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P0A7L3 (RL20_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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 L20
Gene names
Name:rplT
Synonyms:pdzA
Ordered Locus Names:b1716, JW1706
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_00382

Subunit structure

Part of the 50S ribosomal subunit. Contacts L21 (Ref.9). Ref.8

Sequence similarities

Belongs to the ribosomal protein L20P family.

Mass spectrometry

Molecular mass is 13366.9 Da from positions 2 - 118. Determined by MALDI. Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 11811750S ribosomal protein L20 HAMAP-Rule MF_00382
PRO_0000177156

Experimental info

Sequence conflict331R → A in CAA23562. Ref.1
Sequence conflict331R → A in AAA51468. Ref.1

Secondary structure

.................. 118
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7L3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E60AFDBB6F05DFB3

FASTA11813,497
        10         20         30         40         50         60 
MARVKRGVIA RARHKKILKQ AKGYYGARSR VYRVAFQAVI KAGQYAYRDR RQRKRQFRQL 

        70         80         90        100        110 
WIARINAAAR QNGISYSKFI NGLKKASVEI DRKILADIAV FDKVAFTALV EKAKAALA 

« Hide

References

« Hide 'large scale' references
[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]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"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.
[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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRR5EC20. D64930.
RefSeqNP_416231.1. NC_000913.3.
YP_489978.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
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[»]
ProteinModelPortalP0A7L3.
SMRP0A7L3. Positions 2-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47941N.
IntActP0A7L3. 35 interactions.
MINTMINT-1321645.
STRING511145.b1716.

Chemistry

ChEMBLCHEMBL2363135.

Proteomic databases

PaxDbP0A7L3.
PRIDEP0A7L3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74786; AAC74786; b1716.
BAA15483; BAA15483; BAA15483.
GeneID12931309.
945152.
KEGGecj:Y75_p1691.
eco:b1716.
PATRIC32118736. VBIEscCol129921_1786.

Organism-specific databases

EchoBASEEB0874.
EcoGeneEG10881. rplT.

Phylogenomic databases

eggNOGCOG0292.
HOGENOMHOG000035046.
KOK02887.
OMAFISEPIN.
OrthoDBEOG6CGCMB.
PhylomeDBP0A7L3.

Enzyme and pathway databases

BioCycEcoCyc:EG10881-MONOMER.
ECOL316407:JW1706-MONOMER.

Gene expression databases

GenevestigatorP0A7L3.

Family and domain databases

HAMAPMF_00382. Ribosomal_L20.
InterProIPR005813. Ribosomal_L20.
[Graphical view]
PANTHERPTHR10986. PTHR10986. 1 hit.
PfamPF00453. Ribosomal_L20. 1 hit.
[Graphical view]
PRINTSPR00062. RIBOSOMALL20.
TIGRFAMsTIGR01032. rplT_bact. 1 hit.
PROSITEPS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7L3.
PROP0A7L3.

Entry information

Entry nameRL20_ECOLI
AccessionPrimary (citable) accession number: P0A7L3
Secondary accession number(s): P02421, Q47253
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 96 of the entry and version 2 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