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P0A7M9

- RL31_ECOLI

UniProt

P0A7M9 - RL31_ECOLI

Protein

50S ribosomal protein L31

Gene

rpmE

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

    Binds the 23S rRNA.By similarity

    Cofactori

    Binds 1 zinc ion per subunit. Only 1 ligand appears to be Cys, the other are thought to be His and either backbone amides or solvent (PubMed:22196016).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi16 – 161ZincCurated

    GO - Molecular functioni

    1. rRNA binding Source: UniProtKB-KW
    2. structural constituent of ribosome Source: InterPro
    3. zinc ion binding Source: EcoCyc

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    Metal-binding, RNA-binding, rRNA-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10889-MONOMER.
    ECOL316407:JW3907-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L31
    Gene namesi
    Name:rpmE
    Ordered Locus Names:b3936, JW3907
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10889. rpmE.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi16 – 161C → S: No Zn(2+) binding. 1 Publication
    Mutagenesisi18 – 181C → S: Binds Zn(2+) normally. 1 Publication
    Mutagenesisi37 – 404CSKC → SSKS: Binds Zn(2+) normally.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 707050S ribosomal protein L31PRO_0000173102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81N6-acetyllysine1 Publication

    Post-translational modificationi

    Proteolytically cleaved by protease VII to yield a peptide lacking residues 63-70. It is not clear if this is due to protein degradation or is a bona fide processing event in the strain used in PubMed:339950 and PubMed:10556732. In strains B, D10, MRE-600 and Q13 the only protein seen in PubMed:10556732 was full length; the last 7 amino acids were sequenced only for strain MRE-600.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP0A7M9.
    PRIDEiP0A7M9.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7M9.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit.

    Protein-protein interaction databases

    IntActiP0A7M9. 14 interactions.
    STRINGi511145.b3936.

    Structurei

    Secondary structure

    1
    70
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Beta strandi18 – 203
    Beta strandi38 – 403
    Turni49 – 535
    Helixi54 – 574
    Turni62 – 676

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VS6X-ray3.46Z1-70[»]
    1VS8X-ray3.46Z1-70[»]
    2AW4X-ray3.46Z1-70[»]
    2AWBX-ray3.46Z1-70[»]
    2J28electron microscopy8.00Z1-70[»]
    2RDOelectron microscopy9.10Z1-70[»]
    2VHMX-ray3.74Z1-70[»]
    2VHNX-ray3.74Z1-70[»]
    3BBXelectron microscopy10.00Z1-70[»]
    3E1Belectron microscopy-S1-70[»]
    3E1Delectron microscopy-S1-70[»]
    3IZTelectron microscopy-b1-70[»]
    3IZUelectron microscopy-b1-70[»]
    3J0Telectron microscopy12.1021-70[»]
    3J0Welectron microscopy14.7021-70[»]
    3J0Yelectron microscopy13.5021-70[»]
    3J11electron microscopy13.1021-70[»]
    3J12electron microscopy11.5021-70[»]
    3J14electron microscopy11.5021-70[»]
    3J37electron microscopy9.8041-70[»]
    ProteinModelPortaliP0A7M9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7M9.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0254.
    HOGENOMiHOG000284895.
    KOiK02909.
    OMAiTANCSCG.
    OrthoDBiEOG6DVJZM.
    PhylomeDBiP0A7M9.

    Family and domain databases

    HAMAPiMF_00501. Ribosomal_L31_1.
    InterProiIPR002150. Ribosomal_L31.
    IPR027491. Ribosomal_L31_A.
    [Graphical view]
    PfamiPF01197. Ribosomal_L31. 1 hit.
    [Graphical view]
    PRINTSiPR01249. RIBOSOMALL31.
    TIGRFAMsiTIGR00105. L31. 1 hit.
    PROSITEiPS01143. RIBOSOMAL_L31. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0A7M9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKDIHPKYE EITASCSCGN VMKIRSTVGH DLNLDVCSKC HPFFTGKQRD   50
    VATGGRVDRF NKRFNIPGSK 70
    Length:70
    Mass (Da):7,871
    Last modified:June 7, 2005 - v1
    Checksum:iD657A681A0B858CF
    GO

    Mass spectrometryi

    Molecular mass is 6971.1 Da from positions 1 - 62. Determined by MALDI. 1 Publication
    Molecular mass is 7871.0 Da from positions 1 - 70. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78541 Genomic DNA. Translation: CAA55286.1.
    L19201 Genomic DNA. Translation: AAB03068.1.
    U00096 Genomic DNA. Translation: AAC76918.1.
    AP009048 Genomic DNA. Translation: BAE77374.1.
    PIRiS40879. R5EC31.
    RefSeqiNP_418371.1. NC_000913.3.
    YP_491515.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76918; AAC76918; b3936.
    BAE77374; BAE77374; BAE77374.
    GeneIDi12932190.
    948425.
    KEGGiecj:Y75_p3251.
    eco:b3936.
    PATRICi32123389. VBIEscCol129921_4055.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78541 Genomic DNA. Translation: CAA55286.1 .
    L19201 Genomic DNA. Translation: AAB03068.1 .
    U00096 Genomic DNA. Translation: AAC76918.1 .
    AP009048 Genomic DNA. Translation: BAE77374.1 .
    PIRi S40879. R5EC31.
    RefSeqi NP_418371.1. NC_000913.3.
    YP_491515.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VS6 X-ray 3.46 Z 1-70 [» ]
    1VS8 X-ray 3.46 Z 1-70 [» ]
    2AW4 X-ray 3.46 Z 1-70 [» ]
    2AWB X-ray 3.46 Z 1-70 [» ]
    2J28 electron microscopy 8.00 Z 1-70 [» ]
    2RDO electron microscopy 9.10 Z 1-70 [» ]
    2VHM X-ray 3.74 Z 1-70 [» ]
    2VHN X-ray 3.74 Z 1-70 [» ]
    3BBX electron microscopy 10.00 Z 1-70 [» ]
    3E1B electron microscopy - S 1-70 [» ]
    3E1D electron microscopy - S 1-70 [» ]
    3IZT electron microscopy - b 1-70 [» ]
    3IZU electron microscopy - b 1-70 [» ]
    3J0T electron microscopy 12.10 2 1-70 [» ]
    3J0W electron microscopy 14.70 2 1-70 [» ]
    3J0Y electron microscopy 13.50 2 1-70 [» ]
    3J11 electron microscopy 13.10 2 1-70 [» ]
    3J12 electron microscopy 11.50 2 1-70 [» ]
    3J14 electron microscopy 11.50 2 1-70 [» ]
    3J37 electron microscopy 9.80 4 1-70 [» ]
    ProteinModelPortali P0A7M9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A7M9. 14 interactions.
    STRINGi 511145.b3936.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7M9.
    PRIDEi P0A7M9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76918 ; AAC76918 ; b3936 .
    BAE77374 ; BAE77374 ; BAE77374 .
    GeneIDi 12932190.
    948425.
    KEGGi ecj:Y75_p3251.
    eco:b3936.
    PATRICi 32123389. VBIEscCol129921_4055.

    Organism-specific databases

    EchoBASEi EB0882.
    EcoGenei EG10889. rpmE.

    Phylogenomic databases

    eggNOGi COG0254.
    HOGENOMi HOG000284895.
    KOi K02909.
    OMAi TANCSCG.
    OrthoDBi EOG6DVJZM.
    PhylomeDBi P0A7M9.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10889-MONOMER.
    ECOL316407:JW3907-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7M9.
    PROi P0A7M9.

    Gene expression databases

    Genevestigatori P0A7M9.

    Family and domain databases

    HAMAPi MF_00501. Ribosomal_L31_1.
    InterProi IPR002150. Ribosomal_L31.
    IPR027491. Ribosomal_L31_A.
    [Graphical view ]
    Pfami PF01197. Ribosomal_L31. 1 hit.
    [Graphical view ]
    PRINTSi PR01249. RIBOSOMALL31.
    TIGRFAMsi TIGR00105. L31. 1 hit.
    PROSITEi PS01143. RIBOSOMAL_L31. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
      Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Primary structure of Escherichia coli ribosomal protein L31."
      Brosius J.
      Biochemistry 17:501-508(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-62.
      Strain: B.
    5. "Small genes/gene-products in Escherichia coli K-12."
      Wasinger V.C., Humphery-Smith I.
      FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10.
      Strain: K12.
    6. "Characterization of Escherichia coli 50S ribosomal protein L31."
      Eistetter A.J., Butler P.D., Traut R.R., Fanning T.G.
      FEMS Microbiol. Lett. 180:345-349(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 64-70 (STRAIN MRE-600), EXAMINATION OF MOLECULAR WEIGHT IN SEVERAL STRAINS.
      Strain: B, K12 / D10, K12 / Q13 and MRE-600.
    7. "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.
    8. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    9. Cited for: ZINC-BINDING, COFACTOR, MUTAGENESIS OF CYS-16; CYS-18 AND 37-CYS--CYS-40.
      Strain: BW21135.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL31_ECOLI
    AccessioniPrimary (citable) accession number: P0A7M9
    Secondary accession number(s): P02432, Q2M8N2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 88 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