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P20276

- RL2_HALMA

UniProt

P20276 - RL2_HALMA

Protein

50S ribosomal protein L2

Gene

rpl2

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 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome By similarity.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-1464-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L2
    Alternative name(s):
    Hl4
    Hmal2
    Gene namesi
    Name:rpl2
    Ordered Locus Names:rrnAC1608
    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi200 – 2001H → A or G: No incorporation into translating E.coli polysomes; ribosomes assemble normally. Significantly reduced translational activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 24023950S ribosomal protein L2PRO_0000129712Add
    BLAST

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome By similarity. Interacts weakly with protein L37Ae.By similarity2 Publications

    Protein-protein interaction databases

    STRINGi272569.rrnAC1608.

    Structurei

    Secondary structure

    1
    240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 105
    Helixi15 – 173
    Helixi21 – 233
    Beta strandi35 – 373
    Beta strandi40 – 489
    Turni50 – 523
    Beta strandi53 – 619
    Turni62 – 643
    Beta strandi66 – 694
    Beta strandi72 – 743
    Beta strandi76 – 783
    Beta strandi80 – 845
    Beta strandi94 – 963
    Helixi97 – 993
    Beta strandi105 – 1095
    Beta strandi127 – 1315
    Beta strandi137 – 1404
    Turni142 – 1443
    Beta strandi146 – 1494
    Beta strandi154 – 1585
    Turni161 – 1677
    Helixi173 – 1808
    Turni181 – 1844
    Helixi192 – 1943
    Helixi197 – 1993
    Beta strandi205 – 2073
    Beta strandi214 – 2163
    Turni222 – 2243
    Beta strandi227 – 2293

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C04X-ray5.00A46-145[»]
    1FFKX-ray2.40A2-240[»]
    1JJ2X-ray2.40A2-240[»]
    1K73X-ray3.01C2-240[»]
    1K8AX-ray3.00C2-240[»]
    1K9MX-ray3.00C2-240[»]
    1KC8X-ray3.01C2-240[»]
    1KD1X-ray3.00C2-240[»]
    1KQSX-ray3.10A2-240[»]
    1M1KX-ray3.20C2-240[»]
    1M90X-ray2.80C2-240[»]
    1N8RX-ray3.00C2-240[»]
    1NJIX-ray3.00C2-240[»]
    1Q7YX-ray3.20C2-240[»]
    1Q81X-ray2.95C2-240[»]
    1Q82X-ray2.98C2-240[»]
    1Q86X-ray3.00C2-240[»]
    1QVFX-ray3.10A2-240[»]
    1QVGX-ray2.90A2-240[»]
    1S72X-ray2.40A1-240[»]
    1VQ4X-ray2.70A1-240[»]
    1VQ5X-ray2.60A1-240[»]
    1VQ6X-ray2.70A1-240[»]
    1VQ7X-ray2.50A1-240[»]
    1VQ8X-ray2.20A1-240[»]
    1VQ9X-ray2.40A1-240[»]
    1VQKX-ray2.30A1-240[»]
    1VQLX-ray2.30A1-240[»]
    1VQMX-ray2.30A1-240[»]
    1VQNX-ray2.40A1-240[»]
    1VQOX-ray2.20A1-240[»]
    1VQPX-ray2.25A1-240[»]
    1W2BX-ray3.50A2-240[»]
    1YHQX-ray2.40A1-240[»]
    1YI2X-ray2.65A1-240[»]
    1YIJX-ray2.60A1-240[»]
    1YITX-ray2.80A1-240[»]
    1YJ9X-ray2.90A1-240[»]
    1YJNX-ray3.00A1-240[»]
    1YJWX-ray2.90A1-240[»]
    2OTJX-ray2.90A1-240[»]
    2OTLX-ray2.70A2-240[»]
    2QA4X-ray3.00A1-240[»]
    2QEXX-ray2.90A1-240[»]
    3CC2X-ray2.40A1-240[»]
    3CC4X-ray2.70A1-240[»]
    3CC7X-ray2.70A1-240[»]
    3CCEX-ray2.75A1-240[»]
    3CCJX-ray2.70A1-240[»]
    3CCLX-ray2.90A1-240[»]
    3CCMX-ray2.55A1-240[»]
    3CCQX-ray2.90A1-240[»]
    3CCRX-ray3.00A1-240[»]
    3CCSX-ray2.95A1-240[»]
    3CCUX-ray2.80A1-240[»]
    3CCVX-ray2.90A1-240[»]
    3CD6X-ray2.75A1-240[»]
    3CMAX-ray2.80A1-240[»]
    3CMEX-ray2.95A1-240[»]
    3CPWX-ray2.70A1-240[»]
    3CXCX-ray3.00A2-240[»]
    3G4SX-ray3.20A2-238[»]
    3G6EX-ray2.70A2-238[»]
    3G71X-ray2.85A2-238[»]
    3I55X-ray3.11A1-240[»]
    3I56X-ray2.90A1-240[»]
    3OW2X-ray2.70A2-238[»]
    4ADXelectron microscopy6.60A1-240[»]
    4HUBX-ray2.40A1-240[»]
    ProteinModelPortaliP20276.
    SMRiP20276. Positions 14-238.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20276.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L2P family.Curated

    Phylogenomic databases

    eggNOGiCOG0090.
    HOGENOMiHOG000232983.
    KOiK02886.
    OMAiNCTISPL.

    Family and domain databases

    Gene3Di2.30.30.30. 1 hit.
    2.40.50.140. 1 hit.
    4.10.950.10. 1 hit.
    HAMAPiMF_01320_A. Ribosomal_L2_A.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR022666. Rbsml_prot_L2_RNA-bd_dom.
    IPR014722. Rib_L2_dom2.
    IPR002171. Ribosomal_L2.
    IPR023672. Ribosomal_L2_arc.
    IPR022669. Ribosomal_L2_C.
    IPR022671. Ribosomal_L2_CS.
    IPR014726. Ribosomal_L2_dom3.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view]
    PANTHERiPTHR13691. PTHR13691. 1 hit.
    PfamiPF00181. Ribosomal_L2. 1 hit.
    PF03947. Ribosomal_L2_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
    SUPFAMiSSF50104. SSF50104. 1 hit.
    SSF50249. SSF50249. 1 hit.
    PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P20276-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRRIQGQRR GRGTSTFRAP SHRYKADLEH RKVEDGDVIA GTVVDIEHDP    50
    ARSAPVAAVE FEDGDRRLIL APEGVGVGDE LQVGVSAEIA PGNTLPLAEI 100
    PEGVPVCNVE SSPGDGGKFA RASGVNAQLL THDRNVAVVK LPSGEMKRLD 150
    PQCRATIGVV AGGGRTDKPF VKAGNKHHKM KARGTKWPNV RGVAMNAVDH 200
    PFGGGGRQHP GKPKSISRNA PPGRKVGDIA SKRTGRGGNE 240
    Length:240
    Mass (Da):25,309
    Last modified:January 23, 2007 - v4
    Checksum:i986CA69D432C7F74
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861S → D in AAA86862. (PubMed:2406244)Curated
    Sequence conflicti161 – 1611A → G in AAA86862. (PubMed:2406244)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05222 Genomic DNA. Translation: AAA86862.1.
    AY596297 Genomic DNA. Translation: AAV46525.1.
    PIRiF35063. R5HS2L.
    RefSeqiYP_136231.1. NC_006396.1.

    Genome annotation databases

    EnsemblBacteriaiAAV46525; AAV46525; rrnAC1608.
    GeneIDi3128427.
    KEGGihma:rrnAC1608.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05222 Genomic DNA. Translation: AAA86862.1 .
    AY596297 Genomic DNA. Translation: AAV46525.1 .
    PIRi F35063. R5HS2L.
    RefSeqi YP_136231.1. 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 A 46-145 [» ]
    1FFK X-ray 2.40 A 2-240 [» ]
    1JJ2 X-ray 2.40 A 2-240 [» ]
    1K73 X-ray 3.01 C 2-240 [» ]
    1K8A X-ray 3.00 C 2-240 [» ]
    1K9M X-ray 3.00 C 2-240 [» ]
    1KC8 X-ray 3.01 C 2-240 [» ]
    1KD1 X-ray 3.00 C 2-240 [» ]
    1KQS X-ray 3.10 A 2-240 [» ]
    1M1K X-ray 3.20 C 2-240 [» ]
    1M90 X-ray 2.80 C 2-240 [» ]
    1N8R X-ray 3.00 C 2-240 [» ]
    1NJI X-ray 3.00 C 2-240 [» ]
    1Q7Y X-ray 3.20 C 2-240 [» ]
    1Q81 X-ray 2.95 C 2-240 [» ]
    1Q82 X-ray 2.98 C 2-240 [» ]
    1Q86 X-ray 3.00 C 2-240 [» ]
    1QVF X-ray 3.10 A 2-240 [» ]
    1QVG X-ray 2.90 A 2-240 [» ]
    1S72 X-ray 2.40 A 1-240 [» ]
    1VQ4 X-ray 2.70 A 1-240 [» ]
    1VQ5 X-ray 2.60 A 1-240 [» ]
    1VQ6 X-ray 2.70 A 1-240 [» ]
    1VQ7 X-ray 2.50 A 1-240 [» ]
    1VQ8 X-ray 2.20 A 1-240 [» ]
    1VQ9 X-ray 2.40 A 1-240 [» ]
    1VQK X-ray 2.30 A 1-240 [» ]
    1VQL X-ray 2.30 A 1-240 [» ]
    1VQM X-ray 2.30 A 1-240 [» ]
    1VQN X-ray 2.40 A 1-240 [» ]
    1VQO X-ray 2.20 A 1-240 [» ]
    1VQP X-ray 2.25 A 1-240 [» ]
    1W2B X-ray 3.50 A 2-240 [» ]
    1YHQ X-ray 2.40 A 1-240 [» ]
    1YI2 X-ray 2.65 A 1-240 [» ]
    1YIJ X-ray 2.60 A 1-240 [» ]
    1YIT X-ray 2.80 A 1-240 [» ]
    1YJ9 X-ray 2.90 A 1-240 [» ]
    1YJN X-ray 3.00 A 1-240 [» ]
    1YJW X-ray 2.90 A 1-240 [» ]
    2OTJ X-ray 2.90 A 1-240 [» ]
    2OTL X-ray 2.70 A 2-240 [» ]
    2QA4 X-ray 3.00 A 1-240 [» ]
    2QEX X-ray 2.90 A 1-240 [» ]
    3CC2 X-ray 2.40 A 1-240 [» ]
    3CC4 X-ray 2.70 A 1-240 [» ]
    3CC7 X-ray 2.70 A 1-240 [» ]
    3CCE X-ray 2.75 A 1-240 [» ]
    3CCJ X-ray 2.70 A 1-240 [» ]
    3CCL X-ray 2.90 A 1-240 [» ]
    3CCM X-ray 2.55 A 1-240 [» ]
    3CCQ X-ray 2.90 A 1-240 [» ]
    3CCR X-ray 3.00 A 1-240 [» ]
    3CCS X-ray 2.95 A 1-240 [» ]
    3CCU X-ray 2.80 A 1-240 [» ]
    3CCV X-ray 2.90 A 1-240 [» ]
    3CD6 X-ray 2.75 A 1-240 [» ]
    3CMA X-ray 2.80 A 1-240 [» ]
    3CME X-ray 2.95 A 1-240 [» ]
    3CPW X-ray 2.70 A 1-240 [» ]
    3CXC X-ray 3.00 A 2-240 [» ]
    3G4S X-ray 3.20 A 2-238 [» ]
    3G6E X-ray 2.70 A 2-238 [» ]
    3G71 X-ray 2.85 A 2-238 [» ]
    3I55 X-ray 3.11 A 1-240 [» ]
    3I56 X-ray 2.90 A 1-240 [» ]
    3OW2 X-ray 2.70 A 2-238 [» ]
    4ADX electron microscopy 6.60 A 1-240 [» ]
    4HUB X-ray 2.40 A 1-240 [» ]
    ProteinModelPortali P20276.
    SMRi P20276. Positions 14-238.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272569.rrnAC1608.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAV46525 ; AAV46525 ; rrnAC1608 .
    GeneIDi 3128427.
    KEGGi hma:rrnAC1608.

    Phylogenomic databases

    eggNOGi COG0090.
    HOGENOMi HOG000232983.
    KOi K02886.
    OMAi NCTISPL.

    Enzyme and pathway databases

    BioCyci HMAR272569:GJDH-1464-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P20276.

    Family and domain databases

    Gene3Di 2.30.30.30. 1 hit.
    2.40.50.140. 1 hit.
    4.10.950.10. 1 hit.
    HAMAPi MF_01320_A. Ribosomal_L2_A.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR022666. Rbsml_prot_L2_RNA-bd_dom.
    IPR014722. Rib_L2_dom2.
    IPR002171. Ribosomal_L2.
    IPR023672. Ribosomal_L2_arc.
    IPR022669. Ribosomal_L2_C.
    IPR022671. Ribosomal_L2_CS.
    IPR014726. Ribosomal_L2_dom3.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view ]
    PANTHERi PTHR13691. PTHR13691. 1 hit.
    Pfami PF00181. Ribosomal_L2. 1 hit.
    PF03947. Ribosomal_L2_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002158. Ribosomal_L2. 1 hit.
    SUPFAMi SSF50104. SSF50104. 1 hit.
    SSF50249. SSF50249. 1 hit.
    PROSITEi PS00467. RIBOSOMAL_L2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Organization and nucleotide sequence of a gene cluster coding for eight ribosomal proteins in the archaebacterium Halobacterium marismortui."
      Arndt E., Kroemer W., Hatakeyama T.
      J. Biol. Chem. 265:3034-3039(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809.
    3. "Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies."
      Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.
      Biochem. J. 331:423-430(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN REPLACEMENT STUDIES IN E.COLI, MUTAGENESIS.
    4. "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.
    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 nameiRL2_HALMA
    AccessioniPrimary (citable) accession number: P20276
    Secondary accession number(s): Q5V1S7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 116 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein can be partially incorporated into E.coli polysomes in vivo, indicating it can replace the endogenous protein.

    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