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P0A7M6 (RL29_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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) [Reference 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-Rule MF_00374

One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (Ref.9). HAMAP-Rule MF_00374

Subunit structure

Part of the 50s ribosomal subunit. Contacts protein L23 (Ref.7), trigger factor (Ref.9) and protein nascent chains (Ref.10). 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.9

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.11

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636350S ribosomal protein L29 HAMAP-Rule 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] [Europe PMC] [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] [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]"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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CROSS-LINKING TO L23.
[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, DISRUPTION PHENOTYPE.
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 NASCENT PROTEIN CHAINS.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[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] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY.
Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[12]"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.
[13]"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.
[14]"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.
[15]"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: 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_000913.3.
YP_492120.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00w2-63[»]
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[»]
3J0Telectron microscopy12.1001-63[»]
3J0Welectron microscopy14.7001-63[»]
3J0Yelectron microscopy13.5001-63[»]
3J11electron microscopy13.1001-63[»]
3J12electron microscopy11.5001-63[»]
3J14electron microscopy11.5001-63[»]
3J19electron microscopy8.30Y1-63[»]
3J37electron microscopy9.8021-63[»]
3J45electron microscopy9.50Y1-63[»]
3J46electron microscopy10.10Y1-63[»]
3J4Xelectron microscopy12.00Y1-63[»]
3J50electron microscopy20.00Y1-63[»]
3J51electron microscopy17.00Y1-63[»]
3J52electron microscopy12.00Y1-63[»]
3J54electron microscopy13.00Y1-63[»]
3J56electron microscopy15.00Y1-63[»]
3J58electron microscopy17.00Y1-63[»]
3J5Aelectron microscopy12.00Y1-63[»]
3J5Celectron microscopy17.00Y1-63[»]
3J5Eelectron microscopy17.00Y1-63[»]
3J5Gelectron microscopy20.00Y1-63[»]
3J5Ielectron microscopy15.00Y1-63[»]
3J5Kelectron microscopy9.00Y1-63[»]
3J5Oelectron microscopy6.80Y1-63[»]
3J5Uelectron microscopy7.6011-63[»]
3J5Welectron microscopy7.6021-63[»]
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[»]
3SGFX-ray3.2021-63[»]
3UOSX-ray3.7021-63[»]
4GARX-ray3.30Y1-63[»]
4GAUX-ray3.30Y1-63[»]
4KIXX-ray2.90Y1-63[»]
4KIZX-ray2.90Y1-63[»]
4KJ1X-ray2.90Y1-63[»]
4KJ3X-ray2.90Y1-63[»]
4KJ5X-ray2.90Y1-63[»]
4KJ7X-ray2.90Y1-63[»]
4KJ9X-ray2.90Y1-63[»]
4KJBX-ray2.90Y1-63[»]
ProteinModelPortalP0A7M6.
SMRP0A7M6. Positions 1-63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47911N.
IntActP0A7M6. 33 interactions.
MINTMINT-1240640.
STRING511145.b3312.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7M6.
PRIDEP0A7M6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76337; AAC76337; b3312.
BAE77979; BAE77979; BAE77979.
GeneID12934441.
947807.
KEGGecj:Y75_p3864.
eco:b3312.
PATRIC32122056. VBIEscCol129921_3405.

Organism-specific databases

EchoBASEEB0880.
EcoGeneEG10887. rpmC.

Phylogenomic databases

eggNOGCOG0255.
HOGENOMHOG000248754.
KOK02904.
OMALRMQAST.
OrthoDBEOG6VTK8Z.
PhylomeDBP0A7M6.
ProtClustDBPRK00306.

Enzyme and pathway databases

BioCycEcoCyc:EG10887-MONOMER.
ECOL316407:JW3274-MONOMER.

Gene expression databases

GenevestigatorP0A7M6.

Family and domain databases

Gene3D1.10.287.310. 1 hit.
HAMAPMF_00374. Ribosomal_L29.
InterProIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
PfamPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMSSF46561. SSF46561. 1 hit.
TIGRFAMsTIGR00012. L29. 1 hit.
PROSITEPS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7M6.
PROP0A7M6.

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: April 16, 2014
This is version 94 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