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P0A7M6 (RL29_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. 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 L29
Gene names
Name:rpmC
Ordered Locus Names:b3312, JW3274
OrganismEscherichia coli (strain K12)
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). Might also contact SecE and probably does contact SecG when the SecYEG translocation complex is docked with the ribosome.

Disruption phenotype

Cells missing both S17 and L29 grow very slowly and have 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: Exchange of two tryptic peptides.

Ontologies

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 [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]"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: 16292303] [Abstract]
Cited for: POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX.
Strain: MRE-600.
[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.
[14]"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: 21499241] [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: CAA26468.1.
U18997 Genomic DNA. Translation: AAA58109.1.
U00096 Genomic DNA. Translation: AAC76337.1.
AP009048 Genomic DNA. Translation: BAE77979.1.
PIRR5EC29. B37519.
RefSeqNP_417771.1. NC_000913.2.

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[»]
1VT2X-ray3.30Y1-63[»]
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[»]
2WWQelectron microscopy5.8011-63[»]
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[»]
3IZTelectron microscopy-Z1-63[»]
3IZUelectron microscopy-Z1-63[»]
3J01electron microscopy-Y1-63[»]
3KCRelectron microscopy-Y1-63[»]
3OASX-ray3.25Y1-63[»]
3OATX-ray3.25Y1-63[»]
3OFCX-ray3.19Y1-63[»]
3OFDX-ray3.19Y1-63[»]
3OFQX-ray3.10Y1-63[»]
3OFRX-ray3.10Y1-63[»]
3OFZX-ray3.29Y1-63[»]
3OG0X-ray3.29Y1-63[»]
3ORBX-ray3.30Y1-63[»]
3R8SX-ray3.00Y1-63[»]
3R8TX-ray3.00Y1-63[»]
ProteinModelPortalP0A7M6.
SMRP0A7M6. Positions 1-63.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-47911N.
IntActP0A7M6. 33 interactions.
MINTMINT-1240640.

2D gel databases

ECO2DBASEI011.1. 6TH EDITION.

Proteomic databases

PRIDEP0A7M6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000158; EBESCP00000000158; EBESCG00000000126.
EBESCT00000016909; EBESCP00000016200; EBESCG00000015968.
GeneID947807.
GenomeReviewsGene locus JW3274 in contig AP009048_GR.
Gene locus b3312 in contig U00096_GR.
KEGGecj:JW3274.
eco:b3312.
PATRIC32122056. VBIEscCol129921_3405.

Organism-specific databases

EchoBASEEB0880.
EcoGeneEG10887. rpmC.

Phylogenomic databases

eggNOGCOG0255.
GeneTreeEBGT00050000009801.
HOGENOMHBG730819.
OMAKQVRRNI.
PhylomeDBP0A7M6.
ProtClustDBPRK00306.

Enzyme and pathway databases

BioCycEcoCyc:EG10887-MONOMER.

Gene expression databases

GenevestigatorP0A7M6.

Family and domain databases

HAMAPMF_00374. Ribosomal_L29.
[Tree]
InterProIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
Gene3DG3DSA:1.10.287.310. Ribosomal_L29. 1 hit.
KOK02904.
PfamPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMSSF46561. Ribosomal_L29. 1 hit.
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: January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families