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P62399

- RL5_ECOLI

UniProt

P62399 - RL5_ECOLI

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Protein
50S ribosomal protein L5
Gene
rplE, b3308, JW3270
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation
In the 70S ribosome in the initiation state (1 Publication) 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 (1 Publication and 1 Publication). In the two 3.5 A resolved ribosome structures (1 Publication) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction.UniRule annotation
Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.UniRule annotation

GO - Molecular functioni

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

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 L5UniRule annotation
PRO_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 S19.3 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 97
Turni10 – 123
Helixi13 – 208
Helixi25 – 273
Beta strandi31 – 377
Helixi42 – 443
Helixi48 – 6013
Beta strandi61 – 633
Beta strandi66 – 694
Beta strandi71 – 733
Turni75 – 784
Beta strandi81 – 833
Beta strandi84 – 918
Helixi93 – 10513
Turni106 – 1105
Beta strandi111 – 1133
Beta strandi124 – 1263
Beta strandi128 – 1336
Helixi135 – 1373
Helixi139 – 1413
Helixi143 – 1453
Beta strandi153 – 1597
Helixi163 – 1719
Turni172 – 1743

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortaliP62399.
SMRiP62399. Positions 2-178.

Miscellaneous databases

EvolutionaryTraceiP62399.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0094.
HOGENOMiHOG000231311.
KOiK02931.
OMAiTEQLIFP.
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

MAKLHDYYKD EVVKKLMTEF NYNSVMQVPR VEKITLNMGV GEAIADKKLL    50
DNAAADLAAI SGQKPLITKA RKSVAGFKIR QGYPIGCKVT LRGERMWEFF 100
ERLITIAVPR IRDFRGLSAK SFDGRGNYSM GVREQIIFPE IDYDKVDRVR 150
GLDITITTTA KSDEEGRALL AAFDFPFRK 179
Length:179
Mass (Da):20,302
Last modified:January 23, 2007 - v2
Checksum:iB2E95A8BE4B8D2A7
GO

Mass spectrometryi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941E → Q AA sequence 1 Publication
Sequence conflicti127 – 1271N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi G65123. R5EC5.
RefSeqi NP_417767.1. NC_000913.3.
YP_492124.1. 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 g 2-177 [» ]
1P85 electron microscopy 12.30 D 2-179 [» ]
1P86 electron microscopy 11.50 D 2-179 [» ]
1VS6 X-ray 3.46 F 1-179 [» ]
1VS8 X-ray 3.46 F 1-179 [» ]
1VT2 X-ray 3.30 F 1-179 [» ]
2AW4 X-ray 3.46 F 2-179 [» ]
2AWB X-ray 3.46 F 2-179 [» ]
2GYA electron microscopy 15.00 D 3-179 [» ]
2GYC electron microscopy 15.00 D 3-179 [» ]
2I2T X-ray 3.22 F 2-179 [» ]
2I2V X-ray 3.22 F 2-179 [» ]
2J28 electron microscopy 8.00 F 2-179 [» ]
2QAM X-ray 3.21 F 2-179 [» ]
2QAO X-ray 3.21 F 2-179 [» ]
2QBA X-ray 3.54 F 2-179 [» ]
2QBC X-ray 3.54 F 2-179 [» ]
2QBE X-ray 3.30 F 2-179 [» ]
2QBG X-ray 3.30 F 2-179 [» ]
2QBI X-ray 4.00 F 2-179 [» ]
2QBK X-ray 4.00 F 2-179 [» ]
2QOV X-ray 3.93 F 2-179 [» ]
2QOX X-ray 3.93 F 2-179 [» ]
2QOZ X-ray 3.50 F 2-179 [» ]
2QP1 X-ray 3.50 F 2-179 [» ]
2RDO electron microscopy 9.10 F 2-179 [» ]
2VHM X-ray 3.74 F 2-179 [» ]
2VHN X-ray 3.74 F 2-179 [» ]
2WWQ electron microscopy 5.80 F 2-179 [» ]
2Z4L X-ray 4.45 F 2-179 [» ]
2Z4N X-ray 4.45 F 2-179 [» ]
3BBX electron microscopy 10.00 F 2-179 [» ]
3DF2 X-ray 3.50 F 2-178 [» ]
3DF4 X-ray 3.50 F 2-178 [» ]
3E1B electron microscopy - 2 2-179 [» ]
3E1D electron microscopy - 2 2-179 [» ]
3FIK electron microscopy 6.70 F 2-179 [» ]
3I1N X-ray 3.19 F 1-179 [» ]
3I1P X-ray 3.19 F 1-179 [» ]
3I1R X-ray 3.81 F 1-179 [» ]
3I1T X-ray 3.81 F 1-179 [» ]
3I20 X-ray 3.71 F 1-179 [» ]
3I22 X-ray 3.71 F 1-179 [» ]
3IZT electron microscopy - G 1-179 [» ]
3IZU electron microscopy - G 1-179 [» ]
3J01 electron microscopy - F 2-179 [» ]
3J0T electron microscopy 12.10 G 2-179 [» ]
3J0W electron microscopy 14.70 G 2-179 [» ]
3J0Y electron microscopy 13.50 G 2-179 [» ]
3J11 electron microscopy 13.10 G 2-179 [» ]
3J12 electron microscopy 11.50 G 2-179 [» ]
3J14 electron microscopy 11.50 G 2-179 [» ]
3J19 electron microscopy 8.30 F 2-178 [» ]
3J37 electron microscopy 9.80 G 2-179 [» ]
3J4X electron microscopy 12.00 F 1-179 [» ]
3J50 electron microscopy 20.00 F 1-179 [» ]
3J51 electron microscopy 17.00 F 1-179 [» ]
3J52 electron microscopy 12.00 F 1-179 [» ]
3J54 electron microscopy 13.00 F 1-179 [» ]
3J56 electron microscopy 15.00 F 1-179 [» ]
3J58 electron microscopy 17.00 F 1-179 [» ]
3J5A electron microscopy 12.00 F 1-179 [» ]
3J5C electron microscopy 17.00 F 1-179 [» ]
3J5E electron microscopy 17.00 F 1-179 [» ]
3J5G electron microscopy 20.00 F 1-179 [» ]
3J5I electron microscopy 15.00 F 1-179 [» ]
3J5K electron microscopy 9.00 F 1-179 [» ]
3J5L electron microscopy 6.60 F 2-178 [» ]
3J5O electron microscopy 6.80 F 1-179 [» ]
3J5S electron microscopy 7.50 G 2-179 [» ]
3J5U electron microscopy 7.60 G 2-179 [» ]
3J5W electron microscopy 7.60 G 2-179 [» ]
3KCR electron microscopy - F 1-179 [» ]
3OAS X-ray 3.25 F 2-179 [» ]
3OAT X-ray 3.25 F 2-178 [» ]
3OFC X-ray 3.19 F 2-178 [» ]
3OFD X-ray 3.19 F 2-179 [» ]
3OFQ X-ray 3.10 F 2-179 [» ]
3OFR X-ray 3.10 F 2-178 [» ]
3OFZ X-ray 3.29 F 2-178 [» ]
3OG0 X-ray 3.29 F 2-179 [» ]
3ORB X-ray 3.30 F 1-179 [» ]
3R8S X-ray 3.00 F 2-178 [» ]
3R8T X-ray 3.00 F 2-178 [» ]
3SGF X-ray 3.20 F 1-179 [» ]
3UOS X-ray 3.70 F 1-179 [» ]
4CSU electron microscopy 5.50 F 2-179 [» ]
4GAR X-ray 3.30 F 1-179 [» ]
4GAU X-ray 3.30 F 1-179 [» ]
4KIX X-ray 2.90 F 1-179 [» ]
4KIZ X-ray 2.90 F 1-179 [» ]
4KJ1 X-ray 2.90 F 1-179 [» ]
4KJ3 X-ray 2.90 F 1-179 [» ]
4KJ5 X-ray 2.90 F 1-179 [» ]
4KJ7 X-ray 2.90 F 1-179 [» ]
4KJ9 X-ray 2.90 F 1-179 [» ]
4KJB X-ray 2.90 F 1-179 [» ]
ProteinModelPortali P62399.
SMRi P62399. Positions 2-178.
ModBasei Search...

Protein-protein interaction databases

BioGridi 852112. 1 interaction.
DIPi DIP-35914N.
IntActi P62399. 71 interactions.
MINTi MINT-1238892.
STRINGi 511145.b3308.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P62399.
PRIDEi P62399.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76333 ; AAC76333 ; b3308 .
BAE77983 ; BAE77983 ; BAE77983 .
GeneIDi 12934390.
947800.
KEGGi ecj:Y75_p3868.
eco:b3308.
PATRICi 32122048. VBIEscCol129921_3401.

Organism-specific databases

EchoBASEi EB0861.
EcoGenei EG10868. rplE.

Phylogenomic databases

eggNOGi COG0094.
HOGENOMi HOG000231311.
KOi K02931.
OMAi TEQLIFP.
OrthoDBi EOG6M9F1R.
PhylomeDBi P62399.

Enzyme and pathway databases

BioCyci EcoCyc:EG10868-MONOMER.
ECOL316407:JW3270-MONOMER.

Miscellaneous databases

EvolutionaryTracei P62399.
PROi P62399.

Gene expression databases

Genevestigatori P62399.

Family and domain databases

Gene3Di 3.30.1440.10. 1 hit.
HAMAPi MF_01333_B. Ribosomal_L5_B.
InterProi IPR002132. Ribosomal_L5.
IPR020930. Ribosomal_L5_bac-type.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view ]
PANTHERi PTHR11994. PTHR11994. 1 hit.
Pfami PF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMi SSF55282. SSF55282. 1 hit.
PROSITEi PS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 111 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

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