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P14123

- RL18_HALMA

UniProt

P14123 - RL18_HALMA

Protein

50S ribosomal protein L18

Gene

rpl18

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 117 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, where it forms part of the central protuberance and stabilizes the orientation of adjacent RNA domains.

    GO - Molecular functioni

    1. 5S rRNA binding Source: InterPro
    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-1449-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L18
    Alternative name(s):
    Hl12
    Hmal18
    Gene namesi
    Name:rpl18
    Ordered Locus Names:rrnAC1593
    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 – 11Removed1 Publication
    Chaini2 – 18718650S ribosomal protein L18PRO_0000131400Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Interacts with proteins L5 and L21e, and attaches the 5S rRNA to the 23S rRNA. Has been cross-linked to L21e.2 Publications

    Protein-protein interaction databases

    STRINGi272569.rrnAC1593.

    Structurei

    Secondary structure

    1
    187
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi12 – 154
    Helixi21 – 288
    Beta strandi34 – 396
    Beta strandi44 – 507
    Beta strandi53 – 553
    Beta strandi57 – 648
    Helixi65 – 706
    Beta strandi76 – 783
    Helixi79 – 9517
    Beta strandi102 – 1043
    Helixi115 – 12511
    Helixi134 – 1363
    Helixi140 – 1445
    Helixi146 – 1538
    Beta strandi159 – 1624
    Helixi166 – 1683
    Helixi170 – 18112
    Beta strandi182 – 1854

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FFKX-ray2.40K2-186[»]
    1JJ2X-ray2.40M2-187[»]
    1K73X-ray3.01O2-187[»]
    1K8AX-ray3.00O2-187[»]
    1K9MX-ray3.00O2-187[»]
    1KC8X-ray3.01O2-187[»]
    1KD1X-ray3.00O2-187[»]
    1KQSX-ray3.10M2-187[»]
    1M1KX-ray3.20O2-187[»]
    1M90X-ray2.80O2-187[»]
    1N8RX-ray3.00O2-187[»]
    1NJIX-ray3.00O2-187[»]
    1Q7YX-ray3.20O2-187[»]
    1Q81X-ray2.95O2-187[»]
    1Q82X-ray2.98O2-187[»]
    1Q86X-ray3.00O2-187[»]
    1QVFX-ray3.10M2-187[»]
    1QVGX-ray2.90M2-187[»]
    1S72X-ray2.40N1-187[»]
    1VQ4X-ray2.70N1-187[»]
    1VQ5X-ray2.60N1-187[»]
    1VQ6X-ray2.70N1-187[»]
    1VQ7X-ray2.50N1-187[»]
    1VQ8X-ray2.20N1-187[»]
    1VQ9X-ray2.40N1-187[»]
    1VQKX-ray2.30N1-187[»]
    1VQLX-ray2.30N1-187[»]
    1VQMX-ray2.30N1-187[»]
    1VQNX-ray2.40N1-187[»]
    1VQOX-ray2.20N1-187[»]
    1VQPX-ray2.25N1-187[»]
    1W2BX-ray3.50M2-187[»]
    1YHQX-ray2.40N1-187[»]
    1YI2X-ray2.65N1-187[»]
    1YIJX-ray2.60N1-187[»]
    1YITX-ray2.80N1-187[»]
    1YJ9X-ray2.90N1-187[»]
    1YJNX-ray3.00N1-187[»]
    1YJWX-ray2.90N1-187[»]
    2B66X-ray5.90S2-187[»]
    2B9NX-ray6.76S2-187[»]
    2B9PX-ray6.46S2-187[»]
    2OTJX-ray2.90N1-187[»]
    2OTLX-ray2.70N1-187[»]
    2QA4X-ray3.00N1-187[»]
    2QEXX-ray2.90N1-187[»]
    3CC2X-ray2.40N1-187[»]
    3CC4X-ray2.70N1-187[»]
    3CC7X-ray2.70N1-187[»]
    3CCEX-ray2.75N1-187[»]
    3CCJX-ray2.70N1-187[»]
    3CCLX-ray2.90N1-187[»]
    3CCMX-ray2.55N1-187[»]
    3CCQX-ray2.90N1-187[»]
    3CCRX-ray3.00N1-187[»]
    3CCSX-ray2.95N1-187[»]
    3CCUX-ray2.80N1-187[»]
    3CCVX-ray2.90N1-187[»]
    3CD6X-ray2.75N1-187[»]
    3CMAX-ray2.80N1-187[»]
    3CMEX-ray2.95N1-187[»]
    3CPWX-ray2.70M1-187[»]
    3CXCX-ray3.00M2-187[»]
    3G4SX-ray3.20N2-187[»]
    3G6EX-ray2.70N2-187[»]
    3G71X-ray2.85N2-187[»]
    3I55X-ray3.11N1-187[»]
    3I56X-ray2.90N1-187[»]
    3OW2X-ray2.70M2-187[»]
    4ADXelectron microscopy6.60N1-187[»]
    4HUBX-ray2.40N1-187[»]
    ProteinModelPortaliP14123.
    SMRiP14123. Positions 2-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14123.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L18P family.Curated

    Phylogenomic databases

    eggNOGiCOG0256.
    HOGENOMiHOG000105947.
    KOiK02881.
    OMAiEYGWEAP.

    Family and domain databases

    HAMAPiMF_01337_A. Ribosomal_L18_A.
    InterProiIPR005485. Rbsml_L5_euk/L18_arc.
    IPR005484. Ribosomal_L18/L5.
    [Graphical view]
    PANTHERiPTHR23410. PTHR23410. 1 hit.
    PfamiPF00861. Ribosomal_L18p. 1 hit.
    [Graphical view]
    PRINTSiPR00058. RIBOSOMALL5.

    Sequencei

    Sequence statusi: Complete.

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

    P14123-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATGPRYKVP MRRRREARTD YHQRLRLLKS GKPRLVARKS NKHVRAQLVT    50
    LGPNGDDTLA SAHSSDLAEY GWEAPTGNMP SAYLTGLLAG LRAQEAGVEE 100
    AVLDIGLNSP TPGSKVFAIQ EGAIDAGLDI PHNDDVLADW QRTRGAHIAE 150
    YDEQLEEPLY SGDFDAADLP EHFDELRETL LDGDIEL 187
    Length:187
    Mass (Da):20,614
    Last modified:January 23, 2007 - v3
    Checksum:i60E9AF3CB64E7CA5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181R → A AA sequence (PubMed:3196689)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58395 Genomic DNA. Translation: CAA41290.1.
    AY596297 Genomic DNA. Translation: AAV46511.1.
    PIRiS16541. R5HS18.
    RefSeqiWP_011223738.1. NC_006396.1.
    YP_136217.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46511; AAV46511; rrnAC1593.
    GeneIDi3127918.
    KEGGihma:rrnAC1593.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58395 Genomic DNA. Translation: CAA41290.1 .
    AY596297 Genomic DNA. Translation: AAV46511.1 .
    PIRi S16541. R5HS18.
    RefSeqi WP_011223738.1. NC_006396.1.
    YP_136217.1. 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 K 2-186 [» ]
    1JJ2 X-ray 2.40 M 2-187 [» ]
    1K73 X-ray 3.01 O 2-187 [» ]
    1K8A X-ray 3.00 O 2-187 [» ]
    1K9M X-ray 3.00 O 2-187 [» ]
    1KC8 X-ray 3.01 O 2-187 [» ]
    1KD1 X-ray 3.00 O 2-187 [» ]
    1KQS X-ray 3.10 M 2-187 [» ]
    1M1K X-ray 3.20 O 2-187 [» ]
    1M90 X-ray 2.80 O 2-187 [» ]
    1N8R X-ray 3.00 O 2-187 [» ]
    1NJI X-ray 3.00 O 2-187 [» ]
    1Q7Y X-ray 3.20 O 2-187 [» ]
    1Q81 X-ray 2.95 O 2-187 [» ]
    1Q82 X-ray 2.98 O 2-187 [» ]
    1Q86 X-ray 3.00 O 2-187 [» ]
    1QVF X-ray 3.10 M 2-187 [» ]
    1QVG X-ray 2.90 M 2-187 [» ]
    1S72 X-ray 2.40 N 1-187 [» ]
    1VQ4 X-ray 2.70 N 1-187 [» ]
    1VQ5 X-ray 2.60 N 1-187 [» ]
    1VQ6 X-ray 2.70 N 1-187 [» ]
    1VQ7 X-ray 2.50 N 1-187 [» ]
    1VQ8 X-ray 2.20 N 1-187 [» ]
    1VQ9 X-ray 2.40 N 1-187 [» ]
    1VQK X-ray 2.30 N 1-187 [» ]
    1VQL X-ray 2.30 N 1-187 [» ]
    1VQM X-ray 2.30 N 1-187 [» ]
    1VQN X-ray 2.40 N 1-187 [» ]
    1VQO X-ray 2.20 N 1-187 [» ]
    1VQP X-ray 2.25 N 1-187 [» ]
    1W2B X-ray 3.50 M 2-187 [» ]
    1YHQ X-ray 2.40 N 1-187 [» ]
    1YI2 X-ray 2.65 N 1-187 [» ]
    1YIJ X-ray 2.60 N 1-187 [» ]
    1YIT X-ray 2.80 N 1-187 [» ]
    1YJ9 X-ray 2.90 N 1-187 [» ]
    1YJN X-ray 3.00 N 1-187 [» ]
    1YJW X-ray 2.90 N 1-187 [» ]
    2B66 X-ray 5.90 S 2-187 [» ]
    2B9N X-ray 6.76 S 2-187 [» ]
    2B9P X-ray 6.46 S 2-187 [» ]
