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Reviewed, UniProtKB/Swiss-Prot P0A7L3 (RL20_ECOLI)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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 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 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
P0A7L3-1 [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: 6317865] [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: 6397321] [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: 9097039] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 381019] [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: 3158742] [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: 3298242] [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: 2665813] [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: 10094780] [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: 12809609] [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: 16272117] [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

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.
RefSeqAP_002336.1.
NP_416231.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30O2-118[»]
1P86electron microscopy11.50O2-118[»]
1VS6X-ray3.46Q1-118[»]
1VS8X-ray3.46Q1-118[»]
2AW4X-ray3.46Q2-118[»]
2AWBX-ray3.46Q2-118[»]
2GYAelectron microscopy-O3-116[»]
2GYCelectron microscopy2.00O3-117[»]
2I2TX-ray3.22Q2-117[»]
2I2VX-ray3.22Q2-117[»]
2J28electron microscopy8.00Q2-117[»]
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[»]
2Z4LX-ray4.45Q2-118[»]
2Z4NX-ray4.45Q2-118[»]
3BBXelectron microscopy10.00Q2-118[»]
3DF2X-ray3.50Q2-117[»]
3DF4X-ray3.50Q2-117[»]
3FIKelectron microscopy-Q2-118[»]
ModBaseSearch...

Genome annotation databases

GeneID945152.
GenomeReviewsGene locus JW1706 in contig AP009048_GR.
Gene locus b1716 in contig U00096_GR.
KEGGecj:JW1706.
eco:b1716.

Organism-specific databases

EchoBASEEB0874.
EcoGeneEG10881. rplT.
CMRSearch...

Phylogenomic databases

HOGENOMP0A7L3.
OMAP0A7L3. FYGRRKN.

Enzyme and pathway databases

BioCycEcoCyc:EG10881-MON.

Family and domain databases

HAMAPMF_00382.
[Tree]
InterProIPR005813. Ribosomal_L20.
IPR005812. Ribosomal_L20_bac-type.
[Graphical view]
PANTHERPTHR10986. Ribosomal_L20. 1 hit.
PfamPF00453. Ribosomal_L20. 1 hit.
[Graphical view]
PRINTSPR00062. RIBOSOMALL20.
ProDomPD002389. Ribosomal_L20. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01032. rplT_bact. 1 hit.
PROSITEPS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents