Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P0A7N9

- RL33_ECOLI

UniProt

P0A7N9 - RL33_ECOLI

Protein

50S ribosomal protein L33

Gene

rpmG

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

    GO - Molecular functioni

    1. structural constituent of ribosome Source: InterPro
    2. tRNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10891-MONOMER.
    ECOL316407:JW3611-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L33
    Gene namesi
    Name:rpmG
    Ordered Locus Names:b3636, JW3611
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10891. rpmG.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 555450S ribosomal protein L33PRO_0000170158Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-methylalanine

    Keywords - PTMi

    Methylation

    Proteomic databases

    PaxDbiP0A7N9.
    PRIDEiP0A7N9.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7N9.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Cross-links to the P and E site tRNAs.

    Protein-protein interaction databases

    DIPiDIP-35968N.
    IntActiP0A7N9. 53 interactions.
    MINTiMINT-1234559.
    STRINGi511145.b3636.

    Structurei

    Secondary structure

    1
    55
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 1711
    Beta strandi20 – 256
    Turni27 – 293
    Beta strandi36 – 405
    Turni41 – 444
    Beta strandi45 – 506

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P85electron microscopy12.3012-55[»]
    1P86electron microscopy11.5012-55[»]
    1VS6X-ray3.4611-55[»]
    1VS8X-ray3.4611-55[»]
    1VT2X-ray3.3011-55[»]
    2AW4X-ray3.4612-55[»]
    2AWBX-ray3.4612-55[»]
    2GYAelectron microscopy15.0012-53[»]
    2GYCelectron microscopy15.0012-53[»]
    2I2TX-ray3.2212-55[»]
    2I2VX-ray3.2212-55[»]
    2J28electron microscopy8.0012-55[»]
    2QAMX-ray3.2112-55[»]
    2QAOX-ray3.2112-55[»]
    2QBAX-ray3.5412-55[»]
    2QBCX-ray3.5412-55[»]
    2QBEX-ray3.3012-55[»]
    2QBGX-ray3.3012-55[»]
    2QBIX-ray4.0012-55[»]
    2QBKX-ray4.0012-55[»]
    2QOVX-ray3.9312-55[»]
    2QOXX-ray3.9312-55[»]
    2QOZX-ray3.5012-55[»]
    2QP1X-ray3.5012-55[»]
    2RDOelectron microscopy9.1012-55[»]
    2VHMX-ray3.7412-55[»]
    2VHNX-ray3.7412-55[»]
    2WWQelectron microscopy5.8044-53[»]
    2Z4LX-ray4.4512-55[»]
    2Z4NX-ray4.4512-55[»]
    3BBXelectron microscopy10.0012-55[»]
    3DF2X-ray3.5012-54[»]
    3DF4X-ray3.5012-54[»]
    3E1Belectron microscopy-U2-55[»]
    3E1Delectron microscopy-U2-55[»]
    3FIKelectron microscopy6.7014-53[»]
    3I1NX-ray3.1911-55[»]
    3I1PX-ray3.1911-55[»]
    3I1RX-ray3.8111-55[»]
    3I1TX-ray3.8111-55[»]
    3I20X-ray3.7111-55[»]
    3I22X-ray3.7111-55[»]
    3IZTelectron microscopy-d1-55[»]
    3IZUelectron microscopy-d1-55[»]
    3J01electron microscopy-12-55[»]
    3J0Telectron microscopy12.1042-55[»]
    3J0Welectron microscopy14.7042-55[»]
    3J0Yelectron microscopy13.5042-55[»]
    3J11electron microscopy13.1042-55[»]
    3J12electron microscopy11.5042-55[»]
    3J14electron microscopy11.5042-55[»]
    3J19electron microscopy8.3014-53[»]
    3J37electron microscopy9.8062-55[»]
    3J4Xelectron microscopy12.0014-53[»]
    3J50electron microscopy20.0014-53[»]
    3J51electron microscopy17.0014-53[»]
    3J52electron microscopy12.0014-53[»]
    3J54electron microscopy13.0014-53[»]
    3J56electron microscopy15.0014-53[»]
    3J58electron microscopy17.0014-53[»]
    3J5Aelectron microscopy12.0014-53[»]
    3J5Celectron microscopy17.0014-53[»]
    3J5Eelectron microscopy17.0014-53[»]
    3J5Gelectron microscopy20.0014-53[»]
    3J5Ielectron microscopy15.0014-53[»]
    3J5Kelectron microscopy9.0014-53[»]
    3J5Lelectron microscopy6.6014-53[»]
    3J5Oelectron microscopy6.8011-55[»]
    3J5Selectron microscopy7.50H4-53[»]
    3J5Uelectron microscopy7.6042-55[»]
    3J5Welectron microscopy7.6052-55[»]
    3KCRelectron microscopy-11-55[»]
    3OASX-ray3.2514-53[»]
    3OATX-ray3.2514-53[»]
    3OFCX-ray3.1914-53[»]
    3OFDX-ray3.1914-53[»]
    3OFQX-ray3.1014-53[»]
    3OFRX-ray3.1014-53[»]
    3OFZX-ray3.2914-53[»]
    3OG0X-ray3.2914-53[»]
    3ORBX-ray3.3011-55[»]
    3R8SX-ray3.0014-53[»]
    3R8TX-ray3.0014-53[»]
    3SGFX-ray3.2051-55[»]
    3UOSX-ray3.7051-55[»]
    4CSUelectron microscopy5.5042-55[»]
    4GARX-ray3.3011-55[»]
    4GAUX-ray3.3011-55[»]
    4KIXX-ray2.9011-55[»]
    4KIZX-ray2.9011-55[»]
    4KJ1X-ray2.9011-55[»]
    4KJ3X-ray2.9011-55[»]
    4KJ5X-ray2.9011-55[»]
    4KJ7X-ray2.9011-55[»]
    4KJ9X-ray2.9011-55[»]
    4KJBX-ray2.9011-55[»]
    DisProtiDP00143.
    ProteinModelPortaliP0A7N9.
    SMRiP0A7N9. Positions 2-53.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7N9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L33P family.Curated

