50S ribosomal protein L18 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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Q5SHQ4 (RL18_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 72. 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 L18

Alternative name(s):
TL24

Gene names

Name:	rplR
Ordered Locus Names:	TTHA1676

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	112 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	This is one of the proteins that binds and mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. HAMAP-Rule MF_01337_B
Subunit structure	Part of the 50S ribosomal subunit; part of the 5S rRNA/L5/L18/L25 subcomplex. Contacts the 5S and probably the 23S rRNA; has been isolated in a complex with the 5S rRNA and RL25 (Ref.2).
Sequence similarities	Belongs to the ribosomal protein L18P family.
Mass spectrometry	Molecular mass is 12481 Da from positions 2 - 112. Determined by MALDI. Ref.5

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

Initiator methionine

Removed Ref.2 Ref.3 Ref.4

Chain

2 – 112

111

50S ribosomal protein L18 HAMAP-Rule MF_01337_B

PRO_0000131372

Secondary structure

112

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q5SHQ4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EA2AB016AEDB0638
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FASTA

112

12,612

        10         20         30         40         50         60 
MARLTAYERR KFRVRNRIKR TGRLRLSVFR SLKHIYAQII DDEKGVTLVS ASSLALKLKG 

        70         80         90        100        110 
NKTEVARQVG RALAEKALAL GIKQVAFDRG PYKYHGRVKA LAEGAREGGL EF

« 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, purification and partial sequence of four Thermus thermophilus 5S rRNA binding proteins." Kim J.-S., Boysen R.I., Schroeder W., Erdmann V.A., Gessner R.V. Endocyt. Cell Res. 11:177-194(1996) Cited for: PROTEIN SEQUENCE OF 2-24, ISOLATION OF 5S RRNA-ASSOCIATED COMPLEXES.
[3]	"The isolation and complete amino acid sequence of the ribosomal protein L36 from Thermus thermophilus and its zinc-binding motif." Boysen R.I., Lorenz S., Kim J.S., Schroeder W.F.K.J., Erdmann V.A. Endocyt. Cell Res. 11:41-58(1995) Cited for: PROTEIN SEQUENCE OF 2-19.
[4]	"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 2-16.
[5]	"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.
[6]	"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.
[7]	"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: BAD71499.1.

RefSeq

YP_144942.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GIY	X-ray	5.50	Q	1-112	[»]
1YL3	X-ray	5.50	Q	1-112	[»]
2HGJ	X-ray	5.00	R	1-112	[»]
2HGQ	X-ray	5.50	R	1-112	[»]
2HGU	X-ray	4.51	R	1-112	[»]
2J01	X-ray	2.80	S	2-111	[»]
2J03	X-ray	2.80	S	2-111	[»]
2V47	X-ray	3.80	S	2-111	[»]
2V49	X-ray	3.80	S	2-111	[»]
2WDI	X-ray	3.30	S	1-112	[»]
2WDJ	X-ray	3.30	S	1-112	[»]
2WDL	X-ray	3.50	S	1-112	[»]
2WDN	X-ray	3.50	S	1-112	[»]
2WH2	X-ray	3.45	S	1-112	[»]
2WH4	X-ray	3.45	S	1-112	[»]
2WRJ	X-ray	3.60	S	1-112	[»]
2WRL	X-ray	3.60	S	1-112	[»]
2WRO	X-ray	3.60	S	1-112	[»]
2WRR	X-ray	3.60	S	1-112	[»]
2X9S	X-ray	3.10	S	1-112	[»]
2X9U	X-ray	3.10	S	1-112	[»]
2XG0	X-ray	3.20	S	1-112	[»]
2XG2	X-ray	3.20	S	1-112	[»]
2XQE	X-ray	3.10	S	1-112	[»]
2XTG	electron microscopy	7.80	S	1-112	[»]
2XUX	electron microscopy	7.60	S	1-112	[»]
2Y0V	X-ray	3.10	S	1-112	[»]
2Y0X	X-ray	3.10	S	1-112	[»]
2Y0Z	X-ray	3.10	S	1-112	[»]
2Y11	X-ray	3.10	S	1-112	[»]
2Y13	X-ray	3.10	S	1-112	[»]
2Y15	X-ray	3.10	S	1-112	[»]
2Y17	X-ray	3.10	S	1-112	[»]
2Y19	X-ray	3.10	S	1-112	[»]
3FIN	electron microscopy	6.40	S	11-109	[»]
3HUX	X-ray	3.10	S	1-112	[»]
3HUZ	X-ray	3.10	S	1-112	[»]
3I8F	X-ray	3.10	Q	1-112	[»]
3I8I	X-ray	3.10	Q	1-112	[»]
3I9C	X-ray	3.50	Q	1-112	[»]
3I9E	X-ray	3.50	Q	1-112	[»]
3KIR	X-ray	3.30	S	1-112	[»]
3KIT	X-ray	3.30	S	1-112	[»]
3KIW	X-ray	3.60	S	1-112	[»]
3KIY	X-ray	3.60	S	1-112	[»]
3KNI	X-ray	3.00	S	1-112	[»]
3KNK	X-ray	3.00	S	1-112	[»]
3KNM	X-ray	3.45	S	1-112	[»]
3KNO	X-ray	3.45	S	1-112	[»]
3TVE	X-ray	3.10	Q	2-112	[»]
3TVH	X-ray	3.10	Q	2-112	[»]
3UXQ	X-ray	3.20	S	1-112	[»]
3UXR	X-ray	3.20	S	1-112	[»]
3UYE	X-ray	3.00	Q	1-112	[»]
3UYG	X-ray	3.00	Q	1-112	[»]
3UZ1	X-ray	3.30	Q	1-112	[»]
3UZ2	X-ray	3.30	Q	1-112	[»]
3UZ8	X-ray	3.00	Q	1-112	[»]
3UZ9	X-ray	3.00	Q	1-112	[»]
3UZF	X-ray	3.30	Q	1-112	[»]
3UZH	X-ray	3.30	Q	1-112	[»]
3UZK	X-ray	3.30	Q	1-112	[»]
3UZN	X-ray	3.30	Q	1-112	[»]
3V23	X-ray	3.00	S	1-112	[»]
3V25	X-ray	3.00	S	1-112	[»]
3V27	X-ray	3.10	S	1-112	[»]
3V29	X-ray	3.10	S	1-112	[»]
3V2D	X-ray	2.70	S	1-112	[»]
3V2F	X-ray	2.70	S	1-112	[»]
3ZN9	X-ray	3.10	S	1-112	[»]
3ZNE	X-ray	3.10	S	1-112	[»]
3ZVP	X-ray	3.80	S	1-112	[»]
4ABS	X-ray	3.10	S	1-112	[»]
4B8G	X-ray	3.70	S	1-112	[»]
4B8I	X-ray	3.70	S	1-112	[»]
4DHA	X-ray	3.20	S	1-112	[»]
4DHC	X-ray	3.20	S	1-112	[»]
4G5L	X-ray	3.30	Q	1-112	[»]
4G5N	X-ray	3.30	Q	1-112	[»]
4G5U	X-ray	3.10	Q	1-112	[»]
4G5W	X-ray	3.10	Q	1-112	[»]

ProteinModelPortal

Q5SHQ4.

SMR

Q5SHQ4. Positions 3-112.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1676.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71499; BAD71499; BAD71499.

GeneID

3169978.

KEGG

ttj:TTHA1676.

PATRIC

23958307. VBITheThe93045_1646.

Phylogenomic databases

eggNOG

COG0256.

HOGENOM

HOG000248742.

K02881.

OMA

KSTRSHI.

ProtClustDB

PRK05593.

Enzyme and pathway databases

BioCyc

TTHE300852:GH8R-1715-MONOMER.

Family and domain databases

HAMAP

MF_01337_B. Ribosomal_L18_B.

InterPro

IPR005484. Ribosomal_L18/L5.
IPR004389. Ribosomal_L18_bac-type.
[Graphical view]

Pfam

PF00861. Ribosomal_L18p. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00060. L18_bact. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SHQ4.

Entry information

Entry name

RL18_THET8

Accession

Primary (citable) accession number: Q5SHQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 72 of the entry and version 3 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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents