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P02413

- RL15_ECOLI

UniProt

P02413 - RL15_ECOLI

Protein

50S ribosomal protein L15

Gene

rplO

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. rRNA binding Source: UniProtKB-HAMAP
    3. 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

    BioCyciEcoCyc:EG10876-MONOMER.
    ECOL316407:JW3263-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L15
    Gene namesi
    Name:rplO
    Ordered Locus Names:b3301, JW3263
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10876. rplO.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14414450S ribosomal protein L15PRO_0000104721Add
    BLAST

    Proteomic databases

    PaxDbiP02413.
    PRIDEiP02413.

    Expressioni

    Gene expression databases

    GenevestigatoriP02413.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Contacts the 5S rRNA.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rlmNP369793EBI-543017,EBI-559071

    Protein-protein interaction databases

    DIPiDIP-10752N.
    IntActiP02413. 78 interactions.
    MINTiMINT-1260355.
    STRINGi511145.b3301.

    Structurei

    Secondary structure

    1
    144
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni3 – 53
    Beta strandi10 – 134
    Helixi22 – 254
    Turni29 – 324
    Beta strandi35 – 373
    Turni38 – 403
    Beta strandi41 – 433
    Beta strandi47 – 493
    Beta strandi52 – 543
    Helixi57 – 604
    Helixi71 – 733
    Beta strandi74 – 763
    Turni79 – 824
    Helixi83 – 853
    Beta strandi86 – 916
    Turni92 – 998
    Beta strandi103 – 1053
    Beta strandi107 – 1093
    Beta strandi121 – 1244
    Helixi129 – 1368
    Turni137 – 1393
    Beta strandi141 – 1433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ML5electron microscopy14.00o2-144[»]
    1P85electron microscopy12.30J1-144[»]
    1P86electron microscopy11.50J1-144[»]
    1VS6X-ray3.46L1-144[»]
    1VS8X-ray3.46L1-144[»]
    1VT2X-ray3.30L1-144[»]
    2AW4X-ray3.46L1-144[»]
    2AWBX-ray3.46L1-144[»]
    2GYAelectron microscopy15.00J4-143[»]
    2GYCelectron microscopy15.00J4-143[»]
    2I2TX-ray3.22L1-144[»]
    2I2VX-ray3.22L1-144[»]
    2J28electron microscopy8.00L1-144[»]
    2QAMX-ray3.21L1-144[»]
    2QAOX-ray3.21L1-144[»]
    2QBAX-ray3.54L1-144[»]
    2QBCX-ray3.54L1-144[»]
    2QBEX-ray3.30L1-144[»]
    2QBGX-ray3.30L1-144[»]
    2QBIX-ray4.00L1-144[»]
    2QBKX-ray4.00L1-144[»]
    2QOVX-ray3.93L1-144[»]
    2QOXX-ray3.93L1-144[»]
    2QOZX-ray3.50L1-144[»]
    2QP1X-ray3.50L1-144[»]
    2RDOelectron microscopy9.10L1-144[»]
    2VHMX-ray3.74L1-144[»]
    2VHNX-ray3.74L1-144[»]
    2WWQelectron microscopy5.80L2-144[»]
    2Z4LX-ray4.45L1-144[»]
    2Z4NX-ray4.45L1-144[»]
    3BBXelectron microscopy10.00L1-144[»]
    3DF2X-ray3.50L1-144[»]
    3DF4X-ray3.50L1-144[»]
    3E1Belectron microscopy-E1-144[»]
    3E1Delectron microscopy-E1-144[»]
    3FIKelectron microscopy6.70L2-144[»]
    3I1NX-ray3.19L1-144[»]
    3I1PX-ray3.19L1-144[»]
    3I1RX-ray3.81L1-144[»]
    3I1TX-ray3.81L1-144[»]
    3I20X-ray3.71L1-144[»]
    3I22X-ray3.71L1-144[»]
    3IY9electron microscopy14.10L2-144[»]
    3IZTelectron microscopy-M1-144[»]
    3IZUelectron microscopy-M1-144[»]
    3J01electron microscopy-L1-144[»]
    3J0Telectron microscopy12.10N1-144[»]
    3J0Welectron microscopy14.70N1-144[»]
    3J0Yelectron microscopy13.50N1-144[»]
    3J11electron microscopy13.10N1-144[»]
    3J12electron microscopy11.50N1-144[»]
    3J14electron microscopy11.50N1-144[»]
    3J19electron microscopy8.30L2-144[»]
    3J37electron microscopy9.80P1-144[»]
    3J4Xelectron microscopy12.00L1-144[»]
    3J50electron microscopy20.00L1-144[»]
    3J51electron microscopy17.00L1-144[»]
    3J52electron microscopy12.00L1-144[»]
    3J54electron microscopy13.00L1-144[»]
    3J56electron microscopy15.00L1-144[»]
    3J58electron microscopy17.00L1-144[»]
    3J5Aelectron microscopy12.00L1-144[»]
    3J5Celectron microscopy17.00L1-144[»]
    3J5Eelectron microscopy17.00L1-144[»]
    3J5Gelectron microscopy20.00L1-144[»]
    3J5Ielectron microscopy15.00L1-144[»]
    3J5Kelectron microscopy9.00L1-144[»]
    3J5Lelectron microscopy6.60L2-144[»]
    3J5Oelectron microscopy6.80L1-144[»]
    3J5Uelectron microscopy7.60N1-144[»]
    3J5Welectron microscopy7.60O1-144[»]
    3KCRelectron microscopy-L1-144[»]
    3OASX-ray3.25L2-144[»]
    3OATX-ray3.25L2-144[»]
    3OFCX-ray3.19L2-144[»]
    3OFDX-ray3.19L2-144[»]
    3OFQX-ray3.10L2-144[»]
    3OFRX-ray3.10L2-144[»]
    3OFZX-ray3.29L2-144[»]
    3OG0X-ray3.29L2-144[»]
    3ORBX-ray3.30L1-144[»]
    3R8SX-ray3.00L2-144[»]
    3R8TX-ray3.00L2-144[»]
    3SGFX-ray3.20P1-144[»]
    3UOSX-ray3.70P1-144[»]
    4CSUelectron microscopy5.50L2-144[»]
    4GARX-ray3.30L1-144[»]
    4GAUX-ray3.30L1-144[»]
    4KIXX-ray2.90L1-144[»]
    4KIZX-ray2.90L1-144[»]
    4KJ1X-ray2.90L1-144[»]
    4KJ3X-ray2.90L1-144[»]
    4KJ5X-ray2.90L1-144[»]
    4KJ7X-ray2.90L1-144[»]
    4KJ9X-ray2.90L1-144[»]
    4KJBX-ray2.90L1-144[»]
    ProteinModelPortaliP02413.
    SMRiP02413. Positions 2-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02413.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L15P family.Curated

    Phylogenomic databases

    eggNOGiCOG0200.
    HOGENOMiHOG000231262.
    KOiK02876.
    OMAiRGHKGLK.
    OrthoDBiEOG6CGCM5.
    PhylomeDBiP02413.

    Family and domain databases

    HAMAPiMF_01341. Ribosomal_L15.
    InterProiIPR005749. Ribosomal_L15_bac-type.
    IPR001196. Ribosomal_L15_CS.
    IPR021131. Ribosomal_L18e/L15P.
    [Graphical view]
    PANTHERiPTHR12934. PTHR12934. 1 hit.
    PfamiPF00828. Ribosomal_L18e. 1 hit.
    [Graphical view]
    SUPFAMiSSF52080. SSF52080. 1 hit.
    TIGRFAMsiTIGR01071. rplO_bact. 1 hit.
    PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P02413-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLNTLSPAE GSKKAGKRLG RGIGSGLGKT GGRGHKGQKS RSGGGVRRGF    50
    EGGQMPLYRR LPKFGFTSRK AAITAEIRLS DLAKVEGGVV DLNTLKAANI 100
    IGIQIEFAKV ILAGEVTTPV TVRGLRVTKG ARAAIEAAGG KIEE 144
    Length:144
    Mass (Da):14,980
    Last modified:July 21, 1986 - v1
    Checksum:i53D14CD948815FD9
    GO

    Mass spectrometryi

    Molecular mass is 14980.1 Da from positions 1 - 144. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25724.1.
    U18997 Genomic DNA. Translation: AAA58098.1.
    U00096 Genomic DNA. Translation: AAC76326.1.
    AP009048 Genomic DNA. Translation: BAE77990.1.
    PIRiA02794. R5EC15.
    RefSeqiNP_417760.1. NC_000913.3.
    YP_492131.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76326; AAC76326; b3301.
    BAE77990; BAE77990; BAE77990.
    GeneIDi12934400.
    947798.
    KEGGiecj:Y75_p3875.
    eco:b3301.
    PATRICi32122034. VBIEscCol129921_3394.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01563 Genomic DNA. Translation: CAA25724.1 .
    U18997 Genomic DNA. Translation: AAA58098.1 .
    U00096 Genomic DNA. Translation: AAC76326.1 .
    AP009048 Genomic DNA. Translation: BAE77990.1 .
    PIRi A02794. R5EC15.
    RefSeqi NP_417760.1. NC_000913.3.
    YP_492131.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ML5 electron microscopy 14.00 o 2-144 [» ]
    1P85 electron microscopy 12.30 J 1-144 [» ]
    1P86 electron microscopy 11.50 J 1-144 [» ]
    1VS6 X-ray 3.46 L 1-144 [» ]
    1VS8 X-ray 3.46 L 1-144 [» ]
    1VT2 X-ray 3.30 L 1-144 [» ]
    2AW4 X-ray 3.46 L 1-144 [» ]
    2AWB X-ray 3.46 L 1-144 [» ]
    2GYA electron microscopy 15.00 J 4-143 [» ]
    2GYC electron microscopy 15.00 J 4-143 [» ]
    2I2T X-ray 3.22 L 1-144 [» ]
    2I2V X-ray 3.22 L 1-144 [» ]
    2J28 electron microscopy 8.00 L 1-144 [» ]
    2QAM X-ray 3.21 L 1-144 [» ]
    2QAO X-ray 3.21 L 1-144 [» ]
    2QBA X-ray 3.54 L 1-144 [» ]
    2QBC X-ray 3.54 L 1-144 [» ]
    2QBE X-ray 3.30 L 1-144 [» ]
    2QBG X-ray 3.30 L 1-144 [» ]
    2QBI X-ray 4.00 L 1-144 [» ]
    2QBK X-ray 4.00 L 1-144 [» ]
    2QOV X-ray 3.93 L 1-144 [» ]
    2QOX X-ray 3.93 L 1-144 [» ]
    2QOZ X-ray 3.50 L 1-144 [» ]
    2QP1 X-ray 3.50 L 1-144 [» ]
    2RDO electron microscopy 9.10 L 1-144 [» ]
    2VHM X-ray 3.74 L 1-144 [» ]
    2VHN X-ray 3.74 L 1-144 [» ]
    2WWQ electron microscopy 5.80 L 2-144 [» ]
    2Z4L X-ray 4.45 L 1-144 [» ]
    2Z4N X-ray 4.45 L 1-144 [» ]
    3BBX electron microscopy 10.00 L 1-144 [» ]
    3DF2 X-ray 3.50 L 1-144 [» ]
    3DF4 X-ray 3.50 L 1-144 [» ]
    3E1B electron microscopy - E 1-144 [» ]
    3E1D electron microscopy - E 1-144 [» ]
    3FIK electron microscopy 6.70 L 2-144 [» ]
    3I1N X-ray 3.19 L 1-144 [» ]
    3I1P X-ray 3.19 L 1-144 [» ]
    3I1R X-ray 3.81 L 1-144 [» ]
    3I1T X-ray 3.81 L 1-144 [» ]
    3I20 X-ray 3.71 L 1-144 [» ]
    3I22 X-ray 3.71 L 1-144 [» ]
    3IY9 electron microscopy 14.10 L 2-144 [» ]
    3IZT electron microscopy - M 1-144 [» ]
    3IZU electron microscopy - M 1-144 [» ]
    3J01 electron microscopy - L 1-144 [» ]
    3J0T electron microscopy 12.10 N 1-144 [» ]
    3J0W electron microscopy 14.70 N 1-144 [» ]
    3J0Y electron microscopy 13.50 N 1-144 [» ]
    3J11 electron microscopy 13.10 N 1-144 [» ]
    3J12 electron microscopy 11.50 N 1-144 [» ]
    3J14 electron microscopy 11.50 N 1-144 [» ]
    3J19 electron microscopy 8.30 L 2-144 [» ]
    3J37 electron microscopy 9.80 P 1-144 [» ]
    3J4X electron microscopy 12.00 L 1-144 [» ]
    3J50 electron microscopy 20.00 L 1-144 [» ]
    3J51 electron microscopy 17.00 L 1-144 [» ]
    3J52 electron microscopy 12.00 L 1-144 [» ]
    3J54 electron microscopy 13.00 L 1-144 [» ]
    3J56 electron microscopy 15.00 L 1-144 [» ]
    3J58 electron microscopy 17.00 L 1-144 [» ]
    3J5A electron microscopy 12.00 L 1-144 [» ]
    3J5C electron microscopy 17.00 L 1-144 [» ]
    3J5E electron microscopy 17.00 L 1-144 [» ]
    3J5G electron microscopy 20.00 L 1-144 [» ]
    3J5I electron microscopy 15.00 L 1-144 [» ]
    3J5K electron microscopy 9.00 L 1-144 [» ]
    3J5L electron microscopy 6.60 L 2-144 [» ]
    3J5O electron microscopy 6.80 L 1-144 [» ]
    3J5U electron microscopy 7.60 N 1-144 [» ]
    3J5W electron microscopy 7.60 O 1-144 [» ]
    3KCR electron microscopy - L 1-144 [» ]
    3OAS X-ray 3.25 L 2-144 [» ]
    3OAT X-ray 3.25 L 2-144 [» ]
    3OFC X-ray 3.19 L 2-144 [» ]
    3OFD X-ray 3.19 L 2-144 [» ]
    3OFQ X-ray 3.10 L 2-144 [» ]
    3OFR X-ray 3.10 L 2-144 [» ]
    3OFZ X-ray 3.29 L 2-144 [» ]
    3OG0 X-ray 3.29 L 2-144 [» ]
    3ORB X-ray 3.30 L 1-144 [» ]
    3R8S X-ray 3.00 L 2-144 [» ]
    3R8T X-ray 3.00 L 2-144 [» ]
    3SGF X-ray 3.20 P 1-144 [» ]
    3UOS X-ray 3.70 P 1-144 [» ]
    4CSU electron microscopy 5.50 L 2-144 [» ]
    4GAR X-ray 3.30 L 1-144 [» ]
    4GAU X-ray 3.30 L 1-144 [» ]
    4KIX X-ray 2.90 L 1-144 [» ]
    4KIZ X-ray 2.90 L 1-144 [» ]
    4KJ1 X-ray 2.90 L 1-144 [» ]
    4KJ3 X-ray 2.90 L 1-144 [» ]
    4KJ5 X-ray 2.90 L 1-144 [» ]
    4KJ7 X-ray 2.90 L 1-144 [» ]
    4KJ9 X-ray 2.90 L 1-144 [» ]
    4KJB X-ray 2.90 L 1-144 [» ]
    ProteinModelPortali P02413.
    SMRi P02413. Positions 2-144.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10752N.
    IntActi P02413. 78 interactions.
    MINTi MINT-1260355.
    STRINGi 511145.b3301.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P02413.
    PRIDEi P02413.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76326 ; AAC76326 ; b3301 .
    BAE77990 ; BAE77990 ; BAE77990 .
    GeneIDi 12934400.
    947798.
    KEGGi ecj:Y75_p3875.
    eco:b3301.
    PATRICi 32122034. VBIEscCol129921_3394.

    Organism-specific databases

    EchoBASEi EB0869.
    EcoGenei EG10876. rplO.

    Phylogenomic databases

    eggNOGi COG0200.
    HOGENOMi HOG000231262.
    KOi K02876.
    OMAi RGHKGLK.
    OrthoDBi EOG6CGCM5.
    PhylomeDBi P02413.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10876-MONOMER.
    ECOL316407:JW3263-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P02413.
    PROi P02413.

    Gene expression databases

    Genevestigatori P02413.

    Family and domain databases

    HAMAPi MF_01341. Ribosomal_L15.
    InterProi IPR005749. Ribosomal_L15_bac-type.
    IPR001196. Ribosomal_L15_CS.
    IPR021131. Ribosomal_L18e/L15P.
    [Graphical view ]
    PANTHERi PTHR12934. PTHR12934. 1 hit.
    Pfami PF00828. Ribosomal_L18e. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52080. SSF52080. 1 hit.
    TIGRFAMsi TIGR01071. rplO_bact. 1 hit.
    PROSITEi PS00475. RIBOSOMAL_L15. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of protein L15 located at the peptidyltransferase center of Escherichia coli ribosomes."
      Giorginis S., Chen R.
      FEBS Lett. 84:347-350(1977) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: K.
    2. "The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene."
      Cerretti D.P., Dean D., Davis G.R., Bedwell D.M., Nomura M.
      Nucleic Acids Res. 11:2599-2616(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
      Herold M., Nierhaus K.H.
      J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
      Strain: K12.
    6. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
      Arnold R.J., Reilly J.P.
      Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
    7. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
      Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
      Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS).
      Strain: MRE-600.
    8. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL15_ECOLI
    AccessioniPrimary (citable) accession number: P02413
    Secondary accession number(s): Q2M6W6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 148 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, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Ribosomal proteins
      Ribosomal proteins families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3