50S ribosomal protein L11 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A7J7 (RL11_ECOLI)

Last modified February 9, 2010. Version 55. History...

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

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Names and origin

Protein names

Recommended name:
50S ribosomal protein L11

Gene names

Name:	rplK
Synonyms:	relC
Ordered Locus Names:	b3983, JW3946

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors. HAMAP MF_00736
Subunit structure	Part of the 50S ribosomal subunit. HAMAP MF_00736
Sequence similarities	Belongs to the ribosomal protein L11P family.
Mass spectrometry	Molecular mass is 14870.2 Da from positions 2 - 142. Determined by MALDI. Ref.8

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Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Methylation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	stringent response Inferred from direct assay. Source: UniProtKB translational termination Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytosolic large ribosomal subunit Ref.5 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct rRNA binding Inferred from direct assay. Source: UniProtKB structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
prmA	P0A8T1	1	EBI-547288,EBI-556300

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 142

141

50S ribosomal protein L11 HAMAP MF_00736

PRO_0000104283

Amino acid modifications

Modified residue

N,N,N-trimethylalanine HAMAP MF_00736

Modified residue

N6,N6,N6-trimethyllysine HAMAP MF_00736

Modified residue

N6,N6,N6-trimethyllysine HAMAP MF_00736

Secondary structure

142

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A7J7-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C49226BB2462BE0F
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FASTA

142

14,875

        10         20         30         40         50         60 
MAKKVQAYVK LQVAAGMANP SPPVGPALGQ QGVNIMEFCK AFNAKTDSIE KGLPIPVVIT 

        70         80         90        100        110        120 
VYADRSFTFV TKTPPAAVLL KKAAGIKSGS GKPNKDKVGK ISRAQLQEIA QTKAADMTGA 

       130        140 
DIEAMTRSIE GTARSMGLVV ED

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli." Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P. Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed: 377281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes." Dognin M.J., Wittmann-Liebold B. Eur. J. Biochem. 112:131-151(1980) [PubMed: 7004866] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-142. Strain: K12.
[6]	"Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon." Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P. J. Bacteriol. 172:1621-1627(1990) [PubMed: 2137819] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
[7]	"Structural properties of ribosomal protein L11 from Escherichia coli." Choli T. Biochem. Int. 19:1323-1338(1989) [PubMed: 2483975] [Abstract] Cited for: STRUCTURAL STUDIES.
[8]	"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.
[9]	"The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution." Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R. J. Mol. Biol. 298:35-59(2000) [PubMed: 10756104] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[10]	"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.
[11]	"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.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00339 Genomic DNA. Translation: CAA23621.1. Sequence problems.
M30610 Genomic DNA. Translation: AAA24623.1.
U00006 Genomic DNA. Translation: AAC43081.1.
U00096 Genomic DNA. Translation: AAC76957.1.
AP009048 Genomic DNA. Translation: BAE77337.1.

PIR

R5EC11. S12572.

RefSeq

AP_003836.1.
NP_418410.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	G	2-142	[»]
1P86	electron microscopy	11.50	G	2-142	[»]
1VS6	X-ray	3.46	I	1-142	[»]
1VS8	X-ray	3.46	I	1-142	[»]
2AW4	X-ray	3.46	I	2-142	[»]
2AWB	X-ray	3.46	I	2-142	[»]
2GYA	electron microscopy	15.00	G	3-140	[»]
2GYC	electron microscopy	15.00	G	3-141	[»]
2I2T	X-ray	3.22	I	2-141	[»]
2I2V	X-ray	3.22	I	2-141	[»]
2J28	electron microscopy	8.00	I	2-141	[»]
2QAM	X-ray	3.21	I	2-142	[»]
2QAO	X-ray	3.21	I	2-142	[»]
2QBA	X-ray	3.54	I	2-142	[»]
2QBC	X-ray	3.54	I	2-142	[»]
2QBE	X-ray	3.30	I	2-142	[»]
2QBG	X-ray	3.30	I	2-142	[»]
2QBI	X-ray	4.00	I	2-142	[»]
2QBK	X-ray	4.00	I	2-142	[»]
2QOV	X-ray	3.93	I	2-142	[»]
2QOX	X-ray	3.93	I	2-142	[»]
2QOZ	X-ray	3.50	I	2-142	[»]
2QP1	X-ray	3.50	I	2-142	[»]
2RDO	electron microscopy	9.10	I	2-142	[»]
2VHM	X-ray	3.74	I	2-142	[»]
2VHN	X-ray	3.74	I	2-142	[»]
2Z4L	X-ray	4.45	I	2-142	[»]
2Z4N	X-ray	4.45	I	2-142	[»]
3DEG	electron microscopy	-	H	2-142	[»]
3DF2	X-ray	3.50	I	2-141	[»]
3DF4	X-ray	3.50	I	2-141	[»]
3E1B	electron microscopy	-	5	1-142	[»]
3E1D	electron microscopy	-	5	1-142	[»]
3EP2	electron microscopy	-	I	2-142	[»]
3EQ3	electron microscopy	-	I	2-142	[»]
3EQ4	electron microscopy	-	I	2-142	[»]
3FIK	electron microscopy	6.70	I	2-142	[»]
3I1N	X-ray	3.19	I	1-142	[»]
3I1P	X-ray	3.19	I	1-142	[»]
3I1R	X-ray	3.81	I	1-142	[»]
3I1T	X-ray	3.81	I	1-142	[»]
3I20	X-ray	3.71	I	1-142	[»]
3I22	X-ray	3.71	I	1-142	[»]
487D	electron microscopy	7.50	L	10-86	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7J7. 44 interactions.

STRING

P0A7J7.

2-D gel databases

ECO2DBASE

I014.1. 6TH EDITION.

Proteomic databases

PRIDE

P0A7J7.

Genome annotation databases

GeneID

948484.

GenomeReviews

Gene locus JW3946 in contig AP009048_GR.
Gene locus b3983 in contig U00096_GR.

KEGG

ecj:JW3946.
eco:b3983.

Organism-specific databases

EchoBASE

EB0865.

EcoGene

EG10872. rplK.

CMR

Search...

Phylogenomic databases

eggNOG

COG0080.

HOGENOM

HBG594170.

OMA

DRSFDFK.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10872-MONOMER.
ECOL168927:B3983-MONOMER.

Gene expression databases

Genevestigator

P0A7J7.

Family and domain databases

HAMAP

MF_00736_B. Ribosomal_L11_B.
[Tree]

InterPro

IPR000911. Ribosomal_L11.
IPR006519. Ribosomal_L11_bac-type.
IPR020783. Ribosomal_L11_C.
IPR020785. Ribosomal_L11_CS.
IPR020784. Ribosomal_L11_N.
[Graphical view]

Gene3D

G3DSA:1.10.10.250. Ribosomal_L11. 1 hit.
G3DSA:3.30.1550.10. Ribosomal_L11_N. 1 hit.

PANTHER

PTHR11661. Ribosomal_L11. 1 hit.

Pfam

PF00298. Ribosomal_L11. 1 hit.
PF03946. Ribosomal_L11_N. 1 hit.
[Graphical view]

SMART

SM00649. RL11. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01632. L11_bact. 1 hit.

PROSITE

PS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

RL11_ECOLI

Accession

Primary (citable) accession number: P0A7J7
Secondary accession number(s): P02409, P76778, Q2M8R9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents