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Protein

50S ribosomal protein L5

Gene

rplE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18.
In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.2 Publications
Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro
  3. tRNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10868-MONOMER.
ECOL316407:JW3270-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L5
Gene namesi
Name:rplE
Ordered Locus Names:b3308, JW3270
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10868. rplE.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 17917850S ribosomal protein L5PRO_0000124925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP62399.
PRIDEiP62399.

Expressioni

Gene expression databases

GenevestigatoriP62399.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S rRNA; cross-links to the P site tRNA. Forms a bridge to the 30S subunit in the 70S ribosome, contacting protein S13 and S19.

Protein-protein interaction databases

BioGridi852112. 1 interaction.
DIPiDIP-35914N.
IntActiP62399. 71 interactions.
MINTiMINT-1238892.
STRINGi511145.b3308.

Structurei

Secondary structure

1
179
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2018Combined sources
Helixi25 – 273Combined sources
Beta strandi31 – 377Combined sources
Turni42 – 454Combined sources
Helixi47 – 6014Combined sources
Beta strandi61 – 633Combined sources
Beta strandi66 – 694Combined sources
Beta strandi71 – 733Combined sources
Turni75 – 784Combined sources
Beta strandi81 – 833Combined sources
Beta strandi84 – 874Combined sources
Beta strandi88 – 914Combined sources
Helixi93 – 10513Combined sources
Helixi107 – 1104Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1336Combined sources
Helixi135 – 1373Combined sources
Beta strandi138 – 1403Combined sources
Turni143 – 1453Combined sources
Beta strandi152 – 1587Combined sources
Helixi163 – 1719Combined sources
Turni172 – 1743Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00g2-177[»]
1P85electron microscopy12.30D2-179[»]
1P86electron microscopy11.50D2-179[»]
1VS6X-ray3.46F1-179[»]
1VS8X-ray3.46F1-179[»]
1VT2X-ray3.30F1-179[»]
2AW4X-ray3.46F2-179[»]
2AWBX-ray3.46F2-179[»]
2GYAelectron microscopy15.00D3-179[»]
2GYCelectron microscopy15.00D3-179[»]
2I2TX-ray3.22F2-179[»]
2I2VX-ray3.22F2-179[»]
2J28electron microscopy8.00F2-179[»]
2QAMX-ray3.21F2-179[»]
2QAOX-ray3.21F2-179[»]
2QBAX-ray3.54F2-179[»]
2QBCX-ray3.54F2-179[»]
2QBEX-ray3.30F2-179[»]
2QBGX-ray3.30F2-179[»]
2QBIX-ray4.00F2-179[»]
2QBKX-ray4.00F2-179[»]
2QOVX-ray3.93F2-179[»]
2QOXX-ray3.93F2-179[»]
2QOZX-ray3.50F2-179[»]
2QP1X-ray3.50F2-179[»]
2RDOelectron microscopy9.10F2-179[»]
2VHMX-ray3.74F2-179[»]
2VHNX-ray3.74F2-179[»]
2WWQelectron microscopy5.80F2-179[»]
2Z4LX-ray4.45F2-179[»]
2Z4NX-ray4.45F2-179[»]
3BBXelectron microscopy10.00F2-179[»]
3DF2X-ray3.50F2-178[»]
3DF4X-ray3.50F2-178[»]
3E1Belectron microscopy-22-179[»]
3E1Delectron microscopy-22-179[»]
3FIKelectron microscopy6.70F2-179[»]
3I1NX-ray3.19F1-179[»]
3I1PX-ray3.19F1-179[»]
3I1RX-ray3.81F1-179[»]
3I1TX-ray3.81F1-179[»]
3I20X-ray3.71F1-179[»]
3I22X-ray3.71F1-179[»]
3IZTelectron microscopy-G1-179[»]
3IZUelectron microscopy-G1-179[»]
3J01electron microscopy-F2-179[»]
3J0Telectron microscopy12.10G2-179[»]
3J0Welectron microscopy14.70G2-179[»]
3J0Yelectron microscopy13.50G2-179[»]
3J11electron microscopy13.10G2-179[»]
3J12electron microscopy11.50G2-179[»]
3J14electron microscopy11.50G2-179[»]
3J19electron microscopy8.30F2-178[»]
3J37electron microscopy9.80G2-179[»]
3J4Xelectron microscopy12.00F1-179[»]
3J50electron microscopy20.00F1-179[»]
3J51electron microscopy17.00F1-179[»]
3J52electron microscopy12.00F1-179[»]
3J54electron microscopy13.00F1-179[»]
3J56electron microscopy15.00F1-179[»]
3J58electron microscopy17.00F1-179[»]
3J5Aelectron microscopy12.00F1-179[»]
3J5Celectron microscopy17.00F1-179[»]
3J5Eelectron microscopy17.00F1-179[»]
3J5Gelectron microscopy20.00F1-179[»]
3J5Ielectron microscopy15.00F1-179[»]
3J5Kelectron microscopy9.00F1-179[»]
3J5Lelectron microscopy6.60F2-178[»]
3J5Oelectron microscopy6.80F1-179[»]
3J5Selectron microscopy7.50G2-179[»]
3J5Uelectron microscopy7.60G2-179[»]
3J5Welectron microscopy7.60G2-179[»]
3J7Zelectron microscopy3.90F1-179[»]
3KCRelectron microscopy-F1-179[»]
3OASX-ray3.25F2-179[»]
3OATX-ray3.25F2-178[»]
3OFCX-ray3.19F2-178[»]
3OFDX-ray3.19F2-179[»]
3OFQX-ray3.10F2-179[»]
3OFRX-ray3.10F2-178[»]
3OFZX-ray3.29F2-178[»]
3OG0X-ray3.29F2-179[»]
3ORBX-ray3.30F1-179[»]
3R8SX-ray3.00F2-178[»]
3R8TX-ray3.00F2-178[»]
3SGFX-ray3.20F1-179[»]
3UOSX-ray3.70F1-179[»]
4CSUelectron microscopy5.50F2-179[»]
4GARX-ray3.30F1-179[»]
4GAUX-ray3.30F1-179[»]
4KIXX-ray2.90F1-179[»]
4KIZX-ray2.90F1-179[»]
4KJ1X-ray2.90F1-179[»]
4KJ3X-ray2.90F1-179[»]
4KJ5X-ray2.90F1-179[»]
4KJ7X-ray2.90F1-179[»]
4KJ9X-ray2.90F1-179[»]
4KJBX-ray2.90F1-179[»]
4PEBX-ray2.95F2-178[»]
4PECX-ray2.95F2-178[»]
4TOMX-ray3.00F2-178[»]
4TOOX-ray3.00F2-178[»]
4TOVX-ray2.90F2-178[»]
4TOXX-ray2.90F2-178[»]
4TP1X-ray2.90F2-178[»]
4TP3X-ray2.90F2-178[»]
4TP5X-ray2.90F2-178[»]
4TP7X-ray2.90F2-178[»]
4TP9X-ray2.80F2-178[»]
4TPBX-ray2.80F2-178[»]
4TPDX-ray2.80F2-178[»]
4TPFX-ray2.80F2-178[»]
4WAPX-ray3.09F2-178[»]
4WARX-ray3.09F2-178[»]
ProteinModelPortaliP62399.
SMRiP62399. Positions 2-178.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62399.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiCOG0094.
HOGENOMiHOG000231311.
InParanoidiP62399.
KOiK02931.
OMAiEQVMFHE.
OrthoDBiEOG6M9F1R.
PhylomeDBiP62399.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
HAMAPiMF_01333_B. Ribosomal_L5_B.
InterProiIPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62399-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKLHDYYKD EVVKKLMTEF NYNSVMQVPR VEKITLNMGV GEAIADKKLL
60 70 80 90 100
DNAAADLAAI SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF
110 120 130 140 150
ERLITIAVPR IRDFRGLSAK SFDGRGNYSM GVREQIIFPE IDYDKVDRVR
160 170
GLDITITTTA KSDEEGRALL AAFDFPFRK
Length:179
Mass (Da):20,302
Last modified:January 23, 2007 - v2
Checksum:iB2E95A8BE4B8D2A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941E → Q AA sequence (PubMed:791672)Curated
Sequence conflicti127 – 1271N → D AA sequence (PubMed:791672)Curated

Mass spectrometryi

Molecular mass is 20169.8 Da from positions 2 - 179. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25717.1.
U18997 Genomic DNA. Translation: AAA58105.1.
U00096 Genomic DNA. Translation: AAC76333.1.
AP009048 Genomic DNA. Translation: BAE77983.1.
M10195 Genomic DNA. Translation: AAA24051.1.
PIRiG65123. R5EC5.
RefSeqiNP_417767.1. NC_000913.3.
YP_492124.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76333; AAC76333; b3308.
BAE77983; BAE77983; BAE77983.
GeneIDi12934390.
947800.
KEGGiecj:Y75_p3868.
eco:b3308.
PATRICi32122048. VBIEscCol129921_3401.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01563 Genomic DNA. Translation: CAA25717.1.
U18997 Genomic DNA. Translation: AAA58105.1.
U00096 Genomic DNA. Translation: AAC76333.1.
AP009048 Genomic DNA. Translation: BAE77983.1.
M10195 Genomic DNA. Translation: AAA24051.1.
PIRiG65123. R5EC5.
RefSeqiNP_417767.1. NC_000913.3.
YP_492124.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00g2-177[»]
1P85electron microscopy12.30D2-179[»]
1P86electron microscopy11.50D2-179[»]
1VS6X-ray3.46F1-179[»]
1VS8X-ray3.46F1-179[»]
1VT2X-ray3.30F1-179[»]
2AW4X-ray3.46F2-179[»]
2AWBX-ray3.46F2-179[»]
2GYAelectron microscopy15.00D3-179[»]
2GYCelectron microscopy15.00D3-179[»]
2I2TX-ray3.22F2-179[»]
2I2VX-ray3.22F2-179[»]
2J28electron microscopy8.00F2-179[»]
2QAMX-ray3.21F2-179[»]
2QAOX-ray3.21F2-179[»]
2QBAX-ray3.54F2-179[»]
2QBCX-ray3.54F2-179[»]
2QBEX-ray3.30F2-179[»]
2QBGX-ray3.30F2-179[»]
2QBIX-ray4.00F2-179[»]
2QBKX-ray4.00F2-179[»]
2QOVX-ray3.93F2-179[»]
2QOXX-ray3.93F2-179[»]
2QOZX-ray3.50F2-179[»]
2QP1X-ray3.50F2-179[»]
2RDOelectron microscopy9.10F2-179[»]
2VHMX-ray3.74F2-179[»]
2VHNX-ray3.74F2-179[»]
2WWQelectron microscopy5.80F2-179[»]
2Z4LX-ray4.45F2-179[»]
2Z4NX-ray4.45F2-179[»]
3BBXelectron microscopy10.00F2-179[»]
3DF2X-ray3.50F2-178[»]
3DF4X-ray3.50F2-178[»]
3E1Belectron microscopy-22-179[»]
3E1Delectron microscopy-22-179[»]
3FIKelectron microscopy6.70F2-179[»]
3I1NX-ray3.19F1-179[»]
3I1PX-ray3.19F1-179[»]
3I1RX-ray3.81F1-179[»]
3I1TX-ray3.81F1-179[»]
3I20X-ray3.71F1-179[»]
3I22X-ray3.71F1-179[»]
3IZTelectron microscopy-G1-179[»]
3IZUelectron microscopy-G1-179[»]
3J01electron microscopy-F2-179[»]
3J0Telectron microscopy12.10G2-179[»]
3J0Welectron microscopy14.70G2-179[»]
3J0Yelectron microscopy13.50G2-179[»]
3J11electron microscopy13.10G2-179[»]
3J12electron microscopy11.50G2-179[»]
3J14electron microscopy11.50G2-179[»]
3J19electron microscopy8.30F2-178[»]
3J37electron microscopy9.80G2-179[»]
3J4Xelectron microscopy12.00F1-179[»]
3J50electron microscopy20.00F1-179[»]
3J51electron microscopy17.00F1-179[»]
3J52electron microscopy12.00F1-179[»]
3J54electron microscopy13.00F1-179[»]
3J56electron microscopy15.00F1-179[»]
3J58electron microscopy17.00F1-179[»]
3J5Aelectron microscopy12.00F1-179[»]
3J5Celectron microscopy17.00F1-179[»]
3J5Eelectron microscopy17.00F1-179[»]
3J5Gelectron microscopy20.00F1-179[»]
3J5Ielectron microscopy15.00F1-179[»]
3J5Kelectron microscopy9.00F1-179[»]
3J5Lelectron microscopy6.60F2-178[»]
3J5Oelectron microscopy6.80F1-179[»]
3J5Selectron microscopy7.50G2-179[»]
3J5Uelectron microscopy7.60G2-179[»]
3J5Welectron microscopy7.60G2-179[»]
3J7Zelectron microscopy3.90F1-179[»]
3KCRelectron microscopy-F1-179[»]
3OASX-ray3.25F2-179[»]
3OATX-ray3.25F2-178[»]
3OFCX-ray3.19F2-178[»]
3OFDX-ray3.19F2-179[»]
3OFQX-ray3.10F2-179[»]
3OFRX-ray3.10F2-178[»]
3OFZX-ray3.29F2-178[»]
3OG0X-ray3.29F2-179[»]
3ORBX-ray3.30F1-179[»]
3R8SX-ray3.00F2-178[»]
3R8TX-ray3.00F2-178[»]
3SGFX-ray3.20F1-179[»]
3UOSX-ray3.70F1-179[»]
4CSUelectron microscopy5.50F2-179[»]
4GARX-ray3.30F1-179[»]
4GAUX-ray3.30F1-179[»]
4KIXX-ray2.90F1-179[»]
4KIZX-ray2.90F1-179[»]
4KJ1X-ray2.90F1-179[»]
4KJ3X-ray2.90F1-179[»]
4KJ5X-ray2.90F1-179[»]
4KJ7X-ray2.90F1-179[»]
4KJ9X-ray2.90F1-179[»]
4KJBX-ray2.90F1-179[»]
4PEBX-ray2.95F2-178[»]
4PECX-ray2.95F2-178[»]
4TOMX-ray3.00F2-178[»]
4TOOX-ray3.00F2-178[»]
4TOVX-ray2.90F2-178[»]
4TOXX-ray2.90F2-178[»]
4TP1X-ray2.90F2-178[»]
4TP3X-ray2.90F2-178[»]
4TP5X-ray2.90F2-178[»]
4TP7X-ray2.90F2-178[»]
4TP9X-ray2.80F2-178[»]
4TPBX-ray2.80F2-178[»]
4TPDX-ray2.80F2-178[»]
4TPFX-ray2.80F2-178[»]
4WAPX-ray3.09F2-178[»]
4WARX-ray3.09F2-178[»]
ProteinModelPortaliP62399.
SMRiP62399. Positions 2-178.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi852112. 1 interaction.
DIPiDIP-35914N.
IntActiP62399. 71 interactions.
MINTiMINT-1238892.
STRINGi511145.b3308.

Chemistry

ChEMBLiCHEMBL2363135.

Proteomic databases

PaxDbiP62399.
PRIDEiP62399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76333; AAC76333; b3308.
BAE77983; BAE77983; BAE77983.
GeneIDi12934390.
947800.
KEGGiecj:Y75_p3868.
eco:b3308.
PATRICi32122048. VBIEscCol129921_3401.

Organism-specific databases

EchoBASEiEB0861.
EcoGeneiEG10868. rplE.

Phylogenomic databases

eggNOGiCOG0094.
HOGENOMiHOG000231311.
InParanoidiP62399.
KOiK02931.
OMAiEQVMFHE.
OrthoDBiEOG6M9F1R.
PhylomeDBiP62399.

Enzyme and pathway databases

BioCyciEcoCyc:EG10868-MONOMER.
ECOL316407:JW3270-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP62399.
PROiP62399.

Gene expression databases

GenevestigatoriP62399.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
HAMAPiMF_01333_B. Ribosomal_L5_B.
InterProiIPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
    Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
    Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "The primary structure of the 5 S RNA binding protein L5 of Escherichia coli ribosomes."
    Chen R., Ehrke G.
    FEBS Lett. 69:240-245(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-179.
    Strain: K.
  5. "Translational regulation by ribosomal protein S8 in Escherichia coli: structural homology between rRNA binding site and feedback target on mRNA."
    Olins P.O., Nomura M.
    Nucleic Acids Res. 9:1757-1764(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
    Strain: K12 / JM105 / ATCC 47016.
  6. "Stoichiometry, cooperativity, and stability of interactions between 5S RNA and proteins L5, L18, and L25 from the 50S ribosomal subunit of Escherichia coli."
    Spierer P., Zimmermann R.A.
    Biochemistry 17:2474-2479(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: FORMATION OF THE 5S RRNA/L5/L18/L25 SUBCOMPLEX.
    Strain: MRE-600.
  7. "Assembly map of the large subunit (50S) of Escherichia coli ribosomes."
    Rohl R., Nierhaus K.H.
    Proc. Natl. Acad. Sci. U.S.A. 79:729-733(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: REQUIREMENT FOR INCORPORATION OF 5S RRNA INTO THE 50S SUBUNIT.
    Strain: MRE-600.
  8. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
    Osswald M., Doering T., Brimacombe R.
    Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
    Strain: MRE-600.
  9. "5S rRNA sugar-phosphate backbone protection in complexes with specific ribosomal proteins."
    Shpanchenko O.V., Zvereva M.I., Dontsova O.A., Nierhaus K.H., Bogdanov A.A.
    FEBS Lett. 394:71-75(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF A 5S RRNA/L5/L18/L25 SUBCOMPLEX.
    Strain: K12 / A19.
  10. "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.
  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. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  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), INTERSUBUNIT BRIDGE FORMATION.
    Strain: MRE-600.
  14. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON TRANSLOCATION.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES INCLUDING 2 CONFORMATIONS OF INTERSUBUNIT BRIDGE B1B.

Entry informationi

Entry nameiRL5_ECOLI
AccessioniPrimary (citable) accession number: P62399
Secondary accession number(s): P02389, Q2M6X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 115 of the entry and version 2 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.