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P0A7L3

- RL20_ECOLI

UniProt

P0A7L3 - RL20_ECOLI

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Protein

50S ribosomal protein L20

Gene

rplT

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

Functioni

One of the primary rRNA binding proteins, it binds close to the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: EcoCyc
  3. translation repressor activity, nucleic acid binding Source: EcoCyc

GO - Biological processi

  1. negative regulation of translation Source: GOC
  2. ribosomal large subunit assembly Source: EcoCyc
  3. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10881-MONOMER.
ECOL316407:JW1706-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L20
Gene namesi
Name:rplT
Synonyms:pdzA
Ordered Locus Names:b1716, JW1706
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10881. rplT.

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 – 11811750S ribosomal protein L20PRO_0000177156Add
BLAST

Proteomic databases

PaxDbiP0A7L3.
PRIDEiP0A7L3.

Expressioni

Gene expression databases

GenevestigatoriP0A7L3.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts L21 (PubMed:2665813).1 Publication

Protein-protein interaction databases

DIPiDIP-47941N.
IntActiP0A7L3. 35 interactions.
MINTiMINT-1321645.
STRINGi511145.b1716.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014Combined sources
Turni21 – 233Combined sources
Helixi27 – 304Combined sources
Helixi32 – 7140Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 8510Combined sources
Beta strandi86 – 883Combined sources
Helixi92 – 10110Combined sources
Helixi103 – 11715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30O2-118[»]
1P86electron microscopy11.50O2-118[»]
1VS6X-ray3.46Q1-118[»]
1VS8X-ray3.46Q1-118[»]
1VT2X-ray3.30Q1-118[»]
2AW4X-ray3.46Q2-118[»]
2AWBX-ray3.46Q2-118[»]
2GYAelectron microscopy15.00O3-117[»]
2GYCelectron microscopy15.00O3-117[»]
2I2TX-ray3.22Q2-118[»]
2I2VX-ray3.22Q2-118[»]
2J28electron microscopy8.00Q2-118[»]
2QAMX-ray3.21Q2-118[»]
2QAOX-ray3.21Q2-118[»]
2QBAX-ray3.54Q2-118[»]
2QBCX-ray3.54Q2-118[»]
2QBEX-ray3.30Q2-118[»]
2QBGX-ray3.30Q2-118[»]
2QBIX-ray4.00Q2-118[»]
2QBKX-ray4.00Q2-118[»]
2QOVX-ray3.93Q2-118[»]
2QOXX-ray3.93Q2-118[»]
2QOZX-ray3.50Q2-118[»]
2QP1X-ray3.50Q2-118[»]
2RDOelectron microscopy9.10Q2-118[»]
2VHMX-ray3.74Q2-118[»]
2VHNX-ray3.74Q2-118[»]
2WWQelectron microscopy5.80Q2-118[»]
2Z4LX-ray4.45Q2-118[»]
2Z4NX-ray4.45Q2-118[»]
3BBXelectron microscopy10.00Q2-118[»]
3DF2X-ray3.50Q2-117[»]
3DF4X-ray3.50Q2-117[»]
3E1Belectron microscopy-J1-118[»]
3E1Delectron microscopy-J1-118[»]
3FIKelectron microscopy6.70Q2-118[»]
3I1NX-ray3.19Q1-118[»]
3I1PX-ray3.19Q1-118[»]
3I1RX-ray3.81Q1-118[»]
3I1TX-ray3.81Q1-118[»]
3I20X-ray3.71Q1-118[»]
3I22X-ray3.71Q1-118[»]
3IZTelectron microscopy-R1-118[»]
3IZUelectron microscopy-R1-118[»]
3J01electron microscopy-Q2-118[»]
3J0Telectron microscopy12.10S2-118[»]
3J0Welectron microscopy14.70S2-118[»]
3J0Yelectron microscopy13.50S2-118[»]
3J11electron microscopy13.10S2-118[»]
3J12electron microscopy11.50S2-118[»]
3J14electron microscopy11.50S2-118[»]
3J19electron microscopy8.30Q2-118[»]
3J37electron microscopy9.80U2-118[»]
3J4Xelectron microscopy12.00Q1-118[»]
3J50electron microscopy20.00Q1-118[»]
3J51electron microscopy17.00Q1-118[»]
3J52electron microscopy12.00Q1-118[»]
3J54electron microscopy13.00Q1-118[»]
3J56electron microscopy15.00Q1-118[»]
3J58electron microscopy17.00Q1-118[»]
3J5Aelectron microscopy12.00Q1-118[»]
3J5Celectron microscopy17.00Q1-118[»]
3J5Eelectron microscopy17.00Q1-118[»]
3J5Gelectron microscopy20.00Q1-118[»]
3J5Ielectron microscopy15.00Q1-118[»]
3J5Kelectron microscopy9.00Q1-118[»]
3J5Lelectron microscopy6.60Q2-118[»]
3J5Oelectron microscopy6.80Q1-118[»]
3J5Uelectron microscopy7.60S2-118[»]
3J5Welectron microscopy7.60T2-118[»]
3KCRelectron microscopy-Q1-118[»]
3OASX-ray3.25Q2-118[»]
3OATX-ray3.25Q2-118[»]
3OFCX-ray3.19Q2-118[»]
3OFDX-ray3.19Q2-118[»]
3OFQX-ray3.10Q2-118[»]
3OFRX-ray3.10Q2-118[»]
3OFZX-ray3.29Q2-118[»]
3OG0X-ray3.29Q2-118[»]
3ORBX-ray3.30Q1-118[»]
3R8SX-ray3.00Q2-118[»]
3R8TX-ray3.00Q2-118[»]
3SGFX-ray3.20U1-118[»]
3UOSX-ray3.70U1-118[»]
4CSUelectron microscopy5.50Q2-118[»]
4GARX-ray3.30Q1-118[»]
4GAUX-ray3.30Q1-118[»]
4KIXX-ray2.90Q1-118[»]
4KIZX-ray2.90Q1-118[»]
4KJ1X-ray2.90Q1-118[»]
4KJ3X-ray2.90Q1-118[»]
4KJ5X-ray2.90Q1-118[»]
4KJ7X-ray2.90Q1-118[»]
4KJ9X-ray2.90Q1-118[»]
4KJBX-ray2.90Q1-118[»]
4PEBX-ray2.95Q2-118[»]
4PECX-ray2.95Q2-118[»]
4TOMX-ray3.00Q2-118[»]
4TOOX-ray3.00Q2-118[»]
4TOVX-ray2.90Q2-118[»]
4TOXX-ray2.90Q2-118[»]
4TP1X-ray2.90Q2-118[»]
4TP3X-ray2.90Q2-118[»]
4TP5X-ray2.90Q2-118[»]
4TP7X-ray2.90Q2-118[»]
4TP9X-ray2.80Q2-118[»]
4TPBX-ray2.80Q2-118[»]
4TPDX-ray2.80Q2-118[»]
4TPFX-ray2.80Q2-118[»]
ProteinModelPortaliP0A7L3.
SMRiP0A7L3. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7L3.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L20P family.Curated

Phylogenomic databases

eggNOGiCOG0292.
HOGENOMiHOG000035046.
InParanoidiP0A7L3.
KOiK02887.
OMAiFISEPIN.
OrthoDBiEOG6CGCMB.
PhylomeDBiP0A7L3.

