50S ribosomal protein L15P - Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

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P12737 (RL15_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 104. 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 L15P

Alternative name(s):
Hl9
Hmal15

Gene names

Name:	rpl15p
Ordered Locus Names:	rrnAC1590

Organism

Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]

Taxonomic identifier

272569 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Haloarcula ›

Protein attributes

Sequence length	165 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	Binds to the 23S rRNA. HAMAP-Rule MF_01341_A
Subunit structure	Part of the 50S ribosomal subunit. Interacts weakly with proteins L18e and L32e. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
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
Gene Ontology (GO)
Biological_process	translation Inferred from electronic annotation. Source: HAMAP
Cellular_component	large ribosomal subunit Inferred from electronic annotation. Source: InterPro
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.3 Ref.5

Chain

2 – 165

164

50S ribosomal protein L15P HAMAP-Rule MF_01341_A

PRO_0000104860

Experimental info

Sequence conflict

T → D AA sequence Ref.5

Sequence conflict

31 – 32

RG → NR AA sequence Ref.5

Secondary structure

165

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P12737 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: AAF4318ADF0D8879
Show »

FASTA

165

17,973

        10         20         30         40         50         60 
MTSKKKRQRG SRTHGGGSHK NRRGAGHRGG RGDAGRDKHE FHNHEPLGKS GFKRPQKVQE 

        70         80         90        100        110        120 
EAATIDVREI DENVTLLAAD DVAEVEDGGF RVDVRDVVEE ADDADYVKVL GAGQVRHELT 

       130        140        150        160 
LIADDFSEGA REKVEGAGGS VELTDLGEER QAEAEETEDA DADEE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genes for ribosomal protein L15 and the protein equivalent to secY in the archaebacterium Haloarcula (Halobacterium) marismortui." Arndt E. Biochim. Biophys. Acta 1130:113-116(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea." Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V. Genome Res. 14:2221-2234(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[3]	"Primary structures of five ribosomal proteins from the archaebacterium Halobacterium marismortui and their structural relationships to eubacterial and eukaryotic ribosomal proteins." Hatakeyama T., Kaufmann F., Schroeter B., Hatakeyama T. Eur. J. Biochem. 185:685-693(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-155.
[4]	"Organization and nucleotide sequence of ten ribosomal protein genes from the region equivalent to the spectinomycin operon in the archaebacterium Halobacterium marismortui." Scholzen T., Arndt E. Mol. Gen. Genet. 228:70-80(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
[5]	"Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and poly(vinylidene difluoride) membrane." Walsh M.J., McDougall J., Wittmann-Liebold B. Biochemistry 27:6867-6876(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-32.
[6]	"The complete atomic structure of the large ribosomal subunit at 2.4 A resolution." Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. Science 289:905-920(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[7]	"The structural basis of ribosome activity in peptide bond synthesis." Nissen P., Hansen J., Ban N., Moore P.B., Steitz T.A. Science 289:920-930(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[8]	"A pre-translocational intermediate in protein synthesis observed in crystals of enzymatically active 50S subunits." Schmeing T.M., Seila A.C., Hansen J.L., Freeborn B., Soukup J.K., Scaringe S.A., Strobel S.A., Moore P.B., Steitz T.A. Nat. Struct. Biol. 9:225-230(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[9]	"The kink-turn: a new RNA secondary structure motif." Klein D.J., Schmeing T.M., Moore P.B., Steitz T.A. EMBO J. 20:4214-4221(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[10]	"The structures of four macrolide antibiotics bound to the large ribosomal subunit." Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., Steitz T.A. Mol. Cell 10:117-128(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FOUR MACROLIDE ANTIBIOTICS. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[11]	"Structural insights into peptide bond formation." Hansen J.L., Schmeing T.M., Moore P.B., Steitz T.A. Proc. Natl. Acad. Sci. U.S.A. 99:11670-11675(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[12]	"Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit." Hansen J.L., Moore P.B., Steitz T.A. J. Mol. Biol. 330:1061-1075(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE 50S SUBUNIT IN COMPLEX WITH FIVE ANTIBIOTICS AT THE PEPTIDYL TRANSFERASE CENTER. Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
[13]	"Structures of deacylated tRNA mimics bound to the E site of the large ribosomal subunit." Schmeing T.M., Moore P.B., Steitz T.A. RNA 9:1345-1352(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF THE 50S SUBUNIT WITH TWO DIFFERENT E SITE SUBSTRATES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X63127 Genomic DNA. Translation: CAA44837.1.
AY596297 Genomic DNA. Translation: AAV46508.1.
X58395 Genomic DNA. Translation: CAA41293.1.

PIR

R6HS15. S22349.

RefSeq

YP_136214.1. NC_006396.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FFK	X-ray	2.40	J	2-165	[»]
1JJ2	X-ray	2.40	K	2-165	[»]
1K73	X-ray	3.01	M	2-165	[»]
1K8A	X-ray	3.00	M	2-165	[»]
1K9M	X-ray	3.00	M	2-165	[»]
1KC8	X-ray	3.01	M	2-165	[»]
1KD1	X-ray	3.00	M	2-165	[»]
1KQS	X-ray	3.10	K	2-165	[»]
1M1K	X-ray	3.20	M	2-165	[»]
1M90	X-ray	2.80	M	2-165	[»]
1N8R	X-ray	3.00	M	2-165	[»]
1NJI	X-ray	3.00	M	2-165	[»]
1Q7Y	X-ray	3.20	M	2-165	[»]
1Q81	X-ray	2.95	M	2-165	[»]
1Q82	X-ray	2.98	M	2-165	[»]
1Q86	X-ray	3.00	M	2-165	[»]
1QVF	X-ray	3.10	K	2-165	[»]
1QVG	X-ray	2.90	K	2-165	[»]
1S72	X-ray	2.40	L	1-165	[»]
1VQ4	X-ray	2.70	L	1-165	[»]
1VQ5	X-ray	2.60	L	1-165	[»]
1VQ6	X-ray	2.70	L	1-165	[»]
1VQ7	X-ray	2.50	L	1-165	[»]
1VQ8	X-ray	2.20	L	1-165	[»]
1VQ9	X-ray	2.40	L	1-165	[»]
1VQK	X-ray	2.30	L	1-165	[»]
1VQL	X-ray	2.30	L	1-165	[»]
1VQM	X-ray	2.30	L	1-165	[»]
1VQN	X-ray	2.40	L	1-165	[»]
1VQO	X-ray	2.20	L	1-165	[»]
1VQP	X-ray	2.25	L	1-165	[»]
1W2B	X-ray	3.50	K	2-164	[»]
1YHQ	X-ray	2.40	L	1-165	[»]
1YI2	X-ray	2.65	L	1-165	[»]
1YIJ	X-ray	2.60	L	1-165	[»]
1YIT	X-ray	2.80	L	1-165	[»]
1YJ9	X-ray	2.90	L	1-165	[»]
1YJN	X-ray	3.00	L	1-165	[»]
1YJW	X-ray	2.90	L	1-165	[»]
2OTJ	X-ray	2.90	L	1-165	[»]
2OTL	X-ray	2.70	L	1-165	[»]
2QA4	X-ray	3.00	L	1-165	[»]
2QEX	X-ray	2.90	L	1-165	[»]
3CC2	X-ray	2.40	L	1-165	[»]
3CC4	X-ray	2.70	L	1-165	[»]
3CC7	X-ray	2.70	L	1-165	[»]
3CCE	X-ray	2.75	L	1-165	[»]
3CCJ	X-ray	2.70	L	1-165	[»]
3CCL	X-ray	2.90	L	1-165	[»]
3CCM	X-ray	2.55	L	1-165	[»]
3CCQ	X-ray	2.90	L	1-165	[»]
3CCR	X-ray	3.00	L	1-165	[»]
3CCS	X-ray	2.95	L	1-165	[»]
3CCU	X-ray	2.80	L	1-165	[»]
3CCV	X-ray	2.90	L	1-165	[»]
3CD6	X-ray	2.75	L	1-165	[»]
3CMA	X-ray	2.80	L	1-165	[»]
3CME	X-ray	2.95	L	1-165	[»]
3CPW	X-ray	2.70	K	1-165	[»]
3CXC	X-ray	3.00	K	2-164	[»]
3G4S	X-ray	3.20	L	1-165	[»]
3G6E	X-ray	2.70	L	1-165	[»]
3G71	X-ray	2.85	L	1-165	[»]
3I55	X-ray	3.11	L	1-165	[»]
3I56	X-ray	2.90	L	1-165	[»]
3OW2	X-ray	2.70	K	2-151	[»]

ProteinModelPortal

P12737.

SMR

P12737. Positions 2-151.

ModBase

Search...

Protein-protein interaction databases

STRING

272569.rrnAC1590.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAV46508; AAV46508; rrnAC1590.

GeneID

3128809.

KEGG

hma:rrnAC1590.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG0200.

HOGENOM

HOG000231263.

K02876.

OMA

SHTHGWG.

ProtClustDB

PRK06419.

Enzyme and pathway databases

BioCyc

HMAR272569:GJDH-1446-MONOMER.

Family and domain databases

Gene3D

4.10.990.10. 1 hit.

HAMAP

MF_01341_A. Ribosomal_L15_A.

InterPro

IPR027386. 50S_Rbsml_prot_L15P_N.
IPR023681. Ribosomal_L15_arc-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]

Pfam

PF00828. Ribosomal_L18e. 1 hit.
[Graphical view]

SUPFAM

SSF52080. Ribosomal_L18e/L15. 1 hit.

PROSITE

PS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12737.

Entry information

Entry name

RL15_HALMA

Accession

Primary (citable) accession number: P12737
Secondary accession number(s): Q5V1U4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 104 of the entry and version 4 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

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents