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P14135

- RL6_HALMA

UniProt

P14135 - RL6_HALMA

Protein

50S ribosomal protein L6

Gene

rpl6

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 116 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.

    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-1452-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L6UniRule annotation
    Alternative name(s):
    Hl10
    Hmal6
    Gene namesi
    Name:rpl6UniRule annotation
    Ordered Locus Names:rrnAC1596
    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. ribosome Source: UniProtKB-KW

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 17817750S ribosomal protein L6PRO_0000131083Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Interacts weakly with protein L13.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi272569.rrnAC1596.

    Structurei

    Secondary structure

    1
    178
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75
    Beta strandi13 – 175
    Beta strandi20 – 256
    Beta strandi28 – 336
    Beta strandi40 – 445
    Beta strandi47 – 515
    Helixi57 – 7721
    Beta strandi81 – 888
    Beta strandi90 – 923
    Beta strandi95 – 995
    Beta strandi102 – 1076
    Helixi108 – 1103
    Beta strandi115 – 1184
    Beta strandi124 – 1285
    Beta strandi131 – 1377
    Helixi139 – 15113
    Beta strandi156 – 1583
    Turni160 – 1623
    Beta strandi166 – 1716

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C04X-ray5.00B21-25[»]
    1FFKX-ray2.4012-178[»]
    1JJ2X-ray2.40E2-178[»]
    1K73X-ray3.01G2-178[»]
    1K8AX-ray3.00G2-178[»]
    1K9MX-ray3.00G2-178[»]
    1KC8X-ray3.01G2-178[»]
    1KD1X-ray3.00G2-178[»]
    1KQSX-ray3.10E2-178[»]
    1M1KX-ray3.20G2-178[»]
    1M90X-ray2.80G2-178[»]
    1N8RX-ray3.00G2-178[»]
    1NJIX-ray3.00G2-178[»]
    1Q7YX-ray3.20G2-178[»]
    1Q81X-ray2.95G2-178[»]
    1Q82X-ray2.98G2-178[»]
    1Q86X-ray3.00G2-178[»]
    1QVFX-ray3.10E2-178[»]
    1QVGX-ray2.90E2-178[»]
    1S72X-ray2.40E1-178[»]
    1VQ4X-ray2.70E1-178[»]
    1VQ5X-ray2.60E1-178[»]
    1VQ6X-ray2.70E1-178[»]
    1VQ7X-ray2.50E1-178[»]
    1VQ8X-ray2.20E1-178[»]
    1VQ9X-ray2.40E1-178[»]
    1VQKX-ray2.30E1-178[»]
    1VQLX-ray2.30E1-178[»]
    1VQMX-ray2.30E1-178[»]
    1VQNX-ray2.40E1-178[»]
    1VQOX-ray2.20E1-178[»]
    1VQPX-ray2.25E1-178[»]
    1W2BX-ray3.50E2-178[»]
    1YHQX-ray2.40E1-178[»]
    1YI2X-ray2.65E1-178[»]
    1YIJX-ray2.60E1-178[»]
    1YITX-ray2.80E1-178[»]
    1YJ9X-ray2.90E1-178[»]
    1YJNX-ray3.00E1-178[»]
    1YJWX-ray2.90E1-178[»]
    2OTJX-ray2.90E1-178[»]
    2OTLX-ray2.70E1-178[»]
    2QA4X-ray3.00E1-178[»]
    2QEXX-ray2.90E1-178[»]
    3CC2X-ray2.40E1-178[»]
    3CC4X-ray2.70E1-178[»]
    3CC7X-ray2.70E1-178[»]
    3CCEX-ray2.75E1-178[»]
    3CCJX-ray2.70E1-178[»]
    3CCLX-ray2.90E1-178[»]
    3CCMX-ray2.55E1-178[»]
    3CCQX-ray2.90E1-178[»]
    3CCRX-ray3.00E1-178[»]
    3CCSX-ray2.95E1-178[»]
    3CCUX-ray2.80E1-178[»]
    3CCVX-ray2.90E1-178[»]
    3CD6X-ray2.75E1-178[»]
    3CMAX-ray2.80E1-178[»]
    3CMEX-ray2.95E1-178[»]
    3CPWX-ray2.70E1-178[»]
    3CXCX-ray3.00E2-178[»]
    3G4SX-ray3.20E2-173[»]
    3G6EX-ray2.70E2-173[»]
    3G71X-ray2.85E2-173[»]
    3I55X-ray3.11E1-178[»]
    3I56X-ray2.90E1-178[»]
    3OW2X-ray2.70E2-173[»]
    4ADXelectron microscopy6.60E1-178[»]
    4HUBX-ray2.40E1-178[»]
    ProteinModelPortaliP14135.
    SMRiP14135. Positions 2-173.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14135.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L6P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0097.
    HOGENOMiHOG000039905.
    KOiK02933.
    OMAiPRRTTIH.

    Family and domain databases

    Gene3Di3.90.930.12. 2 hits.
    HAMAPiMF_01365_A. Ribosomal_L6_A.
    InterProiIPR000702. Ribosomal_L6.
    IPR020040. Ribosomal_L6_a/b-dom.
    IPR002359. Ribosomal_L6_CS2.
    IPR019907. Ribosomal_L6P_arc.
    [Graphical view]
    PANTHERiPTHR11655. PTHR11655. 1 hit.
    PfamiPF00347. Ribosomal_L6. 2 hits.
    [Graphical view]
    PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
    SUPFAMiSSF56053. SSF56053. 2 hits.
    TIGRFAMsiTIGR03653. arch_L6P. 1 hit.
    PROSITEiPS00700. RIBOSOMAL_L6_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P14135-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRVELEIPE DVDAEQDHLD ITVEGDNGSV TRRLWYPDID VSVDGDTVVI    50
    ESDEDNAKTM STIGTFQSHI ENMFHGVTEG WEYGMEVFYS HFPMQVNVEG 100
    DEVVIENFLG EKAPRRTTIH GDTDVEIDGE ELTVSGPDIE AVGQTAADIE 150
    QLTRINDKDV RVFQDGVYIT RKPNRGDA 178
    Length:178
    Mass (Da):19,944
    Last modified:January 23, 2007 - v3
    Checksum:i380872452165689C
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31R → S.
    Natural varianti24 – 241E → S.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58395 Genomic DNA. Translation: CAA41287.1.
    AY596297 Genomic DNA. Translation: AAV46514.1.
    PIRiS16538. R5HS6L.
    RefSeqiWP_011223740.1. NC_006396.1.
    YP_136220.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46514; AAV46514; rrnAC1596.
    GeneIDi3127517.
    KEGGihma:rrnAC1596.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58395 Genomic DNA. Translation: CAA41287.1 .
    AY596297 Genomic DNA. Translation: AAV46514.1 .
    PIRi S16538. R5HS6L.
    RefSeqi WP_011223740.1. NC_006396.1.
    YP_136220.1. NC_006396.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C04 X-ray 5.00 B 21-25 [» ]
    1FFK X-ray 2.40 1 2-178 [» ]
    1JJ2 X-ray 2.40 E 2-178 [» ]
    1K73 X-ray 3.01 G 2-178 [» ]
    1K8A X-ray 3.00 G 2-178 [» ]
    1K9M X-ray 3.00 G 2-178 [» ]
    1KC8 X-ray 3.01 G 2-178 [» ]
    1KD1 X-ray 3.00 G 2-178 [» ]
    1KQS X-ray 3.10 E 2-178 [» ]
    1M1K X-ray 3.20 G 2-178 [» ]
    1M90 X-ray 2.80 G 2-178 [» ]
    1N8R X-ray 3.00 G 2-178 [» ]
    1NJI X-ray 3.00 G 2-178 [» ]
    1Q7Y X-ray 3.20 G 2-178 [» ]
    1Q81 X-ray 2.95 G 2-178 [» ]
    1Q82 X-ray 2.98 G 2-178 [» ]
    1Q86 X-ray 3.00 G 2-178 [» ]
    1QVF X-ray 3.10 E 2-178 [» ]
    1QVG X-ray 2.90 E 2-178 [» ]
    1S72 X-ray 2.40 E 1-178 [» ]
    1VQ4 X-ray 2.70 E 1-178 [» ]
    1VQ5 X-ray 2.60 E 1-178 [» ]
    1VQ6 X-ray 2.70 E 1-178 [» ]
    1VQ7 X-ray 2.50 E 1-178 [» ]
    1VQ8 X-ray 2.20 E 1-178 [» ]
    1VQ9 X-ray 2.40 E 1-178 [» ]
    1VQK X-ray 2.30 E 1-178 [» ]
    1VQL X-ray 2.30 E 1-178 [» ]
    1VQM X-ray 2.30 E 1-178 [» ]
    1VQN X-ray 2.40 E 1-178 [» ]
    1VQO X-ray 2.20 E 1-178 [» ]
    1VQP X-ray 2.25 E 1-178 [» ]
    1W2B X-ray 3.50 E 2-178 [» ]
    1YHQ X-ray 2.40 E 1-178 [» ]
    1YI2 X-ray 2.65 E 1-178 [» ]
    1YIJ X-ray 2.60 E 1-178 [» ]
    1YIT X-ray 2.80 E 1-178 [» ]
    1YJ9 X-ray 2.90 E 1-178 [» ]
    1YJN X-ray 3.00 E 1-178 [» ]
    1YJW X-ray 2.90 E 1-178 [» ]
    2OTJ X-ray 2.90 E 1-178 [» ]
    2OTL X-ray 2.70 E 1-178 [» ]
    2QA4 X-ray 3.00 E 1-178 [» ]
    2QEX X-ray 2.90 E 1-178 [» ]
    3CC2 X-ray 2.40 E 1-178 [» ]
    3CC4 X-ray 2.70 E 1-178 [» ]
    3CC7 X-ray 2.70 E 1-178 [» ]
    3CCE X-ray 2.75 E 1-178 [» ]
    3CCJ X-ray 2.70 E 1-178 [» ]
    3CCL X-ray 2.90 E 1-178 [» ]
    3CCM X-ray 2.55 E 1-178 [» ]
    3CCQ X-ray 2.90 E 1-178 [» ]
    3CCR X-ray 3.00 E 1-178 [» ]
    3CCS X-ray 2.95 E 1-178 [» ]
    3CCU X-ray 2.80 E 1-178 [» ]
    3CCV X-ray 2.90 E 1-178 [» ]
    3CD6 X-ray 2.75 E 1-178 [» ]
    3CMA X-ray 2.80 E 1-178 [» ]
    3CME X-ray 2.95 E 1-178 [» ]
    3CPW X-ray 2.70 E 1-178 [» ]
    3CXC X-ray 3.00 E 2-178 [» ]
    3G4S X-ray 3.20 E 2-173 [» ]
    3G6E X-ray 2.70 E 2-173 [» ]
    3G71 X-ray 2.85 E 2-173 [» ]
    3I55 X-ray 3.11 E 1-178 [» ]
    3I56 X-ray 2.90 E 1-178 [» ]
    3OW2 X-ray 2.70 E 2-173 [» ]
    4ADX electron microscopy 6.60 E 1-178 [» ]
    4HUB X-ray 2.40 E 1-178 [» ]
    ProteinModelPortali P14135.
    SMRi P14135. Positions 2-173.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1596.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46514 ; AAV46514 ; rrnAC1596 .
    GeneIDi 3127517.
    KEGGi hma:rrnAC1596.

    Phylogenomic databases

    eggNOGi COG0097.
    HOGENOMi HOG000039905.
    KOi K02933.
    OMAi PRRTTIH.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1452-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14135.

    Family and domain databases

    Gene3Di 3.90.930.12. 2 hits.
    HAMAPi MF_01365_A. Ribosomal_L6_A.
    InterProi IPR000702. Ribosomal_L6.
    IPR020040. Ribosomal_L6_a/b-dom.
    IPR002359. Ribosomal_L6_CS2.
    IPR019907. Ribosomal_L6P_arc.
    [Graphical view ]
    PANTHERi PTHR11655. PTHR11655. 1 hit.
    Pfami PF00347. Ribosomal_L6. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF002162. Ribosomal_L6. 1 hit.
    SUPFAMi SSF56053. SSF56053. 2 hits.
    TIGRFAMsi TIGR03653. arch_L6P. 1 hit.
    PROSITEi PS00700. RIBOSOMAL_L6_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    3. "The N-terminal sequence of ribosomal protein L10 from the archaebacterium Halobacterium marismortui and its relationship to eubacterial protein L6 and other ribosomal proteins."
      Dijk J., van den Broek R., Nasiulas G., Beck A., Reinhardt R., Wittmann-Liebold B.
      Biol. Chem. Hoppe-Seyler 368:921-925(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-55.
    4. "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 2-31.
    5. "Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit."
      Ban N., Nissen P., Hansen J., Capel M., Moore P.B., Steitz T.A.
      Nature 400:841-847(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
    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 nameiRL6_HALMA
    AccessioniPrimary (citable) accession number: P14135
    Secondary accession number(s): P12739, Q5V1T8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 3 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