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P0A7Q1

- RL35_ECOLI

UniProt

P0A7Q1 - RL35_ECOLI

Protein

50S ribosomal protein L35

Gene

rpmI

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

    GO - Molecular functioni

    1. structural constituent of ribosome Source: EcoCyc

    GO - Biological processi

    1. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11231-MONOMER.
    ECOL316407:JW1707-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L35
    Alternative name(s):
    Ribosomal protein A
    Gene namesi
    Name:rpmI
    Ordered Locus Names:b1717, JW1707
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11231. rpmI.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 656450S ribosomal protein L35PRO_0000177359Add
    BLAST

    Proteomic databases

    PaxDbiP0A7Q1.
    PRIDEiP0A7Q1.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7Q1.

    Interactioni

    Protein-protein interaction databases

    IntActiP0A7Q1. 4 interactions.
    STRINGi511145.b1717.

    Structurei

    Secondary structure

    1
    65
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114
    Beta strandi14 – 163
    Beta strandi18 – 203
    Beta strandi22 – 254
    Beta strandi30 – 323
    Beta strandi34 – 363
    Helixi38 – 436
    Beta strandi45 – 495
    Turni52 – 543
    Helixi55 – 617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VS6X-ray3.4631-65[»]
    1VS8X-ray3.4631-65[»]
    1VT2X-ray3.3031-65[»]
    2AW4X-ray3.4632-65[»]
    2AWBX-ray3.4632-65[»]
    2I2TX-ray3.2232-65[»]
    2I2VX-ray3.2232-65[»]
    2J28electron microscopy8.0032-65[»]
    2QAMX-ray3.2132-65[»]
    2QAOX-ray3.2132-65[»]
    2QBAX-ray3.5432-65[»]
    2QBCX-ray3.5432-65[»]
    2QBEX-ray3.3032-65[»]
    2QBGX-ray3.3032-65[»]
    2QBIX-ray4.0032-65[»]
    2QBKX-ray4.0032-65[»]
    2QOVX-ray3.9332-65[»]
    2QOXX-ray3.9332-65[»]
    2QOZX-ray3.5032-65[»]
    2QP1X-ray3.5032-65[»]
    2RDOelectron microscopy9.1032-65[»]
    2VHMX-ray3.7432-65[»]
    2VHNX-ray3.7432-65[»]
    2WWQelectron microscopy5.8072-65[»]
    2Z4LX-ray4.4532-65[»]
    2Z4NX-ray4.4532-65[»]
    3BBXelectron microscopy10.0032-65[»]
    3DF2X-ray3.5032-64[»]
    3DF4X-ray3.5032-64[»]
    3E1Belectron microscopy-W2-65[»]
    3E1Delectron microscopy-W2-65[»]
    3FIKelectron microscopy6.7032-65[»]
    3I1NX-ray3.1931-65[»]
    3I1PX-ray3.1931-65[»]
    3I1RX-ray3.8131-65[»]
    3I1TX-ray3.8131-65[»]
    3I20X-ray3.7131-65[»]
    3I22X-ray3.7131-65[»]
    3IZTelectron microscopy-f1-65[»]
    3IZUelectron microscopy-f1-65[»]
    3J01electron microscopy-32-65[»]
    3J0Telectron microscopy12.1062-65[»]
    3J0Welectron microscopy14.7062-65[»]
    3J0Yelectron microscopy13.5062-65[»]
    3J11electron microscopy13.1062-65[»]
    3J12electron microscopy11.5062-65[»]
    3J14electron microscopy11.5062-65[»]
    3J19electron microscopy8.3032-65[»]
    3J37electron microscopy9.8082-65[»]
    3J4Xelectron microscopy12.0031-65[»]
    3J50electron microscopy20.0031-65[»]
    3J51electron microscopy17.0031-65[»]
    3J52electron microscopy12.0031-65[»]
    3J54electron microscopy13.0031-65[»]
    3J56electron microscopy15.0031-65[»]
    3J58electron microscopy17.0031-65[»]
    3J5Aelectron microscopy12.0031-65[»]
    3J5Celectron microscopy17.0031-65[»]
    3J5Eelectron microscopy17.0031-65[»]
    3J5Gelectron microscopy20.0031-65[»]
    3J5Ielectron microscopy15.0031-65[»]
    3J5Kelectron microscopy9.0031-65[»]
    3J5Lelectron microscopy6.6032-65[»]
    3J5Oelectron microscopy6.8031-65[»]
    3J5Uelectron microscopy7.6062-65[»]
    3J5Welectron microscopy7.6072-65[»]
    3KCRelectron microscopy-31-65[»]
    3OASX-ray3.2532-65[»]
    3OATX-ray3.2532-65[»]
    3OFCX-ray3.1932-65[»]
    3OFDX-ray3.1932-65[»]
    3OFQX-ray3.1032-65[»]
    3OFRX-ray3.1032-65[»]
    3OFZX-ray3.2932-65[»]
    3OG0X-ray3.2932-65[»]
    3ORBX-ray3.3031-65[»]
    3R8SX-ray3.0032-65[»]
    3R8TX-ray3.0032-65[»]
    3SGFX-ray3.2071-65[»]
    3UOSX-ray3.7071-65[»]
    4CSUelectron microscopy5.5072-65[»]
    4GARX-ray3.3031-65[»]
    4GAUX-ray3.3031-65[»]
    4KIXX-ray2.9031-65[»]
    4KIZX-ray2.9031-65[»]
    4KJ1X-ray2.9031-65[»]
    4KJ3X-ray2.9031-65[»]
    4KJ5X-ray2.9031-65[»]
    4KJ7X-ray2.9031-65[»]
    4KJ9X-ray2.9031-65[»]
    4KJBX-ray2.9031-65[»]
    ProteinModelPortaliP0A7Q1.
    SMRiP0A7Q1. Positions 2-65.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7Q1.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L35P family.Curated

    Phylogenomic databases

    eggNOGiCOG0291.
    HOGENOMiHOG000040108.
    KOiK02916.
    OMAiSHHNHIL.
    OrthoDBiEOG651T3B.

    Family and domain databases

    HAMAPiMF_00514. Ribosomal_L35.
    InterProiIPR021137. Ribosomal_L35.
    IPR018265. Ribosomal_L35_CS.
    IPR001706. Ribosomal_L35_non-mt.
    [Graphical view]
    PfamiPF01632. Ribosomal_L35p. 1 hit.
    [Graphical view]
    PRINTSiPR00064. RIBOSOMALL35.
    TIGRFAMsiTIGR00001. rpmI_bact. 1 hit.
    PROSITEiPS00936. RIBOSOMAL_L35. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7Q1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKIKTVRGA AKRFKKTGKG GFKHKHANLR HILTKKATKR KRHLRPKAMV   50
    SKGDLGLVIA CLPYA 65
    Length:65
    Mass (Da):7,289
    Last modified:January 23, 2007 - v2
    Checksum:i98A72C0AD6CE0A07
    GO

    Sequence cautioni

    The sequence V00291 differs from that shown. Reason: Frameshift at position 6.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111A → G AA sequence (PubMed:3298224)Curated
    Sequence conflicti11 – 111A → S(PubMed:6325158)Curated
    Sequence conflicti28 – 281N → D AA sequence (PubMed:3542048)Curated

    Mass spectrometryi

    Molecular mass is 7158.0 Da from positions 2 - 65. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00291 Genomic DNA. No translation available.
    U00096 Genomic DNA. Translation: AAC74787.1.
    AP009048 Genomic DNA. Translation: BAA15484.1.
    PIRiE64930. R5EC35.
    RefSeqiNP_416232.3. NC_000913.3.
    YP_489979.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74787; AAC74787; b1717.
    BAA15484; BAA15484; BAA15484.
    GeneIDi12933937.
    946349.
    KEGGiecj:Y75_p1692.
    eco:b1717.
    PATRICi32118738. VBIEscCol129921_1787.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00291 Genomic DNA. No translation available.
    U00096 Genomic DNA. Translation: AAC74787.1 .
    AP009048 Genomic DNA. Translation: BAA15484.1 .
    PIRi E64930. R5EC35.
    RefSeqi NP_416232.3. NC_000913.3.
    YP_489979.1. 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 3 1-65 [» ]
    1VS8 X-ray 3.46 3 1-65 [» ]
    1VT2 X-ray 3.30 3 1-65 [» ]
    2AW4 X-ray 3.46 3 2-65 [» ]
    2AWB X-ray 3.46 3 2-65 [» ]
    2I2T X-ray 3.22 3 2-65 [» ]
    2I2V X-ray 3.22 3 2-65 [» ]
    2J28 electron microscopy 8.00 3 2-65 [» ]
    2QAM X-ray 3.21 3 2-65 [» ]
    2QAO X-ray 3.21 3 2-65 [» ]
    2QBA X-ray 3.54 3 2-65 [» ]
    2QBC X-ray 3.54 3 2-65 [» ]
    2QBE X-ray 3.30 3 2-65 [» ]
    2QBG X-ray 3.30 3 2-65 [» ]
    2QBI X-ray 4.00 3 2-65 [» ]
    2QBK X-ray 4.00 3 2-65 [» ]
    2QOV X-ray 3.93 3 2-65 [» ]
    2QOX X-ray 3.93 3 2-65 [» ]
    2QOZ X-ray 3.50 3 2-65 [» ]
    2QP1 X-ray 3.50 3 2-65 [» ]
    2RDO electron microscopy 9.10 3 2-65 [» ]
    2VHM X-ray 3.74 3 2-65 [» ]
    2VHN X-ray 3.74 3 2-65 [» ]
    2WWQ electron microscopy 5.80 7 2-65 [» ]
    2Z4L X-ray 4.45 3 2-65 [» ]
    2Z4N X-ray 4.45 3 2-65 [» ]
    3BBX electron microscopy 10.00 3 2-65 [» ]
    3DF2 X-ray 3.50 3 2-64 [» ]
    3DF4 X-ray 3.50 3 2-64 [» ]
    3E1B electron microscopy - W 2-65 [» ]
    3E1D electron microscopy - W 2-65 [» ]
    3FIK electron microscopy 6.70 3 2-65 [» ]
    3I1N X-ray 3.19 3 1-65 [» ]
    3I1P X-ray 3.19 3 1-65 [» ]
    3I1R X-ray 3.81 3 1-65 [» ]
    3I1T X-ray 3.81 3 1-65 [» ]
    3I20 X-ray 3.71 3 1-65 [» ]
    3I22 X-ray 3.71 3 1-65 [» ]
    3IZT electron microscopy - f 1-65 [» ]
    3IZU electron microscopy - f 1-65 [» ]
    3J01 electron microscopy - 3 2-65 [» ]
    3J0T electron microscopy 12.10 6 2-65 [» ]
    3J0W electron microscopy 14.70 6 2-65 [» ]
    3J0Y electron microscopy 13.50 6 2-65 [» ]
    3J11 electron microscopy 13.10 6 2-65 [» ]
    3J12 electron microscopy 11.50 6 2-65 [» ]
    3J14 electron microscopy 11.50 6 2-65 [» ]
    3J19 electron microscopy 8.30 3 2-65 [» ]
    3J37 electron microscopy 9.80 8 2-65 [» ]
    3J4X electron microscopy 12.00 3 1-65 [» ]
    3J50 electron microscopy 20.00 3 1-65 [» ]
    3J51 electron microscopy 17.00 3 1-65 [» ]
    3J52 electron microscopy 12.00 3 1-65 [» ]
    3J54 electron microscopy 13.00 3 1-65 [» ]
    3J56 electron microscopy 15.00 3 1-65 [» ]
    3J58 electron microscopy 17.00 3 1-65 [» ]
    3J5A electron microscopy 12.00 3 1-65 [» ]
    3J5C electron microscopy 17.00 3 1-65 [» ]
    3J5E electron microscopy 17.00 3 1-65 [» ]
    3J5G electron microscopy 20.00 3 1-65 [» ]
    3J5I electron microscopy 15.00 3 1-65 [» ]
    3J5K electron microscopy 9.00 3 1-65 [» ]
    3J5L electron microscopy 6.60 3 2-65 [» ]
    3J5O electron microscopy 6.80 3 1-65 [» ]
    3J5U electron microscopy 7.60 6 2-65 [» ]
    3J5W electron microscopy 7.60 7 2-65 [» ]
    3KCR electron microscopy - 3 1-65 [» ]
    3OAS X-ray 3.25 3 2-65 [» ]
    3OAT X-ray 3.25 3 2-65 [» ]
    3OFC X-ray 3.19 3 2-65 [» ]
    3OFD X-ray 3.19 3 2-65 [» ]
    3OFQ X-ray 3.10 3 2-65 [» ]
    3OFR X-ray 3.10 3 2-65 [» ]
    3OFZ X-ray 3.29 3 2-65 [» ]
    3OG0 X-ray 3.29 3 2-65 [» ]
    3ORB X-ray 3.30 3 1-65 [» ]
    3R8S X-ray 3.00 3 2-65 [» ]
    3R8T X-ray 3.00 3 2-65 [» ]
    3SGF X-ray 3.20 7 1-65 [» ]
    3UOS X-ray 3.70 7 1-65 [» ]
    4CSU electron microscopy 5.50 7 2-65 [» ]
    4GAR X-ray 3.30 3 1-65 [» ]
    4GAU X-ray 3.30 3 1-65 [» ]
    4KIX X-ray 2.90 3 1-65 [» ]
    4KIZ X-ray 2.90 3 1-65 [» ]
    4KJ1 X-ray 2.90 3 1-65 [» ]
    4KJ3 X-ray 2.90 3 1-65 [» ]
    4KJ5 X-ray 2.90 3 1-65 [» ]
    4KJ7 X-ray 2.90 3 1-65 [» ]
    4KJ9 X-ray 2.90 3 1-65 [» ]
    4KJB X-ray 2.90 3 1-65 [» ]
    ProteinModelPortali P0A7Q1.
    SMRi P0A7Q1. Positions 2-65.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0A7Q1. 4 interactions.
    STRINGi 511145.b1717.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P0A7Q1.
    PRIDEi P0A7Q1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74787 ; AAC74787 ; b1717 .
    BAA15484 ; BAA15484 ; BAA15484 .
    GeneIDi 12933937.
    946349.
    KEGGi ecj:Y75_p1692.
    eco:b1717.
    PATRICi 32118738. VBIEscCol129921_1787.

    Organism-specific databases

    EchoBASEi EB1213.
    EcoGenei EG11231. rpmI.

    Phylogenomic databases

    eggNOGi COG0291.
    HOGENOMi HOG000040108.
    KOi K02916.
    OMAi SHHNHIL.
    OrthoDBi EOG651T3B.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11231-MONOMER.
    ECOL316407:JW1707-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7Q1.
    PROi P0A7Q1.

    Gene expression databases

    Genevestigatori P0A7Q1.

    Family and domain databases

    HAMAPi MF_00514. Ribosomal_L35.
    InterProi IPR021137. Ribosomal_L35.
    IPR018265. Ribosomal_L35_CS.
    IPR001706. Ribosomal_L35_non-mt.
    [Graphical view ]
    Pfami PF01632. Ribosomal_L35p. 1 hit.
    [Graphical view ]
    PRINTSi PR00064. RIBOSOMALL35.
    TIGRFAMsi TIGR00001. rpmI_bact. 1 hit.
    PROSITEi PS00936. RIBOSOMAL_L35. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of a 1.26-kb DNA fragment containing the structural gene for E.coli initiation factor IF3: presence of an AUU initiator codon."
      Sacerdot C., Fayat G., Dessen P., Springer M., Plumbridge J.A., Grunberg-Manago M., Blanquet S.
      EMBO J. 1:311-315(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    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. "Nonspecific inhibition of Escherichia coli ornithine decarboxylase by various ribosomal proteins: detection of a new ribosomal protein possessing strong antizyme activity."
      Kashiwagi K., Igarashi K.
      Biochim. Biophys. Acta 911:180-190(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-42.
    6. "Primary structures of and genes for new ribosomal proteins A and B in Escherichia coli."
      Wada A., Sako T.
      J. Biochem. 101:817-820(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-36.
    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. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL35_ECOLI
    AccessioniPrimary (citable) accession number: P0A7Q1
    Secondary accession number(s): P07085, P78275
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 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