    Phylogenomic databases

    eggNOGiCOG0267.
    HOGENOMiHOG000004839.
    KOiK02913.
    OMAiVIYREAK.
    OrthoDBiEOG60KNBM.
    PhylomeDBiP0A7N9.

    Family and domain databases

    HAMAPiMF_00294. Ribosomal_L33.
    InterProiIPR001705. Ribosomal_L33.
    IPR018264. Ribosomal_L33_CS.
    IPR011332. Ribosomal_zn-bd.
    [Graphical view]
    PfamiPF00471. Ribosomal_L33. 1 hit.
    [Graphical view]
    SUPFAMiSSF57829. SSF57829. 1 hit.
    TIGRFAMsiTIGR01023. rpmG_bact. 1 hit.
    PROSITEiPS00582. RIBOSOMAL_L33. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7N9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKGIREKIK LVSSAGTGHF YTTTKNKRTK PEKLELKKFD PVVRQHVIYK   50
    EAKIK 55
    Length:55
    Mass (Da):6,372
    Last modified:January 23, 2007 - v2
    Checksum:i31681CC3DAC0C5D6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 492IY → YI AA sequence (PubMed:786732)Curated

    Mass spectrometryi

    Molecular mass is 6254.1 Da from positions 2 - 55. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01677 Genomic DNA. Translation: AAA74100.1.
    L10328 Genomic DNA. Translation: AAA61989.1.
    U00096 Genomic DNA. Translation: AAC76660.1.
    AP009048 Genomic DNA. Translation: BAE77656.1.
    PIRiS42444. R5EC33.
    RefSeqiNP_418093.1. NC_000913.3.
    YP_491797.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76660; AAC76660; b3636.
    BAE77656; BAE77656; BAE77656.
    GeneIDi12931828.
    946318.
    KEGGiecj:Y75_p3538.
    eco:b3636.
    PATRICi32122759. VBIEscCol129921_3756.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01677 Genomic DNA. Translation: AAA74100.1 .
    L10328 Genomic DNA. Translation: AAA61989.1 .
    U00096 Genomic DNA. Translation: AAC76660.1 .
    AP009048 Genomic DNA. Translation: BAE77656.1 .
    PIRi S42444. R5EC33.
    RefSeqi NP_418093.1. NC_000913.3.
    YP_491797.1. 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 1 2-55 [» ]
    1P86 electron microscopy 11.50 1 2-55 [» ]
    1VS6 X-ray 3.46 1 1-55 [» ]
    1VS8 X-ray 3.46 1 1-55 [» ]
    1VT2 X-ray 3.30 1 1-55 [» ]
    2AW4 X-ray 3.46 1 2-55 [» ]
    2AWB X-ray 3.46 1 2-55 [» ]
    2GYA electron microscopy 15.00 1 2-53 [» ]
    2GYC electron microscopy 15.00 1 2-53 [» ]
    2I2T X-ray 3.22 1 2-55 [» ]
    2I2V X-ray 3.22 1 2-55 [» ]
    2J28 electron microscopy 8.00 1 2-55 [» ]
    2QAM X-ray 3.21 1 2-55 [» ]
    2QAO X-ray 3.21 1 2-55 [» ]
    2QBA X-ray 3.54 1 2-55 [» ]
    2QBC X-ray 3.54 1 2-55 [» ]
    2QBE X-ray 3.30 1 2-55 [» ]
    2QBG X-ray 3.30 1 2-55 [» ]
    2QBI X-ray 4.00 1 2-55 [» ]
    2QBK X-ray 4.00 1 2-55 [» ]
    2QOV X-ray 3.93 1 2-55 [» ]
    2QOX X-ray 3.93 1 2-55 [» ]
    2QOZ X-ray 3.50 1 2-55 [» ]
    2QP1 X-ray 3.50 1 2-55 [» ]
    2RDO electron microscopy 9.10 1 2-55 [» ]
    2VHM X-ray 3.74 1 2-55 [» ]
    2VHN X-ray 3.74 1 2-55 [» ]
    2WWQ electron microscopy 5.80 4 4-53 [» ]
    2Z4L X-ray 4.45 1 2-55 [» ]
    2Z4N X-ray 4.45 1 2-55 [» ]
    3BBX electron microscopy 10.00 1 2-55 [» ]
    3DF2 X-ray 3.50 1 2-54 [» ]
    3DF4 X-ray 3.50 1 2-54 [» ]
    3E1B electron microscopy - U 2-55 [» ]
    3E1D electron microscopy - U 2-55 [» ]
    3FIK electron microscopy 6.70 1 4-53 [» ]
    3I1N X-ray 3.19 1 1-55 [» ]
    3I1P X-ray 3.19 1 1-55 [» ]
    3I1R X-ray 3.81 1 1-55 [» ]
    3I1T X-ray 3.81 1 1-55 [» ]
    3I20 X-ray 3.71 1 1-55 [» ]
    3I22 X-ray 3.71 1 1-55 [» ]
    3IZT electron microscopy - d 1-55 [» ]
    3IZU electron microscopy - d 1-55 [» ]
    3J01 electron microscopy - 1 2-55 [» ]
    3J0T electron microscopy 12.10 4 2-55 [» ]
    3J0W electron microscopy 14.70 4 2-55 [» ]
    3J0Y electron microscopy 13.50 4 2-55 [» ]
    3J11 electron microscopy 13.10 4 2-55 [» ]
    3J12 electron microscopy 11.50 4 2-55 [» ]
    3J14 electron microscopy 11.50 4 2-55 [» ]
    3J19 electron microscopy 8.30 1 4-53 [» ]
    3J37 electron microscopy 9.80 6 2-55 [» ]
    3J4X electron microscopy 12.00 1 4-53 [» ]
    3J50 electron microscopy 20.00 1 4-53 [» ]
    3J51 electron microscopy 17.00 1 4-53 [» ]
    3J52 electron microscopy 12.00 1 4-53 [» ]
    3J54 electron microscopy 13.00 1 4-53 [» ]
    3J56 electron microscopy 15.00 1 4-53 [» ]
    3J58 electron microscopy 17.00 1 4-53 [» ]
    3J5A electron microscopy 12.00 1 4-53 [» ]
    3J5C electron microscopy 17.00 1 4-53 [» ]
    3J5E electron microscopy 17.00 1 4-53 [» ]
    3J5G electron microscopy 20.00 1 4-53 [» ]
    3J5I electron microscopy 15.00 1 4-53 [» ]
    3J5K electron microscopy 9.00 1 4-53 [» ]
    3J5L electron microscopy 6.60 1 4-53 [» ]
    3J5O electron microscopy 6.80 1 1-55 [» ]
    3J5S electron microscopy 7.50 H 4-53 [» ]
    3J5U electron microscopy 7.60 4 2-55 [» ]
    3J5W electron microscopy 7.60 5 2-55 [» ]
    3KCR electron microscopy - 1 1-55 [» ]
    3OAS X-ray 3.25 1 4-53 [» ]
    3OAT X-ray 3.25 1 4-53 [» ]
    3OFC X-ray 3.19 1 4-53 [» ]
    3OFD X-ray 3.19 1 4-53 [» ]
    3OFQ X-ray 3.10 1 4-53 [» ]
    3OFR X-ray 3.10 1 4-53 [» ]
    3OFZ X-ray 3.29 1 4-53 [» ]
    3OG0 X-ray 3.29 1 4-53 [» ]
    3ORB X-ray 3.30 1 1-55 [» ]
    3R8S X-ray 3.00 1 4-53 [» ]
    3R8T X-ray 3.00 1 4-53 [» ]
    3SGF X-ray 3.20 5 1-55 [» ]
    3UOS X-ray 3.70 5 1-55 [» ]
    4CSU electron microscopy 5.50 4 2-55 [» ]
    4GAR X-ray 3.30 1 1-55 [» ]
    4GAU X-ray 3.30 1 1-55 [» ]
    4KIX X-ray 2.90 1 1-55 [» ]
    4KIZ X-ray 2.90 1 1-55 [» ]
    4KJ1 X-ray 2.90 1 1-55 [» ]
    4KJ3 X-ray 2.90 1 1-55 [» ]
    4KJ5 X-ray 2.90 1 1-55 [» ]
    4KJ7 X-ray 2.90 1 1-55 [» ]
    4KJ9 X-ray 2.90 1 1-55 [» ]
    4KJB X-ray 2.90 1 1-55 [» ]
    DisProti DP00143.
    ProteinModelPortali P0A7N9.
    SMRi P0A7N9. Positions 2-53.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35968N.
    IntActi P0A7N9. 53 interactions.
    MINTi MINT-1234559.
    STRINGi 511145.b3636.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7N9.
    PRIDEi P0A7N9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76660 ; AAC76660 ; b3636 .
    BAE77656 ; BAE77656 ; BAE77656 .
    GeneIDi 12931828.
    946318.
    KEGGi ecj:Y75_p3538.
    eco:b3636.
    PATRICi 32122759. VBIEscCol129921_3756.

    Organism-specific databases

    EchoBASEi EB0884.
    EcoGenei EG10891. rpmG.

    Phylogenomic databases

    eggNOGi COG0267.
    HOGENOMi HOG000004839.
    KOi K02913.
    OMAi VIYREAK.
    OrthoDBi EOG60KNBM.
    PhylomeDBi P0A7N9.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10891-MONOMER.
    ECOL316407:JW3611-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7N9.
    PROi P0A7N9.

    Gene expression databases

    Genevestigatori P0A7N9.

    Family and domain databases

    HAMAPi MF_00294. Ribosomal_L33.
    InterProi IPR001705. Ribosomal_L33.
    IPR018264. Ribosomal_L33_CS.
    IPR011332. Ribosomal_zn-bd.
    [Graphical view ]
    Pfami PF00471. Ribosomal_L33. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57829. SSF57829. 1 hit.
    TIGRFAMsi TIGR01023. rpmG_bact. 1 hit.
    PROSITEi PS00582. RIBOSOMAL_L33. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and the nucleotide sequence of the genes for Escherichia coli ribosomal proteins L28 (rpmB) and L33 (rpmG)."
      Lee J.S., An G., Friesen J.D., Isono K.
      Mol. Gen. Genet. 184:218-223(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
      Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
      Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "Primary structure of protein L33 from the large subunit of the Escherichia coli ribosome."
      Wittmann-Liebold B., Pannenbecker R.
      FEBS Lett. 68:115-118(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-55.
      Strain: K.
    6. "The ribosomal neighbourhood of the central fold of tRNA: cross-links from position 47 of tRNA located at the A, P or E site."
      Osswald M., Doering T., Brimacombe R.
      Nucleic Acids Res. 23:4635-4641(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO THE TRNA CENTRAL FOLD.
      Strain: 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. "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.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL33_ECOLI
    AccessioniPrimary (citable) accession number: P0A7N9
    Secondary accession number(s): P02436, Q2M7V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 98 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Surface exposed on the 50S subunit.

    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