    2OTJ X-ray 2.90 N 1-187 [» ]
    2OTL X-ray 2.70 N 1-187 [» ]
    2QA4 X-ray 3.00 N 1-187 [» ]
    2QEX X-ray 2.90 N 1-187 [» ]
    3CC2 X-ray 2.40 N 1-187 [» ]
    3CC4 X-ray 2.70 N 1-187 [» ]
    3CC7 X-ray 2.70 N 1-187 [» ]
    3CCE X-ray 2.75 N 1-187 [» ]
    3CCJ X-ray 2.70 N 1-187 [» ]
    3CCL X-ray 2.90 N 1-187 [» ]
    3CCM X-ray 2.55 N 1-187 [» ]
    3CCQ X-ray 2.90 N 1-187 [» ]
    3CCR X-ray 3.00 N 1-187 [» ]
    3CCS X-ray 2.95 N 1-187 [» ]
    3CCU X-ray 2.80 N 1-187 [» ]
    3CCV X-ray 2.90 N 1-187 [» ]
    3CD6 X-ray 2.75 N 1-187 [» ]
    3CMA X-ray 2.80 N 1-187 [» ]
    3CME X-ray 2.95 N 1-187 [» ]
    3CPW X-ray 2.70 M 1-187 [» ]
    3CXC X-ray 3.00 M 2-187 [» ]
    3G4S X-ray 3.20 N 2-187 [» ]
    3G6E X-ray 2.70 N 2-187 [» ]
    3G71 X-ray 2.85 N 2-187 [» ]
    3I55 X-ray 3.11 N 1-187 [» ]
    3I56 X-ray 2.90 N 1-187 [» ]
    3OW2 X-ray 2.70 M 2-187 [» ]
    4ADX electron microscopy 6.60 N 1-187 [» ]
    4HUB X-ray 2.40 N 1-187 [» ]
    ProteinModelPortali P14123.
    SMRi P14123. Positions 2-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1593.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46511 ; AAV46511 ; rrnAC1593 .
    GeneIDi 3127918.
    KEGGi hma:rrnAC1593.

    Phylogenomic databases

    eggNOGi COG0256.
    HOGENOMi HOG000105947.
    KOi K02881.
    OMAi EYGWEAP.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1449-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P14123.

    Family and domain databases

    HAMAPi MF_01337_A. Ribosomal_L18_A.
    InterProi IPR005485. Rbsml_L5_euk/L18_arc.
    IPR005484. Ribosomal_L18/L5.
    [Graphical view ]
    PANTHERi PTHR23410. PTHR23410. 1 hit.
    Pfami PF00861. Ribosomal_L18p. 1 hit.
    [Graphical view ]
    PRINTSi PR00058. RIBOSOMALL5.
    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. "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 2-25.
    4. "Localization of proteins HL29 and HL31 from Haloarcula marismortui within the 50 S ribosomal subunit by chemical crosslinking."
      Bergmann U., Wittmann-Liebold B.
      J. Mol. Biol. 232:693-700(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO L21E.
    5. "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.
    6. "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.
    7. "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.
    8. "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.
    9. "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.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE 50S SUBUNIT.
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    11. "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.
    12. "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.
    13. "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 nameiRL18_HALMA
    AccessioniPrimary (citable) accession number: P14123
    Secondary accession number(s): Q5V1U1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 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