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P22450

- RL14_HALMA

UniProt

P22450 - RL14_HALMA

Protein

50S ribosomal protein L14

Gene

rpl14

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 103 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Forms part of two intersubunit bridges in the 70S ribosome By similarity. Binds to 23S rRNA.By similarity

    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-1458-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L14UniRule annotation
    Alternative name(s):
    Hl27
    Hmal14
    Gene namesi
    Name:rpl14UniRule annotation
    Ordered Locus Names:rrnAC1602
    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
    Chaini1 – 13213250S ribosomal protein L14PRO_0000128571Add
    BLAST

    Proteomic databases

    PRIDEiP22450.

    Interactioni

    Subunit structurei

    The L3/L14/L24e cluster may contact the 16S rRNA in 2 intersubunit bridges By similarity. Part of the 50S ribosomal subunit. Forms a cluster with proteins L3 and L24e.By similarity2 Publications

    Protein-protein interaction databases

    STRINGi272569.rrnAC1602.

    Structurei

    Secondary structure

    1
    132
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Beta strandi17 – 204
    Beta strandi22 – 3413
    Beta strandi52 – 609
    Turni62 – 665
    Beta strandi68 – 758
    Beta strandi87 – 926
    Beta strandi94 – 985
    Beta strandi100 – 1023
    Beta strandi104 – 1074
    Beta strandi111 – 1144
    Helixi115 – 1206
    Helixi122 – 1254
    Beta strandi129 – 1324

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C04X-ray5.00D71-85[»]
    1FFKX-ray2.40H1-132[»]
    1JJ2X-ray2.40J1-132[»]
    1K73X-ray3.01L1-132[»]
    1K8AX-ray3.00L1-132[»]
    1K9MX-ray3.00L1-132[»]
    1KC8X-ray3.01L1-132[»]
    1KD1X-ray3.00L1-132[»]
    1KQSX-ray3.10J1-132[»]
    1M1KX-ray3.20L1-132[»]
    1M90X-ray2.80L1-132[»]
    1N8RX-ray3.00L1-132[»]
    1NJIX-ray3.00L1-132[»]
    1Q7YX-ray3.20L1-132[»]
    1Q81X-ray2.95L1-132[»]
    1Q82X-ray2.98L1-132[»]
    1Q86X-ray3.00L1-132[»]
    1QVFX-ray3.10J1-132[»]
    1QVGX-ray2.90J1-132[»]
    1S72X-ray2.40K1-132[»]
    1VQ4X-ray2.70K1-132[»]
    1VQ5X-ray2.60K1-132[»]
    1VQ6X-ray2.70K1-132[»]
    1VQ7X-ray2.50K1-132[»]
    1VQ8X-ray2.20K1-132[»]
    1VQ9X-ray2.40K1-132[»]
    1VQKX-ray2.30K1-132[»]
    1VQLX-ray2.30K1-132[»]
    1VQMX-ray2.30K1-132[»]
    1VQNX-ray2.40K1-132[»]
    1VQOX-ray2.20K1-132[»]
    1VQPX-ray2.25K1-132[»]
    1W2BX-ray3.50J1-132[»]
    1YHQX-ray2.40K1-132[»]
    1YI2X-ray2.65K1-132[»]
    1YIJX-ray2.60K1-132[»]
    1YITX-ray2.80K1-132[»]
    1YJ9X-ray2.90K1-132[»]
    1YJNX-ray3.00K1-132[»]
    1YJWX-ray2.90K1-132[»]
    2OTJX-ray2.90K1-132[»]
    2OTLX-ray2.70K1-132[»]
    2QA4X-ray3.00K1-132[»]
    2QEXX-ray2.90K1-132[»]
    3CC2X-ray2.40K1-132[»]
    3CC4X-ray2.70K1-132[»]
    3CC7X-ray2.70K1-132[»]
    3CCEX-ray2.75K1-132[»]
    3CCJX-ray2.70K1-132[»]
    3CCLX-ray2.90K1-132[»]
    3CCMX-ray2.55K1-132[»]
    3CCQX-ray2.90K1-132[»]
    3CCRX-ray3.00K1-132[»]
    3CCSX-ray2.95K1-132[»]
    3CCUX-ray2.80K1-132[»]
    3CCVX-ray2.90K1-132[»]
    3CD6X-ray2.75K1-132[»]
    3CMAX-ray2.80K1-132[»]
    3CMEX-ray2.95K1-132[»]
    3CPWX-ray2.70J1-132[»]
    3CXCX-ray3.00J1-132[»]
    3G4SX-ray3.20K1-132[»]
    3G6EX-ray2.70K1-132[»]
    3G71X-ray2.85K1-132[»]
    3I55X-ray3.11K1-132[»]
    3I56X-ray2.90K1-132[»]
    3OW2X-ray2.70J1-132[»]
    4ADXelectron microscopy6.60K1-132[»]
    4HUBX-ray2.40K1-132[»]
    ProteinModelPortaliP22450.
    SMRiP22450. Positions 1-132.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22450.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L14P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0093.
    HOGENOMiHOG000183703.
    KOiK02874.
    OMAiGFPKGTD.

    Family and domain databases

    Gene3Di2.40.150.20. 1 hit.
    HAMAPiMF_01367. Ribosomal_L14.
    InterProiIPR019972. Ribosomal_L14_CS.
    IPR023571. Ribosomal_L14_dom.
    IPR000218. Ribosomal_L14b/L23e.
    IPR019971. Ribosomal_L14P_arc.
    [Graphical view]
    PANTHERiPTHR11761. PTHR11761. 1 hit.
    PfamiPF00238. Ribosomal_L14. 1 hit.
    [Graphical view]
    SUPFAMiSSF50193. SSF50193. 1 hit.
    TIGRFAMsiTIGR03673. rpl14p_arch. 1 hit.
    PROSITEiPS00049. RIBOSOMAL_L14. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22450-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEALGADVTQ GLEKGSLITC ADNTGARELK VISVHGYSGT KNRHPKAGLG    50
    DKITVSVTKG TPEMRRQVLE AVVVRQRKPI RRPDGTRVKF EDNAAVIVDE 100
    NEDPRGTELK GPIAREVAQR FGSVASAATM IV 132
    Length:132
    Mass (Da):14,193
    Last modified:August 1, 1991 - v1
    Checksum:i536F9C4461B7EA87
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55311 Genomic DNA. Translation: CAA39018.1.
    AY596297 Genomic DNA. Translation: AAV46519.1.
    PIRiS10734. R5HS14.
    RefSeqiYP_136225.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46519; AAV46519; rrnAC1602.
    GeneIDi3128380.
    KEGGihma:rrnAC1602.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55311 Genomic DNA. Translation: CAA39018.1 .
    AY596297 Genomic DNA. Translation: AAV46519.1 .
    PIRi S10734. R5HS14.
    RefSeqi YP_136225.1. 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 D 71-85 [» ]
    1FFK X-ray 2.40 H 1-132 [» ]
    1JJ2 X-ray 2.40 J 1-132 [» ]
    1K73 X-ray 3.01 L 1-132 [» ]
    1K8A X-ray 3.00 L 1-132 [» ]
    1K9M X-ray 3.00 L 1-132 [» ]
    1KC8 X-ray 3.01 L 1-132 [» ]
    1KD1 X-ray 3.00 L 1-132 [» ]
    1KQS X-ray 3.10 J 1-132 [» ]
    1M1K X-ray 3.20 L 1-132 [» ]
    1M90 X-ray 2.80 L 1-132 [» ]
    1N8R X-ray 3.00 L 1-132 [» ]
    1NJI X-ray 3.00 L 1-132 [» ]
    1Q7Y X-ray 3.20 L 1-132 [» ]
    1Q81 X-ray 2.95 L 1-132 [» ]
    1Q82 X-ray 2.98 L 1-132 [» ]
    1Q86 X-ray 3.00 L 1-132 [» ]
    1QVF X-ray 3.10 J 1-132 [» ]
    1QVG X-ray 2.90 J 1-132 [» ]
    1S72 X-ray 2.40 K 1-132 [» ]
    1VQ4 X-ray 2.70 K 1-132 [» ]
    1VQ5 X-ray 2.60 K 1-132 [» ]
    1VQ6 X-ray 2.70 K 1-132 [» ]
    1VQ7 X-ray 2.50 K 1-132 [» ]
    1VQ8 X-ray 2.20 K 1-132 [» ]
    1VQ9 X-ray 2.40 K 1-132 [» ]
    1VQK X-ray 2.30 K 1-132 [» ]
    1VQL X-ray 2.30 K 1-132 [» ]
    1VQM X-ray 2.30 K 1-132 [» ]
    1VQN X-ray 2.40 K 1-132 [» ]
    1VQO X-ray 2.20 K 1-132 [» ]
    1VQP X-ray 2.25 K 1-132 [» ]
    1W2B X-ray 3.50 J 1-132 [» ]
    1YHQ X-ray 2.40 K 1-132 [» ]
    1YI2 X-ray 2.65 K 1-132 [» ]
    1YIJ X-ray 2.60 K 1-132 [» ]
    1YIT X-ray 2.80 K 1-132 [» ]
    1YJ9 X-ray 2.90 K 1-132 [» ]
    1YJN X-ray 3.00 K 1-132 [» ]
    1YJW X-ray 2.90 K 1-132 [» ]
    2OTJ X-ray 2.90 K 1-132 [» ]
    2OTL X-ray 2.70 K 1-132 [» ]
    2QA4 X-ray 3.00 K 1-132 [» ]
    2QEX X-ray 2.90 K 1-132 [» ]
    3CC2 X-ray 2.40 K 1-132 [» ]
    3CC4 X-ray 2.70 K 1-132 [» ]
    3CC7 X-ray 2.70 K 1-132 [» ]
    3CCE X-ray 2.75 K 1-132 [» ]
    3CCJ X-ray 2.70 K 1-132 [» ]
    3CCL X-ray 2.90 K 1-132 [» ]
    3CCM X-ray 2.55 K 1-132 [» ]
    3CCQ X-ray 2.90 K 1-132 [» ]
    3CCR X-ray 3.00 K 1-132 [» ]
    3CCS X-ray 2.95 K 1-132 [» ]
    3CCU X-ray 2.80 K 1-132 [» ]
    3CCV X-ray 2.90 K 1-132 [» ]
    3CD6 X-ray 2.75 K 1-132 [» ]
    3CMA X-ray 2.80 K 1-132 [» ]
    3CME X-ray 2.95 K 1-132 [» ]
    3CPW X-ray 2.70 J 1-132 [» ]
    3CXC X-ray 3.00 J 1-132 [» ]
    3G4S X-ray 3.20 K 1-132 [» ]
    3G6E X-ray 2.70 K 1-132 [» ]
    3G71 X-ray 2.85 K 1-132 [» ]
    3I55 X-ray 3.11 K 1-132 [» ]
    3I56 X-ray 2.90 K 1-132 [» ]
    3OW2 X-ray 2.70 J 1-132 [» ]
    4ADX electron microscopy 6.60 K 1-132 [» ]
    4HUB X-ray 2.40 K 1-132 [» ]
    ProteinModelPortali P22450.
    SMRi P22450. Positions 1-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1602.

    Proteomic databases

    PRIDEi P22450.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46519 ; AAV46519 ; rrnAC1602 .
    GeneIDi 3128380.
    KEGGi hma:rrnAC1602.

    Phylogenomic databases

    eggNOGi COG0093.
    HOGENOMi HOG000183703.
    KOi K02874.
    OMAi GFPKGTD.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1458-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P22450.

    Family and domain databases

    Gene3Di 2.40.150.20. 1 hit.
    HAMAPi MF_01367. Ribosomal_L14.
    InterProi IPR019972. Ribosomal_L14_CS.
    IPR023571. Ribosomal_L14_dom.
    IPR000218. Ribosomal_L14b/L23e.
    IPR019971. Ribosomal_L14P_arc.
    [Graphical view ]
    PANTHERi PTHR11761. PTHR11761. 1 hit.
    Pfami PF00238. Ribosomal_L14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50193. SSF50193. 1 hit.
    TIGRFAMsi TIGR03673. rpl14p_arch. 1 hit.
    PROSITEi PS00049. RIBOSOMAL_L14. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of four genes encoding ribosomal proteins from the 'S10 and spectinomycin' operon equivalent region in the archaebacterium Halobacterium marismortui."
      Arndt E.
      FEBS Lett. 267:193-198(1990) [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 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.
    4. "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.
    5. "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.
    6. "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.
    7. "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.
    8. "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.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    10. "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.
    11. "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.
    12. "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 nameiRL14_HALMA
    AccessioniPrimary (citable) accession number: P22450
    Secondary accession number(s): Q5V1T3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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