50S ribosomal protein L17 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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Q9Z9H5 (RL17_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. 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 L17

Gene names

Name:	rplQ
Synonyms:	rpl17
Ordered Locus Names:	TTHA1663

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	118 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Part of the 50S ribosomal subunit. Contacts protein L32 By similarity.
Sequence similarities	Belongs to the ribosomal protein L17P family.
Mass spectrometry	Molecular mass is 13717 Da from positions 1 - 118. Determined by MALDI. Ref.4

Ontologies

Keywords
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	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 – 118

118

50S ribosomal protein L17 HAMAP-Rule MF_01368

PRO_0000175547

Experimental info

Sequence conflict

H → A AA sequence Ref.3

Sequence conflict

H → A AA sequence Ref.3

Secondary structure

118

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9Z9H5 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C9B8DD552F6C42AF
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FASTA

118

13,715

        10         20         30         40         50         60 
MRHLKSGRKL NRHSSHRLAL YRNQAKSLLT HGRITTTVPK AKELRGFVDH LIHLAKRGDL 

        70         80         90        100        110 
HARRLVLRDL QDVKLVRKLF DEIAPRYRDR QGGYTRVLKL AERRRGDGAP LALVELVE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the RNA polymerase alpha subunit gene from Thermus thermophilus HB8 and characterization of the protein." Wada T., Yamazaki T., Kuramitsu S., Kyogoku Y. J. Biochem. 125:143-150(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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.
[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 1-15.
[4]	"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.
[5]	"The crystal structure of the bacteria-specific L17 ribosomal protein from Thermus thermophilus." RIKEN structural genomics initiative (RSGI) Submitted (JAN-2003) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-118.
[6]	"Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon." Petry S., Brodersen D.E., Murphy F.V. IV, Dunham C.M., Selmer M., Tarry M.J., Kelley A.C., Ramakrishnan V. Cell 123:1255-1266(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.9 ANGSTROMS) OF 1-118 OF THE RIBOSOME ALONE OR IN COMPLEX WITH RELEASE FACTOR 1 OR RELEASE FACTOR 2.
[7]	"Translational operator of mRNA on the ribosome: how repressor proteins exclude ribosome binding." Jenner L., Romby P., Rees B., Schulze-Briese C., Springer M., Ehresmann C., Ehresmann B., Moras D., Yusupova G., Yusupov M. Science 308:120-123(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF 14-118.
[8]	"Structure of the 70S ribosome complexed with mRNA and tRNA." Selmer M., Dunham C.M., Murphy F.V. IV, Weixlbaumer A., Petry S., Kelley A.C., Weir J.R., Ramakrishnan V. Science 313:1935-1942(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-118 OF THE RIBOSOME.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB024328 Genomic DNA. Translation: BAA75550.1.
AP008226 Genomic DNA. Translation: BAD71486.1.

RefSeq

YP_144929.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GD8	X-ray	2.30	A/B/C/D/E/F/G/H/I	1-118	[»]
1YL3	X-ray	5.50	0	1-118	[»]
2B66	X-ray	5.90	R	1-118	[»]
2B9N	X-ray	6.76	R	1-118	[»]
2B9P	X-ray	6.46	R	1-118	[»]
2HGJ	X-ray	5.00	Q	1-118	[»]
2HGQ	X-ray	5.50	Q	1-118	[»]
2HGU	X-ray	4.51	Q	1-118	[»]
2J01	X-ray	2.80	R	1-118	[»]
2J03	X-ray	2.80	R	1-118	[»]
2V47	X-ray	3.80	R	1-118	[»]
2V49	X-ray	3.80	R	1-118	[»]
2WDI	X-ray	3.30	R	1-118	[»]
2WDJ	X-ray	3.30	R	1-118	[»]
2WDL	X-ray	3.50	R	1-118	[»]
2WDN	X-ray	3.50	R	1-118	[»]
2WH2	X-ray	3.45	R	1-118	[»]
2WH4	X-ray	3.45	R	1-118	[»]
2WRJ	X-ray	3.60	R	1-118	[»]
2WRL	X-ray	3.60	R	1-118	[»]
2WRO	X-ray	3.60	R	1-118	[»]
2WRR	X-ray	3.60	R	1-118	[»]
2X9S	X-ray	3.10	R	1-118	[»]
2X9U	X-ray	3.10	R	1-118	[»]
2XG0	X-ray	3.20	R	1-118	[»]
2XG2	X-ray	3.20	R	1-118	[»]
2XQE	X-ray	3.10	R	1-118	[»]
2XTG	electron microscopy	7.80	R	1-118	[»]
2XUX	electron microscopy	7.60	R	1-118	[»]
2Y0V	X-ray	3.10	R	1-118	[»]
2Y0X	X-ray	3.10	R	1-118	[»]
2Y0Z	X-ray	3.10	R	1-118	[»]
2Y11	X-ray	3.10	R	1-118	[»]
2Y13	X-ray	3.10	R	1-118	[»]
2Y15	X-ray	3.10	R	1-118	[»]
2Y17	X-ray	3.10	R	1-118	[»]
2Y19	X-ray	3.10	R	1-118	[»]
3FIN	electron microscopy	6.40	R	2-118	[»]
3HUX	X-ray	3.10	R	1-118	[»]
3HUZ	X-ray	3.10	R	1-118	[»]
3I8F	X-ray	3.10	0	1-118	[»]
3I8I	X-ray	3.10	0	1-118	[»]
3I9C	X-ray	3.50	0	1-118	[»]
3I9E	X-ray	3.50	0	1-118	[»]
3KIR	X-ray	3.30	R	1-118	[»]
3KIT	X-ray	3.30	R	1-118	[»]
3KIW	X-ray	3.60	R	1-118	[»]
3KIY	X-ray	3.60	R	1-118	[»]
3KNI	X-ray	3.00	R	1-118	[»]
3KNK	X-ray	3.00	R	1-118	[»]
3KNM	X-ray	3.45	R	1-118	[»]
3KNO	X-ray	3.45	R	1-118	[»]
3TVE	X-ray	3.10	0	1-118	[»]
3TVH	X-ray	3.10	0	2-118	[»]
3UXQ	X-ray	3.20	R	1-118	[»]
3UXR	X-ray	3.20	R	1-118	[»]
3UYE	X-ray	3.00	0	1-118	[»]
3UYG	X-ray	3.00	0	1-118	[»]
3UZ1	X-ray	3.30	0	1-118	[»]
3UZ2	X-ray	3.30	0	1-118	[»]
3UZ8	X-ray	3.00	0	1-118	[»]
3UZ9	X-ray	3.00	0	1-118	[»]
3UZF	X-ray	3.30	0	1-118	[»]
3UZH	X-ray	3.30	0	1-118	[»]
3UZK	X-ray	3.30	0	1-118	[»]
3UZN	X-ray	3.30	0	1-118	[»]
3V23	X-ray	3.00	R	1-118	[»]
3V25	X-ray	3.00	R	1-118	[»]
3V27	X-ray	3.10	R	1-118	[»]
3V29	X-ray	3.10	R	1-118	[»]
3V2D	X-ray	2.70	R	1-118	[»]
3V2F	X-ray	2.70	R	1-118	[»]
3ZVP	X-ray	3.80	R	1-118	[»]
4ABS	X-ray	3.10	R	1-118	[»]
4DHA	X-ray	3.20	R	1-118	[»]
4DHC	X-ray	3.20	R	1-118	[»]
4G5L	X-ray	3.30	0	1-118	[»]
4G5N	X-ray	3.30	0	1-118	[»]
4G5U	X-ray	3.10	0	1-118	[»]
4G5W	X-ray	3.10	0	1-118	[»]

ProteinModelPortal

Q9Z9H5.

SMR

Q9Z9H5. Positions 1-118.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1663.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71486; BAD71486; BAD71486.

GeneID

3168022.

KEGG

ttj:TTHA1663.

PATRIC

23958281. VBITheThe93045_1633.

Phylogenomic databases

eggNOG

COG0203.

HOGENOM

HOG000019780.

K02879.

OMA

LIMNERI.

ProtClustDB

PRK05591.

Family and domain databases

Gene3D

3.90.1030.10. 1 hit.

HAMAP

MF_01368. Ribosomal_L17.

InterPro

IPR000456. Ribosomal_L17.
[Graphical view]

PANTHER

PTHR14413. PTHR14413. 1 hit.

Pfam

PF01196. Ribosomal_L17. 1 hit.
[Graphical view]

SUPFAM

SSF64263. Ribosomal_L17. 1 hit.

TIGRFAMs

TIGR00059. L17. 1 hit.

PROSITE

PS01167. RIBOSOMAL_L17. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9Z9H5.

Entry information

Entry name

RL17_THET8

Accession

Primary (citable) accession number: Q9Z9H5
Secondary accession number(s): Q5SHR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 96 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

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