3J52electron microscopy12.00T1-93[»]
3J54electron microscopy13.00T1-93[»]
3J56electron microscopy15.00T1-93[»]
3J58electron microscopy17.00T1-93[»]
3J5Aelectron microscopy12.00T1-93[»]
3J5Celectron microscopy17.00T1-93[»]
3J5Eelectron microscopy17.00T1-93[»]
3J5Gelectron microscopy20.00T1-93[»]
3J5Ielectron microscopy15.00T1-93[»]
3J5Kelectron microscopy9.00T1-93[»]
3J5Lelectron microscopy6.60T1-93[»]
3J5Oelectron microscopy6.80T1-100[»]
3J5Uelectron microscopy7.60V1-100[»]
3J5Welectron microscopy7.60W1-100[»]
3KCRelectron microscopy-T1-100[»]
3OASX-ray3.25T1-93[»]
3OATX-ray3.25T1-93[»]
3OFCX-ray3.19T1-93[»]
3OFDX-ray3.19T1-93[»]
3OFQX-ray3.10T1-93[»]
3OFRX-ray3.10T1-93[»]
3OFZX-ray3.29T1-93[»]
3OG0X-ray3.29T1-93[»]
3ORBX-ray3.30T1-100[»]
3R8SX-ray3.00T1-93[»]
3R8TX-ray3.00T1-93[»]
3SGFX-ray3.20X1-100[»]
3UOSX-ray3.70X1-100[»]
4GARX-ray3.30T1-100[»]
4GAUX-ray3.30T1-100[»]
4KIXX-ray2.90T1-100[»]
4KIZX-ray2.90T1-100[»]
4KJ1X-ray2.90T1-100[»]
4KJ3X-ray2.90T1-100[»]
4KJ5X-ray2.90T1-100[»]
4KJ7X-ray2.90T1-100[»]
4KJ9X-ray2.90T1-100[»]
4KJBX-ray2.90T1-100[»]
ProteinModelPortalP0ADZ0.
SMRP0ADZ0. Positions 7-98.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35972N.
IntActP0ADZ0. 73 interactions.
MINTMINT-1225825.
STRING511145.b3318.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0ADZ0.
PRIDEP0ADZ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76343; AAC76343; b3318.
BAE77973; BAE77973; BAE77973.
GeneID12932296.
947819.
KEGGecj:Y75_p3858.
eco:b3318.
PATRIC32122068. VBIEscCol129921_3411.

Organism-specific databases

EchoBASEEB0876.
EcoGeneEG10883. rplW.

Phylogenomic databases

eggNOGCOG0089.
HOGENOMHOG000231364.
KOK02892.
OMAFGRRSDW.
OrthoDBEOG6HTP4P.
PhylomeDBP0ADZ0.

Enzyme and pathway databases

BioCycEcoCyc:EG10883-MONOMER.
ECOL316407:JW3280-MONOMER.

Gene expression databases

GenevestigatorP0ADZ0.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
HAMAPMF_01369_B. Ribosomal_L23_B.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001014. Ribosomal_L23/L25_CS.
IPR013025. Ribosomal_L25/23.
[Graphical view]
PfamPF00276. Ribosomal_L23. 1 hit.
[Graphical view]
SUPFAMSSF54189. SSF54189. 1 hit.
PROSITEPS00050. RIBOSOMAL_L23. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ADZ0.
PROP0ADZ0.

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 11, 2014
This is version 88 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