Reviewed, UniProtKB/Swiss-Prot Q5SLP6 (RL11_THET8)

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) [Complete proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 MF_00736 This protein binds directly to 23S ribosomal RNA. HAMAP MF_00736 In the 70S ribosome is in a position where it could interact transiently with the A site tRNA during translation. HAMAP MF_00736
Subunit structure	Part of the 50S ribosomal subunit. Contacts one of the L7 dimers. HAMAP MF_00736
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
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 MF_00736

PRO_0000104399

Amino acid modifications

Modified residue

3

1

N6,N6,N6-trimethyllysine Ref.4

Experimental info

Sequence conflict

20

1

A → G AA sequence Ref.3

Sequence conflict

23

1

V → G Ref.2

Secondary structure

1

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147

Helix Strand Turn

Details...

Beta strand

4 – 13

10

Helix

23 – 28

6

Turn

29 – 31

3

Helix

34 – 45

12

Helix

46 – 48

3

Beta strand

52 – 60

9

Beta strand

65 – 69

5

Helix

74 – 78

5

Helix

104 – 110

7

Beta strand

113 – 115

3

Beta strand

118 – 120

3

Helix

121 – 128

8

Turn

129 – 132

4

Beta strand

133 – 135

3

Sequences

	Sequence		Length	Mass (Da)
	Q5SLP6-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 3D8DECEBE85B5FE9	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

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].
[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: 1447157] [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: 11154066] [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: 10333296] [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: 15317787] [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: 16287167] [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: 11511350] [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: 11283358] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF THE RIBOSOME.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

RefSeq

YP_143513.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GIY	X-ray	5.50	L	-	[»]
1YL3	X-ray	5.50	L	2-139	[»]
2HGJ	X-ray	5.00	L	-	[»]
2HGQ	X-ray	5.50	L	1-147	[»]
2HGU	X-ray	4.51	L	-	[»]
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	[»]
3FIN	electron microscopy	6.40	L	2-139	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q5SLP6.

Genome annotation databases

GeneID

3168343.

GenomeReviews

Gene locus TTHA0247 in contig AP008226_GR.

KEGG

ttj:TTHA0247.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q5SLP6.

OMA

TQSEAGM.

Enzyme and pathway databases

BioCyc

TTHE300852:TTHA0247-MON.

Family and domain databases

HAMAP

MF_00736.
[Tree]

InterPro

IPR000911. Ribosomal_L11.
IPR006519. Ribosomal_L11_bac-type.
[Graphical view]

Gene3D

G3DSA:1.10.10.250. Ribosomal_L11. 1 hit.

PANTHER

PTHR11661:SF1. Ribosom_L11_bac. 1 hit.
PTHR11661. Ribosomal_L11. 1 hit.

Pfam

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

ProDom

PD001367. Ribosomal_L11. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00649. RL11. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01632. L11_bact. 1 hit.

PROSITE

PS00359. RIBOSOMAL_L11. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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