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P0A7M6

- RL29_ECOLI

UniProt

P0A7M6 - RL29_ECOLI

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Protein
50S ribosomal protein L29
Gene
rpmC, b3312, JW3274
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Binds 23S rRNA. It is not essential for growth.UniRule annotation
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (1 Publication).UniRule annotation

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10887-MONOMER.
ECOL316407:JW3274-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L29
Gene namesi
Name:rpmC
Ordered Locus Names:b3312, JW3274
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10887. rpmC.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells missing both S17 and L29 grow very slowly and have a rather unstable temperature-sensitive phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 636350S ribosomal protein L29UniRule annotation
PRO_0000130384Add
BLAST

Proteomic databases

PaxDbiP0A7M6.
PRIDEiP0A7M6.

Expressioni

Gene expression databases

GenevestigatoriP0A7M6.

Interactioni

Subunit structurei

Part of the 50s ribosomal subunit. Contacts protein L23 (1 Publication), trigger factor (1 Publication) and protein nascent chains (1 Publication). Might also contact SecE and probably does contact SecG when the SecYEG translocation complex is docked with the ribosome.

Protein-protein interaction databases

DIPiDIP-47911N.
IntActiP0A7M6. 33 interactions.
MINTiMINT-1240640.
STRINGi511145.b3312.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53
Beta strandi6 – 83
Helixi10 – 2213
Helixi24 – 3310
Beta strandi37 – 393
Helixi41 – 5818
Turni59 – 624

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3J5Lelectron microscopy6.60Y1-63[»]
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[»]
4CSUelectron microscopy5.5011-63[»]
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[»]
ProteinModelPortaliP0A7M6.
SMRiP0A7M6. Positions 1-63.

Miscellaneous databases

EvolutionaryTraceiP0A7M6.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0255.
HOGENOMiHOG000248754.
KOiK02904.
OMAiLRMQAST.
OrthoDBiEOG6VTK8Z.
PhylomeDBiP0A7M6.

Family and domain databases

Gene3Di1.10.287.310. 1 hit.
HAMAPiMF_00374. Ribosomal_L29.
InterProiIPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]
PfamiPF00831. Ribosomal_L29. 1 hit.
[Graphical view]
SUPFAMiSSF46561. SSF46561. 1 hit.
TIGRFAMsiTIGR00012. L29. 1 hit.
PROSITEiPS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A7M6-1 [UniParc]FASTAAdd to Basket

« Hide

MKAKELREKS VEELNTELLN LLREQFNLRM QAASGQLQQS HLLKQVRRDV   50
ARVKTLLNEK AGA 63
Length:63
Mass (Da):7,273
Last modified:April 1, 1988 - v1
Checksum:iDAEF8F126B0AA077
GO

Sequence cautioni

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

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26468.1.
U18997 Genomic DNA. Translation: AAA58109.1.
U00096 Genomic DNA. Translation: AAC76337.1.
AP009048 Genomic DNA. Translation: BAE77979.1.
PIRiB37519. R5EC29.
RefSeqiNP_417771.1. NC_000913.3.
YP_492120.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76337; AAC76337; b3312.
BAE77979; BAE77979; BAE77979.
GeneIDi12934441.
947807.
KEGGiecj:Y75_p3864.
eco:b3312.
PATRICi32122056. VBIEscCol129921_3405.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26468.1 .
U18997 Genomic DNA. Translation: AAA58109.1 .
U00096 Genomic DNA. Translation: AAC76337.1 .
AP009048 Genomic DNA. Translation: BAE77979.1 .
PIRi B37519. R5EC29.
RefSeqi NP_417771.1. NC_000913.3.
YP_492120.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ML5 electron microscopy 14.00 w 2-63 [» ]
1P85 electron microscopy 12.30 W 1-63 [» ]
1P86 electron microscopy 11.50 W 1-63 [» ]
1VS6 X-ray 3.46 X 1-63 [» ]
1VS8 X-ray 3.46 X 1-63 [» ]
1VT2 X-ray 3.30 Y 1-63 [» ]
2AW4 X-ray 3.46 X 1-63 [» ]
2AWB X-ray 3.46 X 1-63 [» ]
2GYA electron microscopy 15.00 W 1-60 [» ]
2GYC electron microscopy 15.00 W 1-60 [» ]
2I2T X-ray 3.22 Y 1-63 [» ]
2I2V X-ray 3.22 Y 1-63 [» ]
2J28 electron microscopy 8.00 X 1-63 [» ]
2QAM X-ray 3.21 X 1-63 [» ]
2QAO X-ray 3.21 X 1-63 [» ]
2QBA X-ray 3.54 X 1-63 [» ]
2QBC X-ray 3.54 X 1-63 [» ]
2QBE X-ray 3.30 X 1-63 [» ]
2QBG X-ray 3.30 X 1-63 [» ]
2QBI X-ray 4.00 X 1-63 [» ]
2QBK X-ray 4.00 X 1-63 [» ]
2QOV X-ray 3.93 X 1-63 [» ]
2QOX X-ray 3.93 X 1-63 [» ]
2QOZ X-ray 3.50 X 1-63 [» ]
2QP1 X-ray 3.50 X 1-63 [» ]
2RDO electron microscopy 9.10 X 1-63 [» ]
2VHM X-ray 3.74 X 1-63 [» ]
2VHN X-ray 3.74 X 1-63 [» ]
2VRH electron microscopy 19.00 D 1-63 [» ]
2WWQ electron microscopy 5.80 1 1-63 [» ]
2Z4L X-ray 4.45 X 1-63 [» ]
2Z4N X-ray 4.45 X 1-63 [» ]
3BBX electron microscopy 10.00 X 1-63 [» ]
3DF2 X-ray 3.50 X 1-63 [» ]
3DF4 X-ray 3.50 X 1-63 [» ]
3E1B electron microscopy - Q 1-63 [» ]
3E1D electron microscopy - Q 1-63 [» ]
3FIK electron microscopy 6.70 Y 1-63 [» ]
3I1N X-ray 3.19 Y 1-63 [» ]
3I1P X-ray 3.19 Y 1-63 [» ]
3I1R X-ray 3.81 Y 1-63 [» ]
3I1T X-ray 3.81 Y 1-63 [» ]
3I20 X-ray 3.71 Y 1-63 [» ]
3I22 X-ray 3.71 Y 1-63 [» ]
3IZT electron microscopy - Z 1-63 [» ]
3IZU electron microscopy - Z 1-63 [» ]
3J01 electron microscopy - Y 1-63 [» ]
3J0T electron microscopy 12.10 0 1-63 [» ]
3J0W electron microscopy 14.70 0 1-63 [» ]
3J0Y electron microscopy 13.50 0 1-63 [» ]
3J11 electron microscopy 13.10 0 1-63 [» ]
3J12 electron microscopy 11.50 0 1-63 [» ]
3J14 electron microscopy 11.50 0 1-63 [» ]
3J19 electron microscopy 8.30 Y 1-63 [» ]
3J37 electron microscopy 9.80 2 1-63 [» ]
3J45 electron microscopy 9.50 Y 1-63 [» ]
3J46 electron microscopy 10.10 Y 1-63 [» ]
3J4X electron microscopy 12.00 Y 1-63 [» ]
3J50 electron microscopy 20.00 Y 1-63 [» ]
3J51 electron microscopy 17.00 Y 1-63 [» ]
3J52 electron microscopy 12.00 Y 1-63 [» ]
3J54 electron microscopy 13.00 Y 1-63 [» ]
3J56 electron microscopy 15.00 Y 1-63 [» ]
3J58 electron microscopy 17.00 Y 1-63 [» ]
3J5A electron microscopy 12.00 Y 1-63 [» ]
3J5C electron microscopy 17.00 Y 1-63 [» ]
3J5E electron microscopy 17.00 Y 1-63 [» ]
3J5G electron microscopy 20.00 Y 1-63 [» ]
3J5I electron microscopy 15.00 Y 1-63 [» ]
3J5K electron microscopy 9.00 Y 1-63 [» ]
3J5L electron microscopy 6.60 Y 1-63 [» ]
3J5O electron microscopy 6.80 Y 1-63 [» ]
3J5U electron microscopy 7.60 1 1-63 [» ]
3J5W electron microscopy 7.60 2 1-63 [» ]
3KCR electron microscopy - Y 1-63 [» ]
3OAS X-ray 3.25 Y 1-63 [» ]
3OAT X-ray 3.25 Y 1-63 [» ]
3OFC X-ray 3.19 Y 1-63 [» ]
3OFD X-ray 3.19 Y 1-63 [» ]
3OFQ X-ray 3.10 Y 1-63 [» ]
3OFR X-ray 3.10 Y 1-63 [» ]
3OFZ X-ray 3.29 Y 1-63 [» ]
3OG0 X-ray 3.29 Y 1-63 [» ]
3ORB X-ray 3.30 Y 1-63 [» ]
3R8S X-ray 3.00 Y 1-63 [» ]
3R8T X-ray 3.00 Y 1-63 [» ]
3SGF X-ray 3.20 2 1-63 [» ]
3UOS X-ray 3.70 2 1-63 [» ]
4CSU electron microscopy 5.50 1 1-63 [» ]
4GAR X-ray 3.30 Y 1-63 [» ]
4GAU X-ray 3.30 Y 1-63 [» ]
4KIX X-ray 2.90 Y 1-63 [» ]
4KIZ X-ray 2.90 Y 1-63 [» ]
4KJ1 X-ray 2.90 Y 1-63 [» ]
4KJ3 X-ray 2.90 Y 1-63 [» ]
4KJ5 X-ray 2.90 Y 1-63 [» ]
4KJ7 X-ray 2.90 Y 1-63 [» ]
4KJ9 X-ray 2.90 Y 1-63 [» ]
4KJB X-ray 2.90 Y 1-63 [» ]
ProteinModelPortali P0A7M6.
SMRi P0A7M6. Positions 1-63.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47911N.
IntActi P0A7M6. 33 interactions.
MINTi MINT-1240640.
STRINGi 511145.b3312.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7M6.
PRIDEi P0A7M6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76337 ; AAC76337 ; b3312 .
BAE77979 ; BAE77979 ; BAE77979 .
GeneIDi 12934441.
947807.
KEGGi ecj:Y75_p3864.
eco:b3312.
PATRICi 32122056. VBIEscCol129921_3405.

Organism-specific databases

EchoBASEi EB0880.
EcoGenei EG10887. rpmC.

Phylogenomic databases

eggNOGi COG0255.
HOGENOMi HOG000248754.
KOi K02904.
OMAi LRMQAST.
OrthoDBi EOG6VTK8Z.
PhylomeDBi P0A7M6.

Enzyme and pathway databases

BioCyci EcoCyc:EG10887-MONOMER.
ECOL316407:JW3274-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7M6.
PROi P0A7M6.

Gene expression databases

Genevestigatori P0A7M6.

Family and domain databases

Gene3Di 1.10.287.310. 1 hit.
HAMAPi MF_00374. Ribosomal_L29.
InterProi IPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view ]
Pfami PF00831. Ribosomal_L29. 1 hit.
[Graphical view ]
SUPFAMi SSF46561. SSF46561. 1 hit.
TIGRFAMsi TIGR00012. L29. 1 hit.
PROSITEi PS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  15. Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH SECYE AND A NASCENT POLYPEPTIDE CHAIN.

Entry informationi

Entry nameiRL29_ECOLI
AccessioniPrimary (citable) accession number: P0A7M6
Secondary accession number(s): P02429, Q2M6X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: September 3, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi