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P0AG44

- RL17_ECOLI

UniProt

P0AG44 - RL17_ECOLI

Protein

50S ribosomal protein L17

Gene

rplQ

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Requires L15 for assembly into the 50S subunit.

    GO - Molecular functioni

    1. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10878-MONOMER.
    ECOL316407:JW3256-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L17UniRule annotation
    Gene namesi
    Name:rplQUniRule annotation
    Ordered Locus Names:b3294, JW3256
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10878. rplQ.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12712750S ribosomal protein L17PRO_0000175524Add
    BLAST

    Proteomic databases

    PaxDbiP0AG44.
    PRIDEiP0AG44.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AG44.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Contacts protein L32.

    Protein-protein interaction databases

    DIPiDIP-35801N.
    IntActiP0AG44. 135 interactions.
    MINTiMINT-1251899.
    STRINGi511145.b3294.

    Structurei

    Secondary structure

    1
    127
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Helixi14 – 3118
    Beta strandi32 – 376
    Helixi38 – 5518
    Helixi60 – 689
    Helixi73 – 819
    Helixi83 – 864
    Turni87 – 893
    Beta strandi95 – 984
    Beta strandi99 – 1024
    Turni104 – 1063
    Beta strandi110 – 1156
    Turni116 – 1194

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P85electron microscopy12.30L1-127[»]
    1P86electron microscopy11.50L1-127[»]
    1VS6X-ray3.46N1-127[»]
    1VS8X-ray3.46N1-127[»]
    1VT2X-ray3.30N1-127[»]
    2AW4X-ray3.46N1-127[»]
    2AWBX-ray3.46N1-127[»]
    2GYAelectron microscopy15.00L3-116[»]
    2GYCelectron microscopy15.00L3-116[»]
    2I2TX-ray3.22N1-127[»]
    2I2VX-ray3.22N1-127[»]
    2J28electron microscopy8.00N1-127[»]
    2QAMX-ray3.21N1-127[»]
    2QAOX-ray3.21N1-127[»]
    2QBAX-ray3.54N1-127[»]
    2QBCX-ray3.54N1-127[»]
    2QBEX-ray3.30N1-127[»]
    2QBGX-ray3.30N1-127[»]
    2QBIX-ray4.00N1-127[»]
    2QBKX-ray4.00N1-127[»]
    2QOVX-ray3.93N1-127[»]
    2QOXX-ray3.93N1-127[»]
    2QOZX-ray3.50N1-127[»]
    2QP1X-ray3.50N1-127[»]
    2RDOelectron microscopy9.10N1-127[»]
    2WWQelectron microscopy5.80N1-120[»]
    2Z4LX-ray4.45N1-127[»]
    2Z4NX-ray4.45N1-127[»]
    3BBXelectron microscopy10.00N1-127[»]
    3E1Belectron microscopy-G1-127[»]
    3E1Delectron microscopy-G1-127[»]
    3FIKelectron microscopy6.70N1-120[»]
    3I1NX-ray3.19N1-127[»]
    3I1PX-ray3.19N1-127[»]
    3I1RX-ray3.81N1-127[»]
    3I1TX-ray3.81N1-127[»]
    3I20X-ray3.71N1-127[»]
    3I22X-ray3.71N1-127[»]
    3IZTelectron microscopy-O1-127[»]
    3IZUelectron microscopy-O1-127[»]
    3J01electron microscopy-N1-127[»]
    3J0Telectron microscopy12.10P1-127[»]
    3J0Welectron microscopy14.70P1-127[»]
    3J0Yelectron microscopy13.50P1-127[»]
    3J11electron microscopy13.10P1-127[»]
    3J12electron microscopy11.50P1-127[»]
    3J14electron microscopy11.50P1-127[»]
    3J19electron microscopy8.30N1-120[»]
    3J37electron microscopy9.80R1-127[»]
    3J4Xelectron microscopy12.00N1-120[»]
    3J50electron microscopy20.00N1-120[»]
    3J51electron microscopy17.00N1-120[»]
    3J52electron microscopy12.00N1-120[»]
    3J54electron microscopy13.00N1-120[»]
    3J56electron microscopy15.00N1-120[»]
    3J58electron microscopy17.00N1-120[»]
    3J5Aelectron microscopy12.00N1-120[»]
    3J5Celectron microscopy17.00N1-120[»]
    3J5Eelectron microscopy17.00N1-120[»]
    3J5Gelectron microscopy20.00N1-120[»]
    3J5Ielectron microscopy15.00N1-120[»]
    3J5Kelectron microscopy9.00N1-120[»]
    3J5Lelectron microscopy6.60N1-120[»]
    3J5Oelectron microscopy6.80N1-127[»]
    3J5Uelectron microscopy7.60P1-127[»]
    3J5Welectron microscopy7.60Q1-127[»]
    3KCRelectron microscopy-N1-127[»]
    3OASX-ray3.25N1-120[»]
    3OATX-ray3.25N1-120[»]
    3OFCX-ray3.19N1-120[»]
    3OFDX-ray3.19N1-120[»]
    3OFQX-ray3.10N1-120[»]
    3OFRX-ray3.10N1-120[»]
    3OFZX-ray3.29N1-120[»]
    3OG0X-ray3.29N1-120[»]
    3ORBX-ray3.30N1-127[»]
    3R8SX-ray3.00N1-120[»]
    3R8TX-ray3.00N1-120[»]
    3SGFX-ray3.20R1-127[»]
    3UOSX-ray3.70R1-127[»]
    4CSUelectron microscopy5.50N1-127[»]
    4GARX-ray3.30N1-127[»]
    4GAUX-ray3.30N1-127[»]
    4KIXX-ray2.90N1-127[»]
    4KIZX-ray2.90N1-127[»]
    4KJ1X-ray2.90N1-127[»]
    4KJ3X-ray2.90N1-127[»]
    4KJ5X-ray2.90N1-127[»]
    4KJ7X-ray2.90N1-127[»]
    4KJ9X-ray2.90N1-127[»]
    4KJBX-ray2.90N1-127[»]
    ProteinModelPortaliP0AG44.
    SMRiP0AG44. Positions 1-120.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AG44.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L17P family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0203.
    HOGENOMiHOG000019780.
    KOiK02879.
    OMAiFARTRNT.
    OrthoDBiEOG6GR3GR.
    PhylomeDBiP0AG44.

    Family and domain databases

    Gene3Di3.90.1030.10. 1 hit.
    HAMAPiMF_01368. Ribosomal_L17.
    InterProiIPR000456. Ribosomal_L17.
    [Graphical view]
    PANTHERiPTHR14413. PTHR14413. 1 hit.
    PfamiPF01196. Ribosomal_L17. 1 hit.
    [Graphical view]
    SUPFAMiSSF64263. SSF64263. 1 hit.
    TIGRFAMsiTIGR00059. L17. 1 hit.
    PROSITEiPS01167. RIBOSOMAL_L17. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AG44-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRHRKSGRQL NRNSSHRQAM FRNMAGSLVR HEIIKTTLPK AKELRRVVEP    50
    LITLAKTDSV ANRRLAFART RDNEIVAKLF NELGPRFASR AGGYTRILKC 100
    GFRAGDNAPM AYIELVDRSE KAEAAAE 127
    Length:127
    Mass (Da):14,365
    Last modified:July 21, 1986 - v1
    Checksum:iD96DF17C07013A11
    GO

    Mass spectrometryi

    Molecular mass is 14364.7 Da from positions 1 - 127. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02543 Genomic DNA. Translation: CAA26396.1.
    J01685 Genomic DNA. Translation: AAA24578.1.
    X00766 Genomic DNA. Translation: CAA25338.1.
    U18997 Genomic DNA. Translation: AAA58091.1.
    U00096 Genomic DNA. Translation: AAC76319.1.
    AP009048 Genomic DNA. Translation: BAE77997.1.
    PIRiB22884. R5EC17.
    RefSeqiNP_417753.1. NC_000913.3.
    YP_492138.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76319; AAC76319; b3294.
    BAE77997; BAE77997; BAE77997.
    GeneIDi12934436.
    947784.
    KEGGiecj:Y75_p3882.
    eco:b3294.
    PATRICi32122020. VBIEscCol129921_3387.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02543 Genomic DNA. Translation: CAA26396.1 .
    J01685 Genomic DNA. Translation: AAA24578.1 .
    X00766 Genomic DNA. Translation: CAA25338.1 .
    U18997 Genomic DNA. Translation: AAA58091.1 .
    U00096 Genomic DNA. Translation: AAC76319.1 .
    AP009048 Genomic DNA. Translation: BAE77997.1 .
    PIRi B22884. R5EC17.
    RefSeqi NP_417753.1. NC_000913.3.
    YP_492138.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P85 electron microscopy 12.30 L 1-127 [» ]
    1P86 electron microscopy 11.50 L 1-127 [» ]
    1VS6 X-ray 3.46 N 1-127 [» ]
    1VS8 X-ray 3.46 N 1-127 [» ]
    1VT2 X-ray 3.30 N 1-127 [» ]
    2AW4 X-ray 3.46 N 1-127 [» ]
    2AWB X-ray 3.46 N 1-127 [» ]
    2GYA electron microscopy 15.00 L 3-116 [» ]
    2GYC electron microscopy 15.00 L 3-116 [» ]
    2I2T X-ray 3.22 N 1-127 [» ]
    2I2V X-ray 3.22 N 1-127 [» ]
    2J28 electron microscopy 8.00 N 1-127 [» ]
    2QAM X-ray 3.21 N 1-127 [» ]
    2QAO X-ray 3.21 N 1-127 [» ]
    2QBA X-ray 3.54 N 1-127 [» ]
    2QBC X-ray 3.54 N 1-127 [» ]
    2QBE X-ray 3.30 N 1-127 [» ]
    2QBG X-ray 3.30 N 1-127 [» ]
    2QBI X-ray 4.00 N 1-127 [» ]
    2QBK X-ray 4.00 N 1-127 [» ]
    2QOV X-ray 3.93 N 1-127 [» ]
    2QOX X-ray 3.93 N 1-127 [» ]
    2QOZ X-ray 3.50 N 1-127 [» ]
    2QP1 X-ray 3.50 N 1-127 [» ]
    2RDO electron microscopy 9.10 N 1-127 [» ]
    2WWQ electron microscopy 5.80 N 1-120 [» ]
    2Z4L X-ray 4.45 N 1-127 [» ]
    2Z4N X-ray 4.45 N 1-127 [» ]
    3BBX electron microscopy 10.00 N 1-127 [» ]
    3E1B electron microscopy - G 1-127 [» ]
    3E1D electron microscopy - G 1-127 [» ]
    3FIK electron microscopy 6.70 N 1-120 [» ]
    3I1N X-ray 3.19 N 1-127 [» ]
    3I1P X-ray 3.19 N 1-127 [» ]
    3I1R X-ray 3.81 N 1-127 [» ]
    3I1T X-ray 3.81 N 1-127 [» ]
    3I20 X-ray 3.71 N 1-127 [» ]
    3I22 X-ray 3.71 N 1-127 [» ]
    3IZT electron microscopy - O 1-127 [» ]
    3IZU electron microscopy - O 1-127 [» ]
    3J01 electron microscopy - N 1-127 [» ]
    3J0T electron microscopy 12.10 P 1-127 [» ]
    3J0W electron microscopy 14.70 P 1-127 [» ]
    3J0Y electron microscopy 13.50 P 1-127 [» ]
    3J11 electron microscopy 13.10 P 1-127 [» ]
    3J12 electron microscopy 11.50 P 1-127 [» ]
    3J14 electron microscopy 11.50 P 1-127 [» ]
    3J19 electron microscopy 8.30 N 1-120 [» ]
    3J37 electron microscopy 9.80 R 1-127 [» ]
    3J4X electron microscopy 12.00 N 1-120 [» ]
    3J50 electron microscopy 20.00 N 1-120 [» ]
    3J51 electron microscopy 17.00 N 1-120 [» ]
    3J52 electron microscopy 12.00 N 1-120 [» ]
    3J54 electron microscopy 13.00 N 1-120 [» ]
    3J56 electron microscopy 15.00 N 1-120 [» ]
    3J58 electron microscopy 17.00 N 1-120 [» ]
    3J5A electron microscopy 12.00 N 1-120 [» ]
    3J5C electron microscopy 17.00 N 1-120 [» ]
    3J5E electron microscopy 17.00 N 1-120 [» ]
    3J5G electron microscopy 20.00 N 1-120 [» ]
    3J5I electron microscopy 15.00 N 1-120 [» ]
    3J5K electron microscopy 9.00 N 1-120 [» ]
    3J5L electron microscopy 6.60 N 1-120 [» ]
    3J5O electron microscopy 6.80 N 1-127 [» ]
    3J5U electron microscopy 7.60 P 1-127 [» ]
    3J5W electron microscopy 7.60 Q 1-127 [» ]
    3KCR electron microscopy - N 1-127 [» ]
    3OAS X-ray 3.25 N 1-120 [» ]
    3OAT X-ray 3.25 N 1-120 [» ]
    3OFC X-ray 3.19 N 1-120 [» ]
    3OFD X-ray 3.19 N 1-120 [» ]
    3OFQ X-ray 3.10 N 1-120 [» ]
    3OFR X-ray 3.10 N 1-120 [» ]
    3OFZ X-ray 3.29 N 1-120 [» ]
    3OG0 X-ray 3.29 N 1-120 [» ]
    3ORB X-ray 3.30 N 1-127 [» ]
    3R8S X-ray 3.00 N 1-120 [» ]
    3R8T X-ray 3.00 N 1-120 [» ]
    3SGF X-ray 3.20 R 1-127 [» ]
    3UOS X-ray 3.70 R 1-127 [» ]
    4CSU electron microscopy 5.50 N 1-127 [» ]
    4GAR X-ray 3.30 N 1-127 [» ]
    4GAU X-ray 3.30 N 1-127 [» ]
    4KIX X-ray 2.90 N 1-127 [» ]
    4KIZ X-ray 2.90 N 1-127 [» ]
    4KJ1 X-ray 2.90 N 1-127 [» ]
    4KJ3 X-ray 2.90 N 1-127 [» ]
    4KJ5 X-ray 2.90 N 1-127 [» ]
    4KJ7 X-ray 2.90 N 1-127 [» ]
    4KJ9 X-ray 2.90 N 1-127 [» ]
    4KJB X-ray 2.90 N 1-127 [» ]
    ProteinModelPortali P0AG44.
    SMRi P0AG44. Positions 1-120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35801N.
    IntActi P0AG44. 135 interactions.
    MINTi MINT-1251899.
    STRINGi 511145.b3294.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0AG44.
    PRIDEi P0AG44.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76319 ; AAC76319 ; b3294 .
    BAE77997 ; BAE77997 ; BAE77997 .
    GeneIDi 12934436.
    947784.
    KEGGi ecj:Y75_p3882.
    eco:b3294.
    PATRICi 32122020. VBIEscCol129921_3387.

    Organism-specific databases

    EchoBASEi EB0871.
    EcoGenei EG10878. rplQ.

    Phylogenomic databases

    eggNOGi COG0203.
    HOGENOMi HOG000019780.
    KOi K02879.
    OMAi FARTRNT.
    OrthoDBi EOG6GR3GR.
    PhylomeDBi P0AG44.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10878-MONOMER.
    ECOL316407:JW3256-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AG44.
    PROi P0AG44.

    Gene expression databases

    Genevestigatori P0AG44.

    Family and domain databases

    Gene3Di 3.90.1030.10. 1 hit.
    HAMAPi MF_01368. Ribosomal_L17.
    InterProi IPR000456. Ribosomal_L17.
    [Graphical view ]
    PANTHERi PTHR14413. PTHR14413. 1 hit.
    Pfami PF01196. Ribosomal_L17. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64263. SSF64263. 1 hit.
    TIGRFAMsi TIGR00059. L17. 1 hit.
    PROSITEi PS01167. RIBOSOMAL_L17. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of protein L17 from the Escherichia coli ribosome."
      Rombauts W., Feytons V., Wittmann-Liebold B.
      FEBS Lett. 149:320-327(1982)
      Cited for: PROTEIN SEQUENCE.
    2. "Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second regulatory binding site for protein S4?"
      Meek D.W., Hayward R.S.
      Nucleic Acids Res. 12:5813-5821(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Nucleotide sequence of the alpha ribosomal protein operon of Escherichia coli."
      Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H., Zengel J.M., Lindahl L.
      Nucleic Acids Res. 13:3891-3903(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "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.
    6. "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.
    7. "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
      Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
      Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO L32.
    8. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    9. "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.
    10. "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.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL17_ECOLI
    AccessioniPrimary (citable) accession number: P0AG44
    Secondary accession number(s): P02416, Q2M6V9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 87 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