Family and domain databases

HAMAPiMF_00382. Ribosomal_L20.
InterProiIPR005813. Ribosomal_L20.
[Graphical view]
PANTHERiPTHR10986. PTHR10986. 1 hit.
PfamiPF00453. Ribosomal_L20. 1 hit.
[Graphical view]
PRINTSiPR00062. RIBOSOMALL20.
TIGRFAMsiTIGR01032. rplT_bact. 1 hit.
PROSITEiPS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0A7L3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARVKRGVIA RARHKKILKQ AKGYYGARSR VYRVAFQAVI KAGQYAYRDR
60 70 80 90 100
RQRKRQFRQL WIARINAAAR QNGISYSKFI NGLKKASVEI DRKILADIAV
110
FDKVAFTALV EKAKAALA
Length:118
Mass (Da):13,497
Last modified:January 23, 2007 - v2
Checksum:iE60AFDBB6F05DFB3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331R → A in CAA23562. (PubMed:6317865)Curated
Sequence conflicti33 – 331R → A in AAA51468. (PubMed:6317865)Curated

Mass spectrometryi

Molecular mass is 13366.9 Da from positions 2 - 118. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. Translation: CAA23562.1.
K02844 Genomic DNA. Translation: AAA51468.1.
U00096 Genomic DNA. Translation: AAC74786.1.
AP009048 Genomic DNA. Translation: BAA15483.1.
M10423 Genomic DNA. Translation: AAA23960.1.
PIRiD64930. R5EC20.
RefSeqiNP_416231.1. NC_000913.3.
YP_489978.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74786; AAC74786; b1716.
BAA15483; BAA15483; BAA15483.
GeneIDi12931309.
945152.
KEGGiecj:Y75_p1691.
eco:b1716.
PATRICi32118736. VBIEscCol129921_1786.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00291 Genomic DNA. Translation: CAA23562.1 .
K02844 Genomic DNA. Translation: AAA51468.1 .
U00096 Genomic DNA. Translation: AAC74786.1 .
AP009048 Genomic DNA. Translation: BAA15483.1 .
M10423 Genomic DNA. Translation: AAA23960.1 .
PIRi D64930. R5EC20.
RefSeqi NP_416231.1. NC_000913.3.
YP_489978.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P85 electron microscopy 12.30 O 2-118 [» ]
1P86 electron microscopy 11.50 O 2-118 [» ]
1VS6 X-ray 3.46 Q 1-118 [» ]
1VS8 X-ray 3.46 Q 1-118 [» ]
1VT2 X-ray 3.30 Q 1-118 [» ]
2AW4 X-ray 3.46 Q 2-118 [» ]
2AWB X-ray 3.46 Q 2-118 [» ]
2GYA electron microscopy 15.00 O 3-117 [» ]
2GYC electron microscopy 15.00 O 3-117 [» ]
2I2T X-ray 3.22 Q 2-118 [» ]
2I2V X-ray 3.22 Q 2-118 [» ]
2J28 electron microscopy 8.00 Q 2-118 [» ]
2QAM X-ray 3.21 Q 2-118 [» ]
2QAO X-ray 3.21 Q 2-118 [» ]
2QBA X-ray 3.54 Q 2-118 [» ]
2QBC X-ray 3.54 Q 2-118 [» ]
2QBE X-ray 3.30 Q 2-118 [» ]
2QBG X-ray 3.30 Q 2-118 [» ]
2QBI X-ray 4.00 Q 2-118 [» ]
2QBK X-ray 4.00 Q 2-118 [» ]
2QOV X-ray 3.93 Q 2-118 [» ]
2QOX X-ray 3.93 Q 2-118 [» ]
2QOZ X-ray 3.50 Q 2-118 [» ]
2QP1 X-ray 3.50 Q 2-118 [» ]
2RDO electron microscopy 9.10 Q 2-118 [» ]
2VHM X-ray 3.74 Q 2-118 [» ]
2VHN X-ray 3.74 Q 2-118 [» ]
2WWQ electron microscopy 5.80 Q 2-118 [» ]
2Z4L X-ray 4.45 Q 2-118 [» ]
2Z4N X-ray 4.45 Q 2-118 [» ]
3BBX electron microscopy 10.00 Q 2-118 [» ]
3DF2 X-ray 3.50 Q 2-117 [» ]
3DF4 X-ray 3.50 Q 2-117 [» ]
3E1B electron microscopy - J 1-118 [» ]
3E1D electron microscopy - J 1-118 [» ]
3FIK electron microscopy 6.70 Q 2-118 [» ]
3I1N X-ray 3.19 Q 1-118 [» ]
3I1P X-ray 3.19 Q 1-118 [» ]
3I1R X-ray 3.81 Q 1-118 [» ]
3I1T X-ray 3.81 Q 1-118 [» ]
3I20 X-ray 3.71 Q 1-118 [» ]
3I22 X-ray 3.71 Q 1-118 [» ]
3IZT electron microscopy - R 1-118 [» ]
3IZU electron microscopy - R 1-118 [» ]
3J01 electron microscopy - Q 2-118 [» ]
3J0T electron microscopy 12.10 S 2-118 [» ]
3J0W electron microscopy 14.70 S 2-118 [» ]
3J0Y electron microscopy 13.50 S 2-118 [» ]
3J11 electron microscopy 13.10 S 2-118 [» ]
3J12 electron microscopy 11.50 S 2-118 [» ]
3J14 electron microscopy 11.50 S 2-118 [» ]
3J19 electron microscopy 8.30 Q 2-118 [» ]
3J37 electron microscopy 9.80 U 2-118 [» ]
3J4X electron microscopy 12.00 Q 1-118 [» ]
3J50 electron microscopy 20.00 Q 1-118 [» ]
3J51 electron microscopy 17.00 Q 1-118 [» ]
3J52 electron microscopy 12.00 Q 1-118 [» ]
3J54 electron microscopy 13.00 Q 1-118 [» ]
3J56 electron microscopy 15.00 Q 1-118 [» ]
3J58 electron microscopy 17.00 Q 1-118 [» ]
3J5A electron microscopy 12.00 Q 1-118 [» ]
3J5C electron microscopy 17.00 Q 1-118 [» ]
3J5E electron microscopy 17.00 Q 1-118 [» ]
3J5G electron microscopy 20.00 Q 1-118 [» ]
3J5I electron microscopy 15.00 Q 1-118 [» ]
3J5K electron microscopy 9.00 Q 1-118 [» ]
3J5L electron microscopy 6.60 Q 2-118 [» ]
3J5O electron microscopy 6.80 Q 1-118 [» ]
3J5U electron microscopy 7.60 S 2-118 [» ]
3J5W electron microscopy 7.60 T 2-118 [» ]
3KCR electron microscopy - Q 1-118 [» ]
3OAS X-ray 3.25 Q 2-118 [» ]
3OAT X-ray 3.25 Q 2-118 [» ]
3OFC X-ray 3.19 Q 2-118 [» ]
3OFD X-ray 3.19 Q 2-118 [» ]
3OFQ X-ray 3.10 Q 2-118 [» ]
3OFR X-ray 3.10 Q 2-118 [» ]
3OFZ X-ray 3.29 Q 2-118 [» ]
3OG0 X-ray 3.29 Q 2-118 [» ]
3ORB X-ray 3.30 Q 1-118 [» ]
3R8S X-ray 3.00 Q 2-118 [» ]
3R8T X-ray 3.00 Q 2-118 [» ]
3SGF X-ray 3.20 U 1-118 [» ]
3UOS X-ray 3.70 U 1-118 [» ]
4CSU electron microscopy 5.50 Q 2-118 [» ]
4GAR X-ray 3.30 Q 1-118 [» ]
4GAU X-ray 3.30 Q 1-118 [» ]
4KIX X-ray 2.90 Q 1-118 [» ]
4KIZ X-ray 2.90 Q 1-118 [» ]
4KJ1 X-ray 2.90 Q 1-118 [» ]
4KJ3 X-ray 2.90 Q 1-118 [» ]
4KJ5 X-ray 2.90 Q 1-118 [» ]
4KJ7 X-ray 2.90 Q 1-118 [» ]
4KJ9 X-ray 2.90 Q 1-118 [» ]
4KJB X-ray 2.90 Q 1-118 [» ]
4PEB X-ray 2.95 Q 2-118 [» ]
4PEC X-ray 2.95 Q 2-118 [» ]
4TOM X-ray 3.00 Q 2-118 [» ]
4TOO X-ray 3.00 Q 2-118 [» ]
4TOV X-ray 2.90 Q 2-118 [» ]
4TOX X-ray 2.90 Q 2-118 [» ]
4TP1 X-ray 2.90 Q 2-118 [» ]
4TP3 X-ray 2.90 Q 2-118 [» ]
4TP5 X-ray 2.90 Q 2-118 [» ]
4TP7 X-ray 2.90 Q 2-118 [» ]
4TP9 X-ray 2.80 Q 2-118 [» ]
4TPB X-ray 2.80 Q 2-118 [» ]
4TPD X-ray 2.80 Q 2-118 [» ]
4TPF X-ray 2.80 Q 2-118 [» ]
ProteinModelPortali P0A7L3.
SMRi P0A7L3. Positions 2-118.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47941N.
IntActi P0A7L3. 35 interactions.
MINTi MINT-1321645.
STRINGi 511145.b1716.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P0A7L3.
PRIDEi P0A7L3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74786 ; AAC74786 ; b1716 .
BAA15483 ; BAA15483 ; BAA15483 .
GeneIDi 12931309.
945152.
KEGGi ecj:Y75_p1691.
eco:b1716.
PATRICi 32118736. VBIEscCol129921_1786.

Organism-specific databases

EchoBASEi EB0874.
EcoGenei EG10881. rplT.

Phylogenomic databases

eggNOGi COG0292.
HOGENOMi HOG000035046.
InParanoidi P0A7L3.
KOi K02887.
OMAi FISEPIN.
OrthoDBi EOG6CGCMB.
PhylomeDBi P0A7L3.

Enzyme and pathway databases

BioCyci EcoCyc:EG10881-MONOMER.
ECOL316407:JW1706-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0A7L3.
PROi P0A7L3.

Gene expression databases

Genevestigatori P0A7L3.

Family and domain databases

HAMAPi MF_00382. Ribosomal_L20.
InterProi IPR005813. Ribosomal_L20.
[Graphical view ]
PANTHERi PTHR10986. PTHR10986. 1 hit.
Pfami PF00453. Ribosomal_L20. 1 hit.
[Graphical view ]
PRINTSi PR00062. RIBOSOMALL20.
TIGRFAMsi TIGR01032. rplT_bact. 1 hit.
PROSITEi PS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Escherichia coli phenylalanyl-tRNA synthetase operon region. Evidence for an attenuation mechanism. Identification of the gene for the ribosomal protein L20."
    Fayat G., Mayaux J.-F., Sacerdot C., Fromant M., Springer M., Grunberg-Manago M., Blanquet S.
    J. Mol. Biol. 171:239-261(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Primary structure of the himA gene of Escherichia coli: homology with DNA-binding protein HU and association with the phenylalanyl-tRNA synthetase operon."
    Miller H.I.
    Cold Spring Harb. Symp. Quant. Biol. 49:691-698(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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.
  6. "The primary structure of protein L20 from the large subunit of the Escherichia coli ribosome."
    Wittmann-Liebold B., Seib C.
    FEBS Lett. 103:61-65(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-118.
    Strain: K12.
  7. "Attenuation control of the Escherichia coli phenylalanyl-tRNA synthetase operon."
    Springer M., Mayaux J.-F., Fayat G., Plumbridge J.A., Graffe M., Blanquet S., Grunberg-Manago M.
    J. Mol. Biol. 181:467-478(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-118.
  8. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
    Herold M., Nierhaus K.H.
    J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
    Strain: K12.
  9. "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 L21.
  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] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  11. "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.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL20_ECOLI
AccessioniPrimary (citable) accession number: P0A7L3
Secondary accession number(s): P02421, Q47253
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 100 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