50S ribosomal protein L21 - Escherichia coli (strain K12)

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P0AG48 (RL21_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 75. 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 L21

Gene names

Name:	rplU
Ordered Locus Names:	b3186, JW3153

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	103 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protein binds to 23S rRNA in the presence of protein L20. HAMAP-Rule MF_01363
Subunit structure	Part of the 50S ribosomal subunit. Contacts protein L20.
Sequence similarities	Belongs to the ribosomal protein L21P family.
Mass spectrometry	Molecular mass is 11562.7 Da from positions 1 - 103. Determined by MALDI. Ref.9

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	translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	rRNA binding Inferred from electronic annotation. Source: HAMAP structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 103

103

50S ribosomal protein L21 HAMAP-Rule MF_01363

PRO_0000181000

Secondary structure

103

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AG48 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 9221F104EC9C8CDB
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FASTA

103

11,564

        10         20         30         40         50         60 
MYAVFQSGGK QHRVSEGQTV RLEKLDIATG ETVEFAEVLM IANGEEVKIG VPFVDGGVIK 

        70         80         90        100 
AEVVAHGRGE KVKIVKFRRR KHYRKQQGHR QWFTDVKITG ISA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Amino acid sequence of the ribosomal protein L21 of Escherichia coli." Heiland I., Wittmann-Liebold B. Biochemistry 18:4605-4612(1979) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli." Jeong J.H., Kitakawa M.S., Isono S., Isono K. DNA Seq. 4:59-67(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"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.
[5]	Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F. Submitted (SEP-1994) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-13. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29." Wower I., Wower J., Meinke M., Brimacombe R. Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO 23S RRNA. Strain: MRE-600.
[7]	"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 L20.
[8]	"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.
[9]	"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.
[10]	"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

D13267 Genomic DNA. Translation: BAA02525.1.
U18997 Genomic DNA. Translation: AAA57987.1.
U00096 Genomic DNA. Translation: AAC76218.1.
AP009048 Genomic DNA. Translation: BAE77230.1.

PIR

R5EC21. JS0766.

RefSeq

NP_417653.1. NC_000913.2.
YP_491371.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VS6	X-ray	3.46	R	1-103	[»]
1VS8	X-ray	3.46	R	1-103	[»]
1VT2	X-ray	3.30	R	1-103	[»]
2AW4	X-ray	3.46	R	1-103	[»]
2AWB	X-ray	3.46	R	1-103	[»]
2I2T	X-ray	3.22	R	1-103	[»]
2I2V	X-ray	3.22	R	1-103	[»]
2J28	electron microscopy	8.00	R	1-103	[»]
2QAM	X-ray	3.21	R	1-103	[»]
2QAO	X-ray	3.21	R	1-103	[»]
2QBA	X-ray	3.54	R	1-103	[»]
2QBC	X-ray	3.54	R	1-103	[»]
2QBE	X-ray	3.30	R	1-103	[»]
2QBG	X-ray	3.30	R	1-103	[»]
2QBI	X-ray	4.00	R	1-103	[»]
2QBK	X-ray	4.00	R	1-103	[»]
2QOV	X-ray	3.93	R	1-103	[»]
2QOX	X-ray	3.93	R	1-103	[»]
2QOZ	X-ray	3.50	R	1-103	[»]
2QP1	X-ray	3.50	R	1-103	[»]
2RDO	electron microscopy	9.10	R	1-103	[»]
2WWQ	electron microscopy	5.80	R	1-103	[»]
2Z4L	X-ray	4.45	R	1-103	[»]
2Z4N	X-ray	4.45	R	1-103	[»]
3BBX	electron microscopy	10.00	R	1-103	[»]
3E1B	electron microscopy	-	K	1-103	[»]
3E1D	electron microscopy	-	K	1-103	[»]
3FIK	electron microscopy	6.70	R	1-103	[»]
3I1N	X-ray	3.19	R	1-103	[»]
3I1P	X-ray	3.19	R	1-103	[»]
3I1R	X-ray	3.81	R	1-103	[»]
3I1T	X-ray	3.81	R	1-103	[»]
3I20	X-ray	3.71	R	1-103	[»]
3I22	X-ray	3.71	R	1-103	[»]
3IZT	electron microscopy	-	S	1-103	[»]
3IZU	electron microscopy	-	S	1-103	[»]
3J01	electron microscopy	-	R	1-103	[»]
3J0T	electron microscopy	12.10	T	1-103	[»]
3J0W	electron microscopy	14.70	T	1-103	[»]
3J0Y	electron microscopy	13.50	T	1-103	[»]
3J11	electron microscopy	13.10	T	1-103	[»]
3J12	electron microscopy	11.50	T	1-103	[»]
3J14	electron microscopy	11.50	T	1-103	[»]
3J19	electron microscopy	8.30	R	1-103	[»]
3J37	electron microscopy	9.80	V	1-103	[»]
3KCR	electron microscopy	-	R	1-103	[»]
3OAS	X-ray	3.25	R	1-103	[»]
3OAT	X-ray	3.25	R	1-103	[»]
3OFC	X-ray	3.19	R	1-103	[»]
3OFD	X-ray	3.19	R	1-103	[»]
3OFQ	X-ray	3.10	R	1-103	[»]
3OFR	X-ray	3.10	R	1-103	[»]
3OFZ	X-ray	3.29	R	1-103	[»]
3OG0	X-ray	3.29	R	1-103	[»]
3ORB	X-ray	3.30	R	1-103	[»]
3R8S	X-ray	3.00	R	1-103	[»]
3R8T	X-ray	3.00	R	1-103	[»]
3SGF	X-ray	3.20	V	1-103	[»]
3UOS	X-ray	3.70	V	1-103	[»]
4GAR	X-ray	3.30	R	1-103	[»]
4GAU	X-ray	3.30	R	1-103	[»]

ProteinModelPortal

P0AG48.

SMR

P0AG48. Positions 1-103.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47852N.

IntAct

P0AG48. 80 interactions.

MINT

MINT-1280768.

STRING

511145.b3186.

2D gel databases

SWISS-2DPAGE

P0AG48.

Proteomic databases

PaxDb

P0AG48.

PRIDE

P0AG48.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76218; AAC76218; b3186.
BAE77230; BAE77230; BAE77230.

GeneID

12932080.
949057.

KEGG

ecj:Y75_p3106.
eco:b3186.

PATRIC

32121792. VBIEscCol129921_3280.

Organism-specific databases

EchoBASE

EB4295.

EcoGene

EG50001. rplU.

Phylogenomic databases

eggNOG

COG0261.

HOGENOM

HOG000036265.

K02888.

OMA

KVTIIKF.

ProtClustDB

PRK05573.

Enzyme and pathway databases

BioCyc

EcoCyc:EG50001-MONOMER.
ECOL316407:JW3153-MONOMER.

Gene expression databases

Genevestigator

P0AG48.

Family and domain databases

HAMAP

MF_01363. Ribosomal_L21.

InterPro

IPR001787. Ribosomal_L21.
IPR018258. Ribosomal_L21_CS.
[Graphical view]

PANTHER

PTHR21349. PTHR21349. 1 hit.

Pfam

PF00829. Ribosomal_L21p. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00061. L21. 1 hit.

PROSITE

PS01169. RIBOSOMAL_L21. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AG48.

Entry information

Entry name

RL21_ECOLI

Accession

Primary (citable) accession number: P0AG48
Secondary accession number(s): P02422, Q2M926

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel 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