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P0A7L0

- RL1_ECOLI

UniProt

P0A7L0 - RL1_ECOLI

Protein

50S ribosomal protein L1

Gene

rplA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    One of the primary rRNA binding proteins, it binds very close to the 3'-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 20 angstroms (PubMed:12859903). This stalk movement is thought to be coupled to movement of deacylated tRNA into and out of the E site, and thus to participate in tRNA translocation (PubMed:12859903). Contacts the P and E site tRNAs.1 Publication
    Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. rRNA binding Source: UniProtKB-HAMAP
    3. structural constituent of ribosome Source: InterPro
    4. tRNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. negative regulation of translational initiation Source: EcoCyc
    2. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Repressor, Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Translation regulation

    Keywords - Ligandi

    RNA-binding, rRNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10864-MONOMER.
    ECOL316407:JW3947-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L1
    Gene namesi
    Name:rplA
    Ordered Locus Names:b3984, JW3947
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10864. rplA.

    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 – 23423350S ribosomal protein L1PRO_0000125654Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051N6-succinyllysine1 Publication
    Modified residuei154 – 1541N6-succinyllysine1 Publication
    Modified residuei186 – 1861N6-succinyllysine1 Publication
    Modified residuei197 – 1971N6-succinyllysine1 Publication

    Proteomic databases

    PaxDbiP0A7L0.
    PRIDEiP0A7L0.

    2D gel databases

    SWISS-2DPAGEP0A7L0.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A7L0.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    cspGP0A9782EBI-543771,EBI-547581
    thrSP0A8M32EBI-543771,EBI-551254

    Protein-protein interaction databases

    DIPiDIP-35746N.
    IntActiP0A7L0. 125 interactions.
    MINTiMINT-1268287.
    STRINGi511145.b3984.

    Structurei

    Secondary structure

    1
    234
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni6 – 105
    Beta strandi11 – 144
    Helixi22 – 276
    Beta strandi30 – 323
    Beta strandi35 – 373
    Beta strandi45 – 473
    Turni54 – 563
    Beta strandi74 – 774
    Helixi82 – 898
    Beta strandi92 – 954
    Helixi99 – 1057
    Beta strandi111 – 1155
    Helixi117 – 1193
    Helixi120 – 1256
    Helixi127 – 1304
    Turni131 – 1344
    Turni139 – 1424
    Helixi148 – 1547
    Beta strandi162 – 1643
    Beta strandi168 – 1703
    Helixi181 – 19616
    Beta strandi207 – 2115
    Beta strandi214 – 2174

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EG0electron microscopy11.50N1-229[»]
    1ML5electron microscopy14.00c2-229[»]
    2GYAelectron microscopy15.0026-227[»]
    2GYCelectron microscopy15.0026-227[»]
    2RDOelectron microscopy9.1092-234[»]
    2WWQelectron microscopy5.8051-234[»]
    3E1Belectron microscopy9.00Z131-224[»]
    3E1Delectron microscopy9.00Z131-224[»]
    3FIKelectron microscopy6.7051-234[»]
    3IZTelectron microscopy-C1-234[»]
    3IZUelectron microscopy-C1-234[»]
    3J01electron microscopy-51-234[»]
    3J0Telectron microscopy12.10C1-234[»]
    3J0Welectron microscopy14.70C1-234[»]
    3J0Yelectron microscopy13.50C1-234[»]
    3J11electron microscopy13.10C1-234[»]
    3J12electron microscopy11.50C1-234[»]
    3J14electron microscopy11.50C1-234[»]
    3J37electron microscopy9.80C1-234[»]
    3J46electron microscopy10.1051-234[»]
    3J4Xelectron microscopy12.0051-234[»]
    3J50electron microscopy20.0051-234[»]
    3J51electron microscopy17.0051-234[»]
    3J52electron microscopy12.0051-234[»]
    3J54electron microscopy13.0051-234[»]
    3J56electron microscopy15.0051-234[»]
    3J58electron microscopy17.0051-234[»]
    3J5Aelectron microscopy12.0051-234[»]
    3J5Celectron microscopy17.0051-234[»]
    3J5Eelectron microscopy17.0051-234[»]
    3J5Gelectron microscopy20.0051-234[»]
    3J5Ielectron microscopy15.0051-234[»]
    3J5Kelectron microscopy9.0051-234[»]
    3J5Selectron microscopy7.50F1-234[»]
    3J5Uelectron microscopy7.60C2-234[»]
    3J5Welectron microscopy7.60C2-234[»]
    3KCRelectron microscopy-51-234[»]
    487Delectron microscopy7.50H29-201[»]
    4CSUelectron microscopy5.5051-234[»]
    ProteinModelPortaliP0A7L0.
    SMRiP0A7L0. Positions 1-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7L0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L1P family.Curated

    Phylogenomic databases

    eggNOGiCOG0081.
    HOGENOMiHOG000207015.
    KOiK02863.
    OMAiVDSTKQY.
    OrthoDBiEOG6FBX2G.
    PhylomeDBiP0A7L0.

    Family and domain databases

    Gene3Di3.30.190.20. 2 hits.
    3.40.50.790. 1 hit.
    HAMAPiMF_01318_B. Ribosomal_L1_B.
    InterProiIPR005878. Ribosom_L1_bac-type.
    IPR002143. Ribosomal_L1.
    IPR023674. Ribosomal_L1-like.
    IPR028364. Ribosomal_L1/biogenesis.
    IPR016094. Ribosomal_L1_2-a/b-sand.
    IPR016095. Ribosomal_L1_3-a/b-sand.
    IPR023673. Ribosomal_L1_CS.
    [Graphical view]
    PfamiPF00687. Ribosomal_L1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002155. Ribosomal_L1. 1 hit.
    SUPFAMiSSF56808. SSF56808. 1 hit.
    TIGRFAMsiTIGR01169. rplA_bact. 1 hit.
    PROSITEiPS01199. RIBOSOMAL_L1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7L0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKLTKRMRV IREKVDATKQ YDINEAIALL KELATAKFVE SVDVAVNLGI    50
    DARKSDQNVR GATVLPHGTG RSVRVAVFTQ GANAEAAKAA GAELVGMEDL 100
    ADQIKKGEMN FDVVIASPDA MRVVGQLGQV LGPRGLMPNP KVGTVTPNVA 150
    EAVKNAKAGQ VRYRNDKNGI IHTTIGKVDF DADKLKENLE ALLVALKKAK 200
    PTQAKGVYIK KVSISTTMGA GVAVDQAGLS ASVN 234
    Length:234
    Mass (Da):24,730
    Last modified:January 23, 2007 - v2
    Checksum:iD751704B34748D53
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121R → I AA sequence (PubMed:9298646)Curated

    Mass spectrometryi

    Molecular mass is 24598.9 Da from positions 2 - 234. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00339 Genomic DNA. Translation: CAA23622.1.
    U00006 Genomic DNA. Translation: AAC43082.1.
    U00096 Genomic DNA. Translation: AAC76958.1.
    AP009048 Genomic DNA. Translation: BAE77336.1.
    PIRiS12573. R5EC1.
    RefSeqiNP_418411.1. NC_000913.3.
    YP_491477.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76958; AAC76958; b3984.
    BAE77336; BAE77336; BAE77336.
    GeneIDi12930515.
    948483.
    KEGGiecj:Y75_p3213.
    eco:b3984.
    PATRICi32123489. VBIEscCol129921_4097.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V00339 Genomic DNA. Translation: CAA23622.1 .
    U00006 Genomic DNA. Translation: AAC43082.1 .
    U00096 Genomic DNA. Translation: AAC76958.1 .
    AP009048 Genomic DNA. Translation: BAE77336.1 .
    PIRi S12573. R5EC1.
    RefSeqi NP_418411.1. NC_000913.3.
    YP_491477.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EG0 electron microscopy 11.50 N 1-229 [» ]
    1ML5 electron microscopy 14.00 c 2-229 [» ]
    2GYA electron microscopy 15.00 2 6-227 [» ]
    2GYC electron microscopy 15.00 2 6-227 [» ]
    2RDO electron microscopy 9.10 9 2-234 [» ]
    2WWQ electron microscopy 5.80 5 1-234 [» ]
    3E1B electron microscopy 9.00 Z 131-224 [» ]
    3E1D electron microscopy 9.00 Z 131-224 [» ]
    3FIK electron microscopy 6.70 5 1-234 [» ]
    3IZT electron microscopy - C 1-234 [» ]
    3IZU electron microscopy - C 1-234 [» ]
    3J01 electron microscopy - 5 1-234 [» ]
    3J0T electron microscopy 12.10 C 1-234 [» ]
    3J0W electron microscopy 14.70 C 1-234 [» ]
    3J0Y electron microscopy 13.50 C 1-234 [» ]
    3J11 electron microscopy 13.10 C 1-234 [» ]
    3J12 electron microscopy 11.50 C 1-234 [» ]
    3J14 electron microscopy 11.50 C 1-234 [» ]
    3J37 electron microscopy 9.80 C 1-234 [» ]
    3J46 electron microscopy 10.10 5 1-234 [» ]
    3J4X electron microscopy 12.00 5 1-234 [» ]
    3J50 electron microscopy 20.00 5 1-234 [» ]
    3J51 electron microscopy 17.00 5 1-234 [» ]
    3J52 electron microscopy 12.00 5 1-234 [» ]
    3J54 electron microscopy 13.00 5 1-234 [» ]
    3J56 electron microscopy 15.00 5 1-234 [» ]
    3J58 electron microscopy 17.00 5 1-234 [» ]
    3J5A electron microscopy 12.00 5 1-234 [» ]
    3J5C electron microscopy 17.00 5 1-234 [» ]
    3J5E electron microscopy 17.00 5 1-234 [» ]
    3J5G electron microscopy 20.00 5 1-234 [» ]
    3J5I electron microscopy 15.00 5 1-234 [» ]
    3J5K electron microscopy 9.00 5 1-234 [» ]
    3J5S electron microscopy 7.50 F 1-234 [» ]
    3J5U electron microscopy 7.60 C 2-234 [» ]
    3J5W electron microscopy 7.60 C 2-234 [» ]
    3KCR electron microscopy - 5 1-234 [» ]
    487D electron microscopy 7.50 H 29-201 [» ]
    4CSU electron microscopy 5.50 5 1-234 [» ]
    ProteinModelPortali P0A7L0.
    SMRi P0A7L0. Positions 1-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35746N.
    IntActi P0A7L0. 125 interactions.
    MINTi MINT-1268287.
    STRINGi 511145.b3984.

    Chemistry

    ChEMBLi CHEMBL2363135.

    2D gel databases

    SWISS-2DPAGE P0A7L0.

    Proteomic databases

    PaxDbi P0A7L0.
    PRIDEi P0A7L0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76958 ; AAC76958 ; b3984 .
    BAE77336 ; BAE77336 ; BAE77336 .
    GeneIDi 12930515.
    948483.
    KEGGi ecj:Y75_p3213.
    eco:b3984.
    PATRICi 32123489. VBIEscCol129921_4097.

    Organism-specific databases

    EchoBASEi EB0857.
    EcoGenei EG10864. rplA.

    Phylogenomic databases

    eggNOGi COG0081.
    HOGENOMi HOG000207015.
    KOi K02863.
    OMAi VDSTKQY.
    OrthoDBi EOG6FBX2G.
    PhylomeDBi P0A7L0.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10864-MONOMER.
    ECOL316407:JW3947-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7L0.
    PROi P0A7L0.

    Gene expression databases

    Genevestigatori P0A7L0.

    Family and domain databases

    Gene3Di 3.30.190.20. 2 hits.
    3.40.50.790. 1 hit.
    HAMAPi MF_01318_B. Ribosomal_L1_B.
    InterProi IPR005878. Ribosom_L1_bac-type.
    IPR002143. Ribosomal_L1.
    IPR023674. Ribosomal_L1-like.
    IPR028364. Ribosomal_L1/biogenesis.
    IPR016094. Ribosomal_L1_2-a/b-sand.
    IPR016095. Ribosomal_L1_3-a/b-sand.
    IPR023673. Ribosomal_L1_CS.
    [Graphical view ]
    Pfami PF00687. Ribosomal_L1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002155. Ribosomal_L1. 1 hit.
    SUPFAMi SSF56808. SSF56808. 1 hit.
    TIGRFAMsi TIGR01169. rplA_bact. 1 hit.
    PROSITEi PS01199. RIBOSOMAL_L1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the ribosomal protein gene cluster adjacent to the gene for RNA polymerase subunit beta in Escherichia coli."
      Post L.E., Strycharz G.D., Nomura M., Lewis H., Dennis P.P.
      Proc. Natl. Acad. Sci. U.S.A. 76:1697-1701(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
      Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
      Nucleic Acids Res. 21:5408-5417(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. "The primary structure of protein L1 from the large ribosomal subunit of Escherichia coli."
      Brauer D., Oechsner I.
      FEBS Lett. 96:317-321(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-234.
      Strain: K.
    6. Erratum
      Brauer D., Oechsner I.
      FEBS Lett. 98:411-411(1979)
    7. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    8. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
      Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
      EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 199-203, CROSS-LINKING TO RRNA.
      Strain: MRE-600.
    9. "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.
    10. "Translational regulation of the L11 ribosomal protein operon of Escherichia coli: mutations that define the target site for repression by L1."
      Thomas M.S., Nomura M.
      Nucleic Acids Res. 15:3085-3096(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: MECHANISM OF TRANSLATION REGULATION.
      Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
    11. "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.
    12. "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.
    13. "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.
    14. "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
      Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
      J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.
      Strain: MRE-600.
    15. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION AT LYS-105; LYS-154; LYS-186 AND LYS-197.
      Strain: K12.
    16. Cited for: 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES IMPLYING THE INVOLVEMENT OF THE L1 STALK IN TRANSLOCATION OF TRNAS FROM THE P TO E SITE.
    17. Cited for: LOCALIZATION IN THE 3.5 ANGSTROM RIBOSOMAL STRUCTURES AND DISCUSSION OF ITS MOVEMENT.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL1_ECOLI
    AccessioniPrimary (citable) accession number: P0A7L0
    Secondary accession number(s): P02384, Q2M8S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 96 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