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P12737 (RL15_HALMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
50S ribosomal protein L15P
Alternative name(s):
Hl9
Hmal15
Gene names
Name:rpl15p
Ordered Locus Names:rrnAC1590
OrganismHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui) [Complete proteome] [HAMAP]
Taxonomic identifier272569 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 Ref.14

Sequence similarities

Belongs to the ribosomal protein L15P family.

Ontologies

Keywords
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processtranslation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentlarge ribosomal subunit

Inferred from electronic annotation. Source: InterPro

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.5
Chain2 – 16516450S ribosomal protein L15P HAMAP-Rule MF_01341_A
PRO_0000104860

Experimental info

Sequence conflict21T → D AA sequence Ref.5
Sequence conflict31 – 322RG → NR AA sequence Ref.5

Secondary structure

................................... 165
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12737 [UniParc].

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

FASTA16517,973
        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' 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.
[14]"Revisiting the Haloarcula marismortui 50S ribosomal subunit model."
Gabdulkhakov A., Nikonov S., Garber M.
Acta Crystallogr. D 69:997-1004(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF THE 50S SUBUNIT.
+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.
PIRR6HS15. S22349.
RefSeqYP_136214.1. NC_006396.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FFKX-ray2.40J2-165[»]
1JJ2X-ray2.40K2-165[»]
1K73X-ray3.01M2-165[»]
1K8AX-ray3.00M2-165[»]
1K9MX-ray3.00M2-165[»]
1KC8X-ray3.01M2-165[»]
1KD1X-ray3.00M2-165[»]
1KQSX-ray3.10K2-165[»]
1M1KX-ray3.20M2-165[»]
1M90X-ray2.80M2-165[»]
1N8RX-ray3.00M2-165[»]
1NJIX-ray3.00M2-165[»]
1Q7YX-ray3.20M2-165[»]
1Q81X-ray2.95M2-165[»]
1Q82X-ray2.98M2-165[»]
1Q86X-ray3.00M2-165[»]
1QVFX-ray3.10K2-165[»]
1QVGX-ray2.90K2-165[»]
1S72X-ray2.40L1-165[»]
1VQ4X-ray2.70L1-165[»]
1VQ5X-ray2.60L1-165[»]
1VQ6X-ray2.70L1-165[»]
1VQ7X-ray2.50L1-165[»]
1VQ8X-ray2.20L1-165[»]
1VQ9X-ray2.40L1-165[»]
1VQKX-ray2.30L1-165[»]
1VQLX-ray2.30L1-165[»]
1VQMX-ray2.30L1-165[»]
1VQNX-ray2.40L1-165[»]
1VQOX-ray2.20L1-165[»]
1VQPX-ray2.25L1-165[»]
1W2BX-ray3.50K2-165[»]
1YHQX-ray2.40L1-165[»]
1YI2X-ray2.65L1-165[»]
1YIJX-ray2.60L1-165[»]
1YITX-ray2.80L1-165[»]
1YJ9X-ray2.90L1-165[»]
1YJNX-ray3.00L1-165[»]
1YJWX-ray2.90L1-165[»]
2B66X-ray5.90P2-165[»]
2B9NX-ray6.76P2-165[»]
2B9PX-ray6.46P2-165[»]
2OTJX-ray2.90L1-165[»]
2OTLX-ray2.70L1-165[»]
2QA4X-ray3.00L1-165[»]
2QEXX-ray2.90L1-165[»]
3CC2X-ray2.40L1-165[»]
3CC4X-ray2.70L1-165[»]
3CC7X-ray2.70L1-165[»]
3CCEX-ray2.75L1-165[»]
3CCJX-ray2.70L1-165[»]
3CCLX-ray2.90L1-165[»]
3CCMX-ray2.55L1-165[»]
3CCQX-ray2.90L1-165[»]
3CCRX-ray3.00L1-165[»]
3CCSX-ray2.95L1-165[»]
3CCUX-ray2.80L1-165[»]
3CCVX-ray2.90L1-165[»]
3CD6X-ray2.75L1-165[»]
3CMAX-ray2.80L1-165[»]
3CMEX-ray2.95L1-165[»]
3CPWX-ray2.70K1-165[»]
3CXCX-ray3.00K2-165[»]
3G4SX-ray3.20L1-165[»]
3G6EX-ray2.70L1-165[»]
3G71X-ray2.85L1-165[»]
3I55X-ray3.11L1-165[»]
3I56X-ray2.90L1-165[»]
3OW2X-ray2.70K2-151[»]
4ADXelectron microscopy6.60L1-165[»]
4HUBX-ray2.40L1-165[»]
ProteinModelPortalP12737.
SMRP12737. Positions 2-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272569.rrnAC1590.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV46508; AAV46508; rrnAC1590.
GeneID3128809.
KEGGhma:rrnAC1590.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0200.
HOGENOMHOG000231263.
KOK02876.
OMASHTHGWG.

Enzyme and pathway databases

BioCycHMAR272569:GJDH-1446-MONOMER.

Family and domain databases

Gene3D4.10.990.10. 1 hit.
HAMAPMF_01341_A. Ribosomal_L15_A.
InterProIPR027386. 50S_Rbsml_prot_L15P_N.
IPR023681. Ribosomal_L15_arc-type.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PfamPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMSSF52080. SSF52080. 1 hit.
PROSITEPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12737.

Entry information

Entry nameRL15_HALMA
AccessionPrimary (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: July 9, 2014
This is version 111 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references