50S ribosomal protein L15 - Deinococcus radiodurans

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Q9RSK9 (RL15_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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 L15

Gene names

Name:	rplO
Ordered Locus Names:	DR_2115

Organism

Deinococcus radiodurans

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	156 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds to the 23S rRNA. HAMAP MF_01341_B
Subunit structure	Part of the 50S ribosomal subunit. Contacts proteins L4, L21 and L35. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8
Sequence similarities	Belongs to the ribosomal protein L15P family.

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: InterPro
Cellular component	large ribosomal subunit Inferred from electronic annotation. Source: InterPro
Molecular function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 156

156

50S ribosomal protein L15 HAMAP MF_01341_B

PRO_0000104716

Secondary structure

156

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9RSK9 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 04D58FA897437A33
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FASTA

156

16,860

        10         20         30         40         50         60 
MKLHDLKPTP GSRKDRKRVG RGPGGTDKTA GRGHKGQKSR SGAGKGAFFE GGRSRLIARL 

        70         80         90        100        110        120 
PKRGFNNVGT TYEVVKLSQL QDLEDTTFDR DTLEAYRLVR RKNRPVKLLA SGEISRAVTV 

       130        140        150 
HVDAASAAAI KAVEAAGGRV VLPEVQTQQD DAQKAE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[2]	"High resolution structure of the large ribosomal subunit from a mesophilic eubacterium." Harms J., Schluenzen F., Zarivach R., Bashan A., Gat S., Agmon I., Bartels H., Franceschi F., Yonath A. Cell 107:679-688(2001) [PubMed: 11733066] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT, PROTEIN SEQUENCE OF 1-5. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[3]	"Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria." Schluenzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R., Yonath A., Franceschi F. Nature 413:814-821(2001) [PubMed: 11677599] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[4]	"Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression." Bashan A., Agmon I., Zarivach R., Schluenzen F., Harms J., Berisio R., Bartels H., Franceschi F., Auerbach T., Hansen H.A., Kossoy E., Kessler M., Yonath A. Mol. Cell 11:91-102(2003) [PubMed: 12535524] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH TRNA MIMICS. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[5]	"Structural basis for the antibiotic activity of ketolides and azalides." Schluenzen F., Harms J.M., Franceschi F., Hansen H.A., Bartels H., Zarivach R., Yonath A. Structure 11:329-338(2003) [PubMed: 12623020] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH MODIFIED MACROLIDE ANTIBIOTICS. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[6]	"Structural insight into the role of the ribosomal tunnel in cellular regulation." Berisio R., Schluenzen F., Harms J., Bashan A., Auerbach T., Baram D., Yonath A. Nat. Struct. Biol. 10:366-370(2003) [PubMed: 12665853] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH TROLEANDOMYCIN. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[7]	"Alterations at the peptidyl transferase centre of the ribosome induced by the synergistic action of the streptogramins dalfopristin and quinupristin." Harms J.M., Schluenzen F., Fucini P., Bartels H., Yonath A. BMC Biol. 2:4-4(2004) [PubMed: 15059283] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH THE STREPTOGRAMINS QUINUPRISTIN AND DALFOPRISTIN. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[8]	"Inhibition of peptide bond formation by pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin." Schluenzen F., Pyetan E., Fucini P., Yonath A., Harms J.M. Mol. Microbiol. 54:1287-1294(2004) [PubMed: 15554968] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH TIAMULIN. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000513 Genomic DNA. Translation: AAF11664.1.

PIR

F75314.

RefSeq

NP_295838.1. NC_001263.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GS2	model	-	J	68-145	[»]
1NKW	X-ray	3.10	J	1-156	[»]
1NWX	X-ray	3.50	J	1-156	[»]
1NWY	X-ray	3.30	J	1-156	[»]
1PNU	X-ray	8.70	J	4-144	[»]
1PNY	X-ray	9.50	J	4-144	[»]
1SM1	X-ray	3.42	J	1-156	[»]
1XBP	X-ray	3.50	J	1-156	[»]
2ZJP	X-ray	3.70	I	1-156	[»]
2ZJQ	X-ray	3.30	I	1-156	[»]
2ZJR	X-ray	2.91	I	1-156	[»]
3CF5	X-ray	3.30	I	1-156	[»]
3DLL	X-ray	3.50	I	1-156	[»]
3PIO	X-ray	3.25	I	1-156	[»]
3PIP	X-ray	3.45	I	1-156	[»]

ProteinModelPortal

Q9RSK9.

SMR

Q9RSK9. Positions 4-144.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1797297.

GenomeReviews

Gene locus DR_2115 in contig AE000513_GR.

KEGG

dra:DR_2115.

NMPDR

fig|243230.1.peg.2297.

PATRIC

21631906. VBIDeiRad64572_2338.

TIGR

DR_2115.

Phylogenomic databases

HOGENOM

HBG727142.

OMA

RKGRGHA.

PhylomeDB

Q9RSK9.

ProtClustDB

PRK05592.

Enzyme and pathway databases

BioCyc

DRAD243230:DR_2115-MONOMER.

Family and domain databases

HAMAP

MF_01341_B. Ribosomal_L15_B.
[Tree]

InterPro

IPR005749. Ribosomal_L15_bac-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]

K02876.

PANTHER

PTHR12934. Ribosom_L15_bac. 1 hit.

Pfam

PF00828. Ribosomal_L18e. 1 hit.
[Graphical view]

SUPFAM

SSF52080. Ribosomal_L18e/L15. 1 hit.

TIGRFAMs

TIGR01071. RplO_bact. 1 hit.

PROSITE

PS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

RL15_DEIRA

Accession

Primary (citable) accession number: Q9RSK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2004
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents