50S ribosomal protein L20 - Escherichia coli (strain K12)

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P0A7L3 (RL20_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
50S ribosomal protein L20

Gene names

Name:	rplT
Synonyms:	pdzA
Ordered Locus Names:	b1716, JW1706

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	118 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ribosomal large subunit assembly Inferred from direct assay PubMed 7021848. Source: EcoCyc translation Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosolic large ribosomal subunit Inferred from mutant phenotype PubMed 8628231. Source: EcoCyc
Molecular_function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from direct assay PubMed 7021848. Source: EcoCyc translation repressor activity, nucleic acid binding Inferred from direct assay PubMed 1453449. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 118

117

50S ribosomal protein L20 HAMAP-Rule MF_00382

PRO_0000177156

Experimental info

Sequence conflict

R → A in CAA23562. Ref.1

Sequence conflict

R → A in AAA51468. Ref.1

Secondary structure

118

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7L3 [UniParc].

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

118

13,497

        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' referencesShow '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. 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 277:1453-1474(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.

PIR

R5EC20. D64930.

RefSeq

NP_416231.1. NC_000913.2.
YP_489978.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	3-116	[»]
2GYC	electron microscopy	15.00	O	3-117	[»]
2I2T	X-ray	3.22	Q	2-117	[»]
2I2V	X-ray	3.22	Q	2-117	[»]
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	2-117	[»]
3J0W	electron microscopy	14.70	S	2-117	[»]
3J0Y	electron microscopy	13.50	S	2-117	[»]
3J11	electron microscopy	13.10	S	2-117	[»]
3J12	electron microscopy	11.50	S	2-117	[»]
3J14	electron microscopy	11.50	S	2-117	[»]
3J19	electron microscopy	8.30	Q	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	[»]
4GAR	X-ray	3.30	Q	1-118	[»]
4GAU	X-ray	3.30	Q	1-118	[»]

ProteinModelPortal

P0A7L3.

SMR

P0A7L3. Positions 2-118.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47941N.

IntAct

P0A7L3. 35 interactions.

MINT

MINT-1321645.

STRING

511145.b1716.

Proteomic databases

PaxDb

P0A7L3.

PRIDE

P0A7L3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74786; AAC74786; b1716.
BAA15483; BAA15483; BAA15483.

GeneID

12931309.
945152.

KEGG

ecj:Y75_p1691.
eco:b1716.

PATRIC

32118736. VBIEscCol129921_1786.

Organism-specific databases

EchoBASE

EB0874.

EcoGene

EG10881. rplT.

Phylogenomic databases

eggNOG

COG0292.

HOGENOM

HOG000035046.

K02887.

OMA

GRRKNVW.

ProtClustDB

PRK05185.

Enzyme and pathway databases

BioCyc

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

Gene expression databases

Genevestigator

P0A7L3.

Family and domain databases

HAMAP

MF_00382. Ribosomal_L20.

InterPro

IPR005813. Ribosomal_L20.
[Graphical view]

PANTHER

PTHR10986. PTHR10986. 1 hit.

Pfam

PF00453. Ribosomal_L20. 1 hit.
[Graphical view]

PRINTS

PR00062. RIBOSOMALL20.

TIGRFAMs

TIGR01032. rplT_bact. 1 hit.

PROSITE

PS00937. RIBOSOMAL_L20. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7L3.

Entry information

Entry name

RL20_ECOLI

Accession

Primary (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:	May 29, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents