50S ribosomal protein L23 - Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

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Q5SHP0 (RL23_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. 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 L23

Gene names

Name:	rplW
Ordered Locus Names:	TTHA1690

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

General annotation (Comments)

Function	One of the early assembly proteins By similarity it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome By similarity.
Subunit structure	Contacts protein L29, and trigger factor when it is bound to the ribosome By similarity. Part of the 50S ribosomal subunit.
Sequence similarities	Belongs to the ribosomal protein L23P family.
Mass spectrometry	Molecular mass is 10737 Da from positions 1 - 96. Determined by MALDI. Ref.3

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	nucleotide binding Inferred from electronic annotation. Source: InterPro 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 – 96

50S ribosomal protein L23 HAMAP-Rule MF_01369

PRO_0000129427

Experimental info

Sequence conflict

Y → R AA sequence Ref.2

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q5SHP0 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 28ABA3C2D83A102A
Show »

FASTA

10,737

        10         20         30         40         50         60 
MKTAYDVILA PVLSEKAYAG FAEGKYTFWV HPKATKTEIK NAVETAFKVK VVKVNTLHVR 

        70         80         90 
GKKKRLGRYL GKRPDRKKAI VQVAPGQKIE ALEGLI

« 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 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 1-23.
[3]	"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.
[4]	"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.
[5]	"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: BAD71513.1.

RefSeq

YP_144956.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GIY	X-ray	5.50	T	1-96	[»]
1YL3	X-ray	5.50	T	1-96	[»]
2J01	X-ray	2.80	X	1-96	[»]
2J03	X-ray	2.80	X	1-96	[»]
2V47	X-ray	3.80	X	1-96	[»]
2V49	X-ray	3.80	X	1-96	[»]
2WDI	X-ray	3.30	X	1-96	[»]
2WDJ	X-ray	3.30	X	1-96	[»]
2WDL	X-ray	3.50	X	1-96	[»]
2WDN	X-ray	3.50	X	1-96	[»]
2WH2	X-ray	3.45	X	1-96	[»]
2WH4	X-ray	3.45	X	1-96	[»]
2WRJ	X-ray	3.60	X	1-96	[»]
2WRL	X-ray	3.60	X	1-96	[»]
2WRO	X-ray	3.60	X	1-96	[»]
2WRR	X-ray	3.60	X	1-96	[»]
2X9S	X-ray	3.10	X	1-96	[»]
2X9U	X-ray	3.10	X	1-96	[»]
2XG0	X-ray	3.20	X	1-96	[»]
2XG2	X-ray	3.20	X	1-96	[»]
2XQE	X-ray	3.10	X	1-96	[»]
2XTG	electron microscopy	7.80	X	1-96	[»]
2XUX	electron microscopy	7.60	X	1-96	[»]
2Y0V	X-ray	3.10	X	1-96	[»]
2Y0X	X-ray	3.10	X	1-96	[»]
2Y0Z	X-ray	3.10	X	1-96	[»]
2Y11	X-ray	3.10	X	1-96	[»]
2Y13	X-ray	3.10	X	1-96	[»]
2Y15	X-ray	3.10	X	1-96	[»]
2Y17	X-ray	3.10	X	1-96	[»]
2Y19	X-ray	3.10	X	1-96	[»]
3FIN	electron microscopy	6.40	X	3-95	[»]
3HUX	X-ray	3.10	X	1-96	[»]
3HUZ	X-ray	3.10	X	1-96	[»]
3I8F	X-ray	3.10	T	1-96	[»]
3I8I	X-ray	3.10	T	1-96	[»]
3I9C	X-ray	3.50	T	1-96	[»]
3I9E	X-ray	3.50	T	1-96	[»]
3KIR	X-ray	3.30	X	1-96	[»]
3KIT	X-ray	3.30	X	1-96	[»]
3KIW	X-ray	3.60	X	1-96	[»]
3KIY	X-ray	3.60	X	1-96	[»]
3KNI	X-ray	3.00	X	1-96	[»]
3KNK	X-ray	3.00	X	1-96	[»]
3KNM	X-ray	3.45	X	1-96	[»]
3KNO	X-ray	3.45	X	1-96	[»]
3TVE	X-ray	3.10	T	3-94	[»]
3TVH	X-ray	3.10	T	3-94	[»]
3UXQ	X-ray	3.20	X	1-96	[»]
3UXR	X-ray	3.20	X	1-96	[»]
3UYE	X-ray	3.00	T	1-96	[»]
3UYG	X-ray	3.00	T	1-96	[»]
3UZ1	X-ray	3.30	T	1-96	[»]
3UZ2	X-ray	3.30	T	1-96	[»]
3UZ8	X-ray	3.00	T	1-96	[»]
3UZ9	X-ray	3.00	T	1-96	[»]
3UZF	X-ray	3.30	T	1-96	[»]
3UZH	X-ray	3.30	T	1-96	[»]
3UZK	X-ray	3.30	T	1-96	[»]
3UZN	X-ray	3.30	T	1-96	[»]
3V23	X-ray	3.00	X	1-96	[»]
3V25	X-ray	3.00	X	1-96	[»]
3V27	X-ray	3.10	X	1-96	[»]
3V29	X-ray	3.10	X	1-96	[»]
3V2D	X-ray	2.70	X	1-96	[»]
3V2F	X-ray	2.70	X	1-96	[»]
3ZVP	X-ray	3.80	X	1-96	[»]
4ABS	X-ray	3.10	X	1-96	[»]
4DHA	X-ray	3.20	X	1-96	[»]
4DHC	X-ray	3.20	X	1-96	[»]
4G5L	X-ray	3.30	T	1-96	[»]
4G5N	X-ray	3.30	T	1-96	[»]
4G5U	X-ray	3.10	T	1-96	[»]
4G5W	X-ray	3.10	T	1-96	[»]

ProteinModelPortal

Q5SHP0.

SMR

Q5SHP0. Positions 1-96.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1690.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

BAD71513; BAD71513; BAD71513.

GeneID

3168722.

KEGG

ttj:TTHA1690.

PATRIC

23958335. VBITheThe93045_1660.

Phylogenomic databases

eggNOG

COG0089.

HOGENOM

HOG000231366.

K02892.

OMA

MIRRENN.

ProtClustDB

PRK05738.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

HAMAP

MF_01369_B. Ribosomal_L23_B.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR013025. Ribosomal_L25/23.
[Graphical view]

Pfam

PF00276. Ribosomal_L23. 1 hit.
[Graphical view]

SUPFAM

SSF54189. L23_L15e_core. 1 hit.

PROSITE

PS00050. RIBOSOMAL_L23. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q5SHP0.

Entry information

Entry name

RL23_THET8

Accession

Primary (citable) accession number: Q5SHP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	December 21, 2004
Last modified:	May 1, 2013
This is version 71 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