50S ribosomal protein L11 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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Q5SLP6 (RL11_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 73. History...

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

Documents (3) |

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 L11

Gene names

Name:	rplK
Ordered Locus Names:	TTHA0247

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of the L7 dimers in conjuction with L11 and its bound segment of 23S rRNA forms what is known as the L7/L12 stalk, which extends beyond the surface of the 70S ribosome. The stalk is preferentially stabilized in 70S versus 50S crystals. HAMAP-Rule MF_00736_B This protein binds directly to 23S ribosomal RNA. HAMAP-Rule MF_00736_B In the 70S ribosome is in a position where it could interact transiently with the A site tRNA during translation. HAMAP-Rule MF_00736_B
Subunit structure	Part of the 50S ribosomal subunit. Contacts one of the L7 dimers.
Post-translational modification	The protein probably contains twelve methyl groups; at least one lysine residue (Lys-3) is known to be trimethylated. Methylation of the protein is not required for function. Ref.4 Ref.5
Sequence similarities	Belongs to the ribosomal protein L11P family.
Mass spectrometry	Molecular mass is 15506.2 Da from positions 1 - 147. Determined by MALDI. Weight of the unmethylated protein. Ref.5 Molecular mass is 15675.1 Da from positions 1 - 147. Determined by MALDI. Weight of the methylated protein. Ref.5 Molecular mass is 15678 Da from positions 1 - 147. Determined by MALDI. Ref.6

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Methylation
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 – 147

147

50S ribosomal protein L11 HAMAP-Rule MF_00736_B

PRO_0000104399

Amino acid modifications

Modified residue

N6,N6,N6-trimethyllysine Ref.4

Experimental info

Sequence conflict

A → G AA sequence Ref.3

Sequence conflict

V → G Ref.2

Secondary structure

147

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q5SLP6 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 3D8DECEBE85B5FE9
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FASTA

147

15,505

        10         20         30         40         50         60 
MKKVVAVVKL QLPAGKATPA PPVGPALGQH GANIMEFVKA FNAATANMGD AIVPVEITIY 

        70         80         90        100        110        120 
ADRSFTFVTK TPPASYLIRK AAGLEKGAHK PGREKVGRIT WEQVLEIAKQ KMPDLNTTDL 

       130        140 
EAAARMIAGS ARSMGVEVVG APEVKDA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[2]	"Identification of the gene encoding transcription factor NusG of Thermus thermophilus." Heinrich T., Schroeder W., Erdmann V.A., Hartmann R.K. J. Bacteriol. 174:7859-7863(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
[3]	"Identification of the 50S ribosomal proteins from the eubacterium Thermus thermophilus." Katsani K.R., Tsiboli P., Anagnostopoulos K., Urlaub H., Choli-Papadopoulou T. Biol. Chem. 381:1079-1087(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-32 AND 71-85, BLOCKAGE OF N-TERMINUS.
[4]	"Structural and functional studies on the overproduced L11 protein from Thermus thermophilus." Triantafillidou D., Simitsopoulou M., Franceschi F., Choli-Papadopoulou T. J. Protein Chem. 18:215-223(1999) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-3.
[5]	"Thermus thermophilus L11 methyltransferase, PrmA, is dispensable for growth and preferentially modifies free ribosomal protein L11 prior to ribosome assembly." Cameron D.M., Gregory S.T., Thompson J., Suh M.-J., Limbach P.A., Dahlberg A.E. J. Bacteriol. 186:5819-5825(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, METHYLATION.
[6]	"Extending ribosomal protein identifications to unsequenced bacterial strains using matrix-assisted laser desorption/ionization mass spectrometry." Suh M.-J., Hamburg D.M., Gregory S.T., Dahlberg A.E., Limbach P.A. Proteomics 5:4818-4831(2005) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY.
[7]	"The path of messenger RNA through the ribosome." Yusupova G.Z., Yusupov M.M., Cate J.H.D., Noller H.F. Cell 106:233-241(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF THE RIBOSOME.
[8]	"Crystal structure of the ribosome at 5.5 A resolution." Yusupov M.M., Yusupova G.Z., Baucom A., Lieberman K., Earnest T.N., Cate J.H.D., Noller H.F. Science 292:883-896(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP008226 Genomic DNA. Translation: BAD70070.1.
L10348 Genomic DNA. No translation available.

RefSeq

YP_143513.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GIY	X-ray	5.50	L	1-147	[»]
1YL3	X-ray	5.50	L	2-139	[»]
2HGJ	X-ray	5.00	L	1-147	[»]
2HGQ	X-ray	5.50	L	1-147	[»]
2HGU	X-ray	4.51	L	1-147	[»]
2J01	X-ray	2.80	K	1-147	[»]
2J03	X-ray	2.80	K	1-147	[»]
2WH2	X-ray	3.45	K	1-147	[»]
2WH4	X-ray	3.45	K	1-147	[»]
2WRJ	X-ray	3.60	K	1-147	[»]
2WRL	X-ray	3.60	K	1-147	[»]
2X9S	X-ray	3.10	K	1-147	[»]
2X9U	X-ray	3.10	K	1-147	[»]
2XTG	electron microscopy	7.80	K	1-147	[»]
2XUX	electron microscopy	7.60	K	1-147	[»]
3EGV	X-ray	1.75	B	2-147	[»]
3FIN	electron microscopy	6.40	L	2-139	[»]
3I8I	X-ray	3.10	L	1-147	[»]

ProteinModelPortal

Q5SLP6.

SMR

Q5SLP6. Positions 1-147.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-4299414.

STRING

300852.TTHA0247.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD70070; BAD70070; BAD70070.

GeneID

3168343.

KEGG

ttj:TTHA0247.

PATRIC

23955441. VBITheThe93045_0247.

Phylogenomic databases

eggNOG

COG0080.

HOGENOM

HOG000082123.

K02867.

OMA

KQFNAKT.

ProtClustDB

PRK00140.

Family and domain databases

Gene3D

1.10.10.250. 1 hit.
3.30.1550.10. 1 hit.

HAMAP

MF_00736_B. Ribosomal_L11_B.

InterPro

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

PANTHER

PTHR11661. PTHR11661. 1 hit.

Pfam

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

SMART

SM00649. RL11. 1 hit.
[Graphical view]

SUPFAM

SSF46906. Ribosomal_L11. 1 hit.
SSF54747. Ribosomal_L11. 1 hit.

TIGRFAMs

TIGR01632. L11_bact. 1 hit.

PROSITE

PS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SLP6.

Entry information

Entry name

RL11_THET8

Accession

Primary (citable) accession number: Q5SLP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 73 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

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

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents