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Reviewed, UniProtKB/Swiss-Prot P0A7M6 (RL29_ECOLI)

Last modified February 9, 2010. Version 58. 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    50S ribosomal protein L29
Gene names
Name: rpmC
Ordered Locus Names: b3312, JW3274
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length63 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Binds 23S rRNA. It is not essential for growth. HAMAP MF_00374

One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (Ref.8). HAMAP MF_00374

Subunit structure

Part of the 50s ribosomal subunit. Contacts protein L23 (Ref.7), trigger factor (Ref.8) and protein nascent chains (Ref.9). HAMAP MF_00374

Disruption phenotype

Cells missing both S17 and L29 grows very slowly and has a rather unstable temperature-sensitive phenotype. Ref.8

Sequence similarities

Belongs to the ribosomal protein L29P family.

Mass spectrometry

Molecular mass is 7273.4 Da from positions 1 - 63. Determined by MALDI. Ref.10

Sequence caution

The sequence described in Ref.1 differs from that shown. Reason: Miscellaneous discrepancy. Exchange of two tryptic peptides.

Ontologies

Keywords
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636350S ribosomal protein L29 HAMAP MF_00374
PRO_0000130384

Secondary structure

.............. 63
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7M6-1 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: DAEF8F126B0AA077

FASTA637,273
        10         20         30         40         50         60 
MKAKELREKS VEELNTELLN LLREQFNLRM QAASGQLQQS HLLKQVRRDV ARVKTLLNEK 


AGA 

« Hide

References

« Hide 'large scale' references
[1]"The primary structure of the ribosomal protein L29 from Escherichia coli."
Bitar K.G.
Biochim. Biophys. Acta 386:99-106(1975) [PubMed: 1092361] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: K.
[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]"A mutant from Escherichia coli which lacks ribosomal proteins S17 and L29 used to localize these two proteins on the ribosomal surface."
Stoeffler-Meilicke M., Dabbs E.R., Albrecht-Ehrlich R., Stoeffler G.
Eur. J. Biochem. 150:485-490(1985) [PubMed: 3926498] [Abstract]
Cited for: CHARACTERIZATION OF A STRAIN MISSING S17 AND L29.
Strain: AM111.
[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 L23.
[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, DISRUPTION PHENOTYPE.
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 NASCENT PROTEIN CHAINS.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[10]"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.
[11]"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.
[12]"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
X02613 Genomic DNA. Translation: CAA26468.1.
U18997 Genomic DNA. Translation: AAA58109.1.
U00096 Genomic DNA. Translation: AAC76337.1.
AP009048 Genomic DNA. Translation: BAE77979.1.
PIRR5EC29. B37519.
RefSeqAP_004478.1.
NP_417771.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30W1-63[»]
1P86electron microscopy11.50W1-63[»]
1VS6X-ray3.46X1-63[»]
1VS8X-ray3.46X1-63[»]
2AW4X-ray3.46X1-63[»]
2AWBX-ray3.46X1-63[»]
2GYAelectron microscopy15.00W1-60[»]
2GYCelectron microscopy15.00W1-60[»]
2I2TX-ray3.22Y1-63[»]
2I2VX-ray3.22Y1-63[»]
2J28electron microscopy8.00X1-63[»]
2QAMX-ray3.21X1-63[»]
2QAOX-ray3.21X1-63[»]
2QBAX-ray3.54X1-63[»]
2QBCX-ray3.54X1-63[»]
2QBEX-ray3.30X1-63[»]
2QBGX-ray3.30X1-63[»]
2QBIX-ray4.00X1-63[»]
2QBKX-ray4.00X1-63[»]
2QOVX-ray3.93X1-63[»]
2QOXX-ray3.93X1-63[»]
2QOZX-ray3.50X1-63[»]
2QP1X-ray3.50X1-63[»]
2RDOelectron microscopy9.10X1-63[»]
2VHMX-ray3.74X1-63[»]
2VHNX-ray3.74X1-63[»]
2VRHelectron microscopy19.00D1-63[»]
2Z4LX-ray4.45X1-63[»]
2Z4NX-ray4.45X1-63[»]
3BBXelectron microscopy10.00X1-63[»]
3DF2X-ray3.50X1-63[»]
3DF4X-ray3.50X1-63[»]
3E1Belectron microscopy-Q1-63[»]
3E1Delectron microscopy-Q1-63[»]
3FIKelectron microscopy6.70Y1-63[»]
3I1NX-ray3.19Y1-63[»]
3I1PX-ray3.19Y1-63[»]
3I1RX-ray3.81Y1-63[»]
3I1TX-ray3.81Y1-63[»]
3I20X-ray3.71Y1-63[»]
3I22X-ray3.71Y1-63[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP0A7M6.

2-D gel databases

ECO2DBASEI011.1. 6TH EDITION.

Proteomic databases

PRIDEP0A7M6.

Genome annotation databases

GeneID947807.
GenomeReviewsGene locus JW3274 in contig AP009048_GR.
Gene locus b3312 in contig U00096_GR.
KEGGecj:JW3274.
eco:b3312.

Organism-specific databases

EchoBASEEB0880.
EcoGeneEG10887. rpmC.
CMRSearch...

Phylogenomic databases

eggNOGCOG0255.
HOGENOMHBG730819.
OMANEVRKDI.

Enzyme and pathway databases

BioCycEcoCyc:EG10887-MONOMER.
ECOL168927:B3312-MONOMER.

Gene expression databases

GenevestigatorP0A7M6.

Family and domain databases

HAMAPMF_00374_B. Ribosomal_L29_B.
[Tree]
InterProIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
Gene3DG3DSA:1.10.287.310. Ribosomal_L29. 1 hit.
PfamPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
TIGRFAMsTIGR00012. L29. 1 hit.
PROSITEPS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRL29_ECOLI
AccessionPrimary (citable) accession number: P0A7M6
Secondary accession number(s): P02429, Q2M6X7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: February 9, 2010
This is version 58 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents