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P12737

- RL15_HALMA

UniProt

P12737 - RL15_HALMA

Protein

50S ribosomal protein L15

Gene

rpl15

Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Binds to the 23S rRNA.

    GO - Molecular functioni

    1. rRNA binding Source: UniProtKB-HAMAP
    2. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciHMAR272569:GJDH-1446-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L15
    Alternative name(s):
    Hl9
    Hmal15
    Gene namesi
    Name:rpl15
    Ordered Locus Names:rrnAC1590
    OrganismiHaloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809) (Halobacterium marismortui)
    Taxonomic identifieri272569 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloarcula
    ProteomesiUP000001169: Chromosome I

    Subcellular locationi

    GO - Cellular componenti

    1. large ribosomal subunit Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 16516450S ribosomal protein L15PRO_0000104860Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Interacts weakly with proteins L18e and L32e.2 Publications

    Protein-protein interaction databases

    STRINGi272569.rrnAC1590.

    Structurei

    Secondary structure

    1
    165
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 74
    Turni8 – 103
    Beta strandi11 – 133
    Beta strandi16 – 183
    Beta strandi21 – 244
    Helixi25 – 284
    Turni32 – 409
    Beta strandi42 – 443
    Helixi56 – 583
    Beta strandi62 – 665
    Helixi67 – 726
    Helixi75 – 773
    Beta strandi91 – 933
    Helixi94 – 963
    Turni99 – 1035
    Beta strandi104 – 1107
    Beta strandi120 – 1267
    Helixi128 – 1369
    Beta strandi140 – 1434
    Turni145 – 1473

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP12737.
    SMRiP12737. Positions 2-151.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12737.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L15P family.Curated

    Phylogenomic databases

    eggNOGiCOG0200.
    HOGENOMiHOG000231263.
    KOiK02876.
    OMAiSHTHGWG.

    Family and domain databases

    Gene3Di4.10.990.10. 1 hit.
    HAMAPiMF_01341. Ribosomal_L15.
    InterProiIPR027386. 50S_Rbsml_prot_L15P_N.
    IPR023681. Ribosomal_L15_arc-type.
    IPR001196. Ribosomal_L15_CS.
    IPR021131. Ribosomal_L18e/L15P.
    [Graphical view]
    PfamiPF00828. Ribosomal_L18e. 1 hit.
    [Graphical view]
    SUPFAMiSSF52080. SSF52080. 1 hit.
    PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P12737-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSKKKRQRG SRTHGGGSHK NRRGAGHRGG RGDAGRDKHE FHNHEPLGKS    50
    GFKRPQKVQE EAATIDVREI DENVTLLAAD DVAEVEDGGF RVDVRDVVEE 100
    ADDADYVKVL GAGQVRHELT LIADDFSEGA REKVEGAGGS VELTDLGEER 150
    QAEAEETEDA DADEE 165
    Length:165
    Mass (Da):17,973
    Last modified:January 23, 2007 - v4
    Checksum:iAAF4318ADF0D8879
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21T → D AA sequence (PubMed:3196689)Curated
    Sequence conflicti31 – 322RG → NR AA sequence (PubMed:3196689)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63127 Genomic DNA. Translation: CAA44837.1.
    AY596297 Genomic DNA. Translation: AAV46508.1.
    X58395 Genomic DNA. Translation: CAA41293.1.
    PIRiS22349. R6HS15.
    RefSeqiWP_011223737.1. NC_006396.1.
    YP_136214.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46508; AAV46508; rrnAC1590.
    GeneIDi3128809.
    KEGGihma:rrnAC1590.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X63127 Genomic DNA. Translation: CAA44837.1 .
    AY596297 Genomic DNA. Translation: AAV46508.1 .
    X58395 Genomic DNA. Translation: CAA41293.1 .
    PIRi S22349. R6HS15.
    RefSeqi WP_011223737.1. NC_006396.1.
    YP_136214.1. NC_006396.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 2-165 [» ]
    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 [» ]
    2B66 X-ray 5.90 P 2-165 [» ]
    2B9N X-ray 6.76 P 2-165 [» ]
    2B9P X-ray 6.46 P 2-165 [» ]
    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 2-165 [» ]
    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 [» ]
    4ADX electron microscopy 6.60 L 1-165 [» ]
    4HUB X-ray 2.40 L 1-165 [» ]
    ProteinModelPortali P12737.
    SMRi P12737. Positions 2-151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1590.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46508 ; AAV46508 ; rrnAC1590 .
    GeneIDi 3128809.
    KEGGi hma:rrnAC1590.

    Phylogenomic databases

    eggNOGi COG0200.
    HOGENOMi HOG000231263.
    KOi K02876.
    OMAi SHTHGWG.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1446-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P12737.

    Family and domain databases

    Gene3Di 4.10.990.10. 1 hit.
    HAMAPi MF_01341. Ribosomal_L15.
    InterProi IPR027386. 50S_Rbsml_prot_L15P_N.
    IPR023681. Ribosomal_L15_arc-type.
    IPR001196. Ribosomal_L15_CS.
    IPR021131. Ribosomal_L18e/L15P.
    [Graphical view ]
    Pfami PF00828. Ribosomal_L18e. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52080. SSF52080. 1 hit.
    PROSITEi PS00475. RIBOSOMAL_L15. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiRL15_HALMA
    AccessioniPrimary (citable) accession number: P12737
    Secondary accession number(s): Q5V1U4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 113 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3