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P60422

- RL2_ECOLI

UniProt

P60422 - RL2_ECOLI

Protein

50S ribosomal protein L2

Gene

rplB

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 127 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.
    In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. rRNA binding Source: UniProtKB-HAMAP
    3. structural constituent of ribosome Source: InterPro
    4. transferase activity Source: InterPro
    5. zinc ion binding Source: EcoliWiki

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10865-MONOMER.
    ECOL316407:JW3279-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L2
    Gene namesi
    Name:rplB
    Ordered Locus Names:b3317, JW3279
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10865. rplB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi230 – 2301H → Q: Loss of peptidyltransferase activity in reconstituted ribosomes. No change in rRNA binding or assembly into ribosomes. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 27327250S ribosomal protein L2PRO_0000129559Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei242 – 2421N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP60422.
    PRIDEiP60422.

    Expressioni

    Gene expression databases

    GenevestigatoriP60422.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Interacts weakly with S6 in one of the 3.5 A resolved structures.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    dnaAP030044EBI-543515,EBI-548951
    gspEP457592EBI-543515,EBI-1132437
    metGP009592EBI-543515,EBI-909268
    rpoAP0A7Z45EBI-543515,EBI-544985

    Protein-protein interaction databases

    BioGridi852132. 1 interaction.
    DIPiDIP-35747N.
    IntActiP60422. 362 interactions.
    MINTiMINT-1322809.
    STRINGi511145.b3317.

    Structurei

    Secondary structure

    1
    273
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi8 – 103
    Turni11 – 155
    Beta strandi17 – 193
    Beta strandi22 – 243
    Helixi31 – 333
    Beta strandi34 – 363
    Beta strandi47 – 493
    Beta strandi51 – 544
    Beta strandi61 – 633
    Beta strandi72 – 743
    Beta strandi76 – 783
    Beta strandi80 – 823
    Beta strandi87 – 893
    Beta strandi91 – 933
    Beta strandi96 – 994
    Beta strandi101 – 1055
    Beta strandi107 – 1093
    Beta strandi112 – 1154
    Beta strandi116 – 1227
    Beta strandi125 – 1273
    Beta strandi129 – 1313
    Helixi132 – 1343
    Beta strandi142 – 1443
    Beta strandi145 – 1473
    Turni148 – 1503
    Beta strandi157 – 1593
    Beta strandi163 – 1664
    Beta strandi169 – 1713
    Beta strandi172 – 1754
    Beta strandi177 – 1793
    Beta strandi181 – 1844
    Beta strandi186 – 1883
    Beta strandi189 – 1913
    Helixi199 – 2024
    Helixi208 – 2125
    Turni213 – 2153
    Helixi222 – 2243
    Turni227 – 2293
    Beta strandi230 – 2323
    Beta strandi236 – 2383
    Beta strandi245 – 2484
    Beta strandi251 – 2544
    Beta strandi258 – 2603
    Beta strandi261 – 2633
    Helixi264 – 2663
    Beta strandi267 – 2693

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P85electron microscopy12.30A2-273[»]
    1P86electron microscopy11.50A2-273[»]
    1VS6X-ray3.46C1-273[»]
    1VS8X-ray3.46C1-273[»]
    1VT2X-ray3.30C1-273[»]
    2AW4X-ray3.46C1-273[»]
    2AWBX-ray3.46C1-273[»]
    2GYAelectron microscopy15.00A39-265[»]
    2GYCelectron microscopy15.00A39-265[»]
    2I2TX-ray3.22C2-273[»]
    2I2VX-ray3.22C2-273[»]
    2J28electron microscopy8.00C4-270[»]
    2QAMX-ray3.21C2-273[»]
    2QAOX-ray3.21C2-273[»]
    2QBAX-ray3.54C2-273[»]
    2QBCX-ray3.54C2-273[»]
    2QBEX-ray3.30C2-273[»]
    2QBGX-ray3.30C2-273[»]
    2QBIX-ray4.00C2-273[»]
    2QBKX-ray4.00C2-273[»]
    2QOVX-ray3.93C2-273[»]
    2QOXX-ray3.93C2-273[»]
    2QOZX-ray3.50C2-273[»]
    2QP1X-ray3.50C2-273[»]
    2RDOelectron microscopy9.10C2-273[»]
    2VHMX-ray3.74C1-273[»]
    2VHNX-ray3.74C1-273[»]
    2WWQelectron microscopy5.80C2-272[»]
    2Z4LX-ray4.45C2-273[»]
    2Z4NX-ray4.45C2-273[»]
    3BBXelectron microscopy10.00C1-273[»]
    3DF2X-ray3.50C1-273[»]
    3DF4X-ray3.50C1-273[»]
    3E1Belectron microscopy-N1-270[»]
    3E1Delectron microscopy-N1-270[»]
    3FIKelectron microscopy6.70C2-272[»]
    3I1NX-ray3.19C1-273[»]
    3I1PX-ray3.19C1-273[»]
    3I1RX-ray3.81C1-273[»]
    3I1TX-ray3.81C1-273[»]
    3I20X-ray3.71C1-273[»]
    3I22X-ray3.71C1-273[»]
    3IZTelectron microscopy-D1-273[»]
    3IZUelectron microscopy-D1-273[»]
    3J01electron microscopy-62-273[»]
    3J0Telectron microscopy12.10D2-273[»]
    3J0Welectron microscopy14.70D2-273[»]
    3J0Yelectron microscopy13.50D2-273[»]
    3J11electron microscopy13.10D2-273[»]
    3J12electron microscopy11.50D2-273[»]
    3J14electron microscopy11.50D2-273[»]
    3J19electron microscopy8.30C2-272[»]
    3J37electron microscopy9.80D2-273[»]
    3J4Xelectron microscopy12.00C1-272[»]
    3J50electron microscopy20.00C1-272[»]
    3J51electron microscopy17.00C1-272[»]
    3J52electron microscopy12.00C1-272[»]
    3J54electron microscopy13.00C1-272[»]
    3J56electron microscopy15.00C1-272[»]
    3J58electron microscopy17.00C1-272[»]
    3J5Aelectron microscopy12.00C1-272[»]
    3J5Celectron microscopy17.00C1-272[»]
    3J5Eelectron microscopy17.00C1-272[»]
    3J5Gelectron microscopy20.00C1-272[»]
    3J5Ielectron microscopy15.00C1-272[»]
    3J5Kelectron microscopy9.00C1-272[»]
    3J5Lelectron microscopy6.60C2-272[»]
    3J5Oelectron microscopy6.80C1-273[»]
    3J5Uelectron microscopy7.60D2-273[»]
    3J5Welectron microscopy7.60D2-273[»]
    3KCRelectron microscopy-61-273[»]
    3OASX-ray3.25C2-272[»]
    3OATX-ray3.25C2-272[»]
    3OFCX-ray3.19C2-272[»]
    3OFDX-ray3.19C2-272[»]
    3OFQX-ray3.10C2-272[»]
    3OFRX-ray3.10C2-272[»]
    3OFZX-ray3.29C2-272[»]
    3OG0X-ray3.29C2-272[»]
    3ORBX-ray3.30C1-273[»]
    3R8SX-ray3.00C2-272[»]
    3R8TX-ray3.00C2-272[»]
    3SGFX-ray3.20C1-273[»]
    3UOSX-ray3.70C1-273[»]
    487Delectron microscopy7.50I62-172[»]
    4CSUelectron microscopy5.50C2-273[»]
    4GARX-ray3.30C1-273[»]
    4GAUX-ray3.30C1-273[»]
    4KIXX-ray2.90C1-273[»]
    4KIZX-ray2.90C1-273[»]
    4KJ1X-ray2.90C1-273[»]
    4KJ3X-ray2.90C1-273[»]
    4KJ5X-ray2.90C1-273[»]
    4KJ7X-ray2.90C1-273[»]
    4KJ9X-ray2.90C1-273[»]
    4KJBX-ray2.90C1-273[»]
    ProteinModelPortaliP60422.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60422.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L2P family.Curated

    Phylogenomic databases

    eggNOGiCOG0090.
    HOGENOMiHOG000232982.
    KOiK02886.
    OMAiSAMNPID.
    OrthoDBiEOG6TR0J1.
    PhylomeDBiP60422.

    Family and domain databases

    Gene3Di2.30.30.30. 1 hit.
    2.40.50.140. 1 hit.
    4.10.950.10. 1 hit.
    HAMAPiMF_01320_B. Ribosomal_L2_B.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR022666. Rbsml_prot_L2_RNA-bd_dom.
    IPR014722. Rib_L2_dom2.
    IPR002171. Ribosomal_L2.
    IPR005880. Ribosomal_L2_bac/org-type.
    IPR022669. Ribosomal_L2_C.
    IPR022671. Ribosomal_L2_CS.
    IPR014726. Ribosomal_L2_dom3.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view]
    PANTHERiPTHR13691. PTHR13691. 1 hit.
    PTHR13691:SF5. PTHR13691:SF5. 1 hit.
    PfamiPF00181. Ribosomal_L2. 1 hit.
    PF03947. Ribosomal_L2_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
    SUPFAMiSSF50104. SSF50104. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
    PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P60422-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVVKCKPTS PGRRHVVKVV NPELHKGKPF APLLEKNSKS GGRNNNGRIT    50
    TRHIGGGHKQ AYRIVDFKRN KDGIPAVVER LEYDPNRSAN IALVLYKDGE 100
    RRYILAPKGL KAGDQIQSGV DAAIKPGNTL PMRNIPVGST VHNVEMKPGK 150
    GGQLARSAGT YVQIVARDGA YVTLRLRSGE MRKVEADCRA TLGEVGNAEH 200
    MLRVLGKAGA ARWRGVRPTV RGTAMNPVDH PHGGGEGRNF GKHPVTPWGV 250
    QTKGKKTRSN KRTDKFIVRR RSK 273
    Length:273
    Mass (Da):29,860
    Last modified:January 23, 2007 - v2
    Checksum:i1010BDE8D8C68B9B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti232 – 2354HGGG → GGGH AA sequence 1 PublicationCurated

    Mass spectrometryi

    Molecular mass is 29732.3 Da from positions 2 - 273. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26463.1.
    U18997 Genomic DNA. Translation: AAA58114.1.
    U00096 Genomic DNA. Translation: AAC76342.1.
    AP009048 Genomic DNA. Translation: BAE77974.1.
    PIRiE23129. R5EC2.
    RefSeqiNP_417776.1. NC_000913.3.
    YP_492115.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76342; AAC76342; b3317.
    BAE77974; BAE77974; BAE77974.
    GeneIDi12932295.
    947820.
    KEGGiecj:Y75_p3859.
    eco:b3317.
    PATRICi32122066. VBIEscCol129921_3410.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26463.1 .
    U18997 Genomic DNA. Translation: AAA58114.1 .
    U00096 Genomic DNA. Translation: AAC76342.1 .
    AP009048 Genomic DNA. Translation: BAE77974.1 .
    PIRi E23129. R5EC2.
    RefSeqi NP_417776.1. NC_000913.3.
    YP_492115.1. 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 A 2-273 [» ]
    1P86 electron microscopy 11.50 A 2-273 [» ]
    1VS6 X-ray 3.46 C 1-273 [» ]
    1VS8 X-ray 3.46 C 1-273 [» ]
    1VT2 X-ray 3.30 C 1-273 [» ]
    2AW4 X-ray 3.46 C 1-273 [» ]
    2AWB X-ray 3.46 C 1-273 [» ]
    2GYA electron microscopy 15.00 A 39-265 [» ]
    2GYC electron microscopy 15.00 A 39-265 [» ]
    2I2T X-ray 3.22 C 2-273 [» ]
    2I2V X-ray 3.22 C 2-273 [» ]
    2J28 electron microscopy 8.00 C 4-270 [» ]
    2QAM X-ray 3.21 C 2-273 [» ]
    2QAO X-ray 3.21 C 2-273 [» ]
    2QBA X-ray 3.54 C 2-273 [» ]
    2QBC X-ray 3.54 C 2-273 [» ]
    2QBE X-ray 3.30 C 2-273 [» ]
    2QBG X-ray 3.30 C 2-273 [» ]
    2QBI X-ray 4.00 C 2-273 [» ]
    2QBK X-ray 4.00 C 2-273 [» ]
    2QOV X-ray 3.93 C 2-273 [» ]
    2QOX X-ray 3.93 C 2-273 [» ]
    2QOZ X-ray 3.50 C 2-273 [» ]
    2QP1 X-ray 3.50 C 2-273 [» ]
    2RDO electron microscopy 9.10 C 2-273 [» ]
    2VHM X-ray 3.74 C 1-273 [» ]
    2VHN X-ray 3.74 C 1-273 [» ]
    2WWQ electron microscopy 5.80 C 2-272 [» ]
    2Z4L X-ray 4.45 C 2-273 [» ]
    2Z4N X-ray 4.45 C 2-273 [» ]
    3BBX electron microscopy 10.00 C 1-273 [» ]
    3DF2 X-ray 3.50 C 1-273 [» ]
    3DF4 X-ray 3.50 C 1-273 [» ]
    3E1B electron microscopy - N 1-270 [» ]
    3E1D electron microscopy - N 1-270 [» ]
    3FIK electron microscopy 6.70 C 2-272 [» ]
    3I1N X-ray 3.19 C 1-273 [» ]
    3I1P X-ray 3.19 C 1-273 [» ]
    3I1R X-ray 3.81 C 1-273 [» ]
    3I1T X-ray 3.81 C 1-273 [» ]
    3I20 X-ray 3.71 C 1-273 [» ]
    3I22 X-ray 3.71 C 1-273 [» ]
    3IZT electron microscopy - D 1-273 [» ]
    3IZU electron microscopy - D 1-273 [» ]
    3J01 electron microscopy - 6 2-273 [» ]
    3J0T electron microscopy 12.10 D 2-273 [» ]
    3J0W electron microscopy 14.70 D 2-273 [» ]
    3J0Y electron microscopy 13.50 D 2-273 [» ]
    3J11 electron microscopy 13.10 D 2-273 [» ]
    3J12 electron microscopy 11.50 D 2-273 [» ]
    3J14 electron microscopy 11.50 D 2-273 [» ]
    3J19 electron microscopy 8.30 C 2-272 [» ]
    3J37 electron microscopy 9.80 D 2-273 [» ]
    3J4X electron microscopy 12.00 C 1-272 [» ]
    3J50 electron microscopy 20.00 C 1-272 [» ]
    3J51 electron microscopy 17.00 C 1-272 [» ]
    3J52 electron microscopy 12.00 C 1-272 [» ]
    3J54 electron microscopy 13.00 C 1-272 [» ]
    3J56 electron microscopy 15.00 C 1-272 [» ]
    3J58 electron microscopy 17.00 C 1-272 [» ]
    3J5A electron microscopy 12.00 C 1-272 [» ]
    3J5C electron microscopy 17.00 C 1-272 [» ]
    3J5E electron microscopy 17.00 C 1-272 [» ]
    3J5G electron microscopy 20.00 C 1-272 [» ]
    3J5I electron microscopy 15.00 C 1-272 [» ]
    3J5K electron microscopy 9.00 C 1-272 [» ]
    3J5L electron microscopy 6.60 C 2-272 [» ]
    3J5O electron microscopy 6.80 C 1-273 [» ]
    3J5U electron microscopy 7.60 D 2-273 [» ]
    3J5W electron microscopy 7.60 D 2-273 [» ]
    3KCR electron microscopy - 6 1-273 [» ]
    3OAS X-ray 3.25 C 2-272 [» ]
    3OAT X-ray 3.25 C 2-272 [» ]
    3OFC X-ray 3.19 C 2-272 [» ]
    3OFD X-ray 3.19 C 2-272 [» ]
    3OFQ X-ray 3.10 C 2-272 [» ]
    3OFR X-ray 3.10 C 2-272 [» ]
    3OFZ X-ray 3.29 C 2-272 [» ]
    3OG0 X-ray 3.29 C 2-272 [» ]
    3ORB X-ray 3.30 C 1-273 [» ]
    3R8S X-ray 3.00 C 2-272 [» ]
    3R8T X-ray 3.00 C 2-272 [» ]
    3SGF X-ray 3.20 C 1-273 [» ]
    3UOS X-ray 3.70 C 1-273 [» ]
    487D electron microscopy 7.50 I 62-172 [» ]
    4CSU electron microscopy 5.50 C 2-273 [» ]
    4GAR X-ray 3.30 C 1-273 [» ]
    4GAU X-ray 3.30 C 1-273 [» ]
    4KIX X-ray 2.90 C 1-273 [» ]
    4KIZ X-ray 2.90 C 1-273 [» ]
    4KJ1 X-ray 2.90 C 1-273 [» ]
    4KJ3 X-ray 2.90 C 1-273 [» ]
    4KJ5 X-ray 2.90 C 1-273 [» ]
    4KJ7 X-ray 2.90 C 1-273 [» ]
    4KJ9 X-ray 2.90 C 1-273 [» ]
    4KJB X-ray 2.90 C 1-273 [» ]
    ProteinModelPortali P60422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 852132. 1 interaction.
    DIPi DIP-35747N.
    IntActi P60422. 362 interactions.
    MINTi MINT-1322809.
    STRINGi 511145.b3317.

    Chemistry

    ChEMBLi CHEMBL2363135.

    Proteomic databases

    PaxDbi P60422.
    PRIDEi P60422.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76342 ; AAC76342 ; b3317 .
    BAE77974 ; BAE77974 ; BAE77974 .
    GeneIDi 12932295.
    947820.
    KEGGi ecj:Y75_p3859.
    eco:b3317.
    PATRICi 32122066. VBIEscCol129921_3410.

    Organism-specific databases

    EchoBASEi EB0858.
    EcoGenei EG10865. rplB.

    Phylogenomic databases

    eggNOGi COG0090.
    HOGENOMi HOG000232982.
    KOi K02886.
    OMAi SAMNPID.
    OrthoDBi EOG6TR0J1.
    PhylomeDBi P60422.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10865-MONOMER.
    ECOL316407:JW3279-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P60422.
    PROi P60422.

    Gene expression databases

    Genevestigatori P60422.

    Family and domain databases

    Gene3Di 2.30.30.30. 1 hit.
    2.40.50.140. 1 hit.
    4.10.950.10. 1 hit.
    HAMAPi MF_01320_B. Ribosomal_L2_B.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR022666. Rbsml_prot_L2_RNA-bd_dom.
    IPR014722. Rib_L2_dom2.
    IPR002171. Ribosomal_L2.
    IPR005880. Ribosomal_L2_bac/org-type.
    IPR022669. Ribosomal_L2_C.
    IPR022671. Ribosomal_L2_CS.
    IPR014726. Ribosomal_L2_dom3.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view ]
    PANTHERi PTHR13691. PTHR13691. 1 hit.
    PTHR13691:SF5. PTHR13691:SF5. 1 hit.
    Pfami PF00181. Ribosomal_L2. 1 hit.
    PF03947. Ribosomal_L2_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002158. Ribosomal_L2. 1 hit.
    SUPFAMi SSF50104. SSF50104. 1 hit.
    SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR01171. rplB_bact. 1 hit.
    PROSITEi PS00467. RIBOSOMAL_L2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the Escherichia coli S10 ribosomal protein operon."
      Zurawski G., Zurawski S.M.
      Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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. "The primary structure of protein L2 from the Escherichia coli ribosome."
      Kimura M., Mende L., Wittmann-Liebold B.
      FEBS Lett. 149:304-312(1982)
      Cited for: PROTEIN SEQUENCE OF 2-273.
    5. "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 60-71 AND 200-208, CROSS-LINKING TO RRNA.
      Strain: MRE-600.
    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. "Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity."
      Cooperman B.S., Wooten T., Romero D.P., Traut R.R.
      Biochem. Cell Biol. 73:1087-1094(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-230.
    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. "Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies."
      Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.
      Biochem. J. 331:423-430(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN REPLACEMENT STUDIES.
    10. "Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer."
      Diedrich G., Spahn C.M.T., Stelzl U., Schaefer M.A., Wooten T., Bochkariov D.E., Cooperman B.S., Traut R.R., Nierhaus K.H.
      EMBO J. 19:5241-5250(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REQUIREMENT FOR 70S RIBOSOME FORMATION, TRNA-BINDING, MUTAGENESIS OF CONSERVED RESIDUES.
    11. "Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome."
      Willumeit R., Forthmann S., Beckmann J., Diedrich G., Ratering R., Stuhrmann H.B., Nierhaus K.H.
      J. Mol. Biol. 305:167-177(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSITION IN THE 50S SUBUNIT AND 70S RIBOSOME.
      Strain: MRE-600.
    12. "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.
    13. "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-242, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    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.
    15. "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), INTERSUBUNIT BRIDGE FORMATION.
      Strain: MRE-600.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL2_ECOLI
    AccessioniPrimary (citable) accession number: P60422
    Secondary accession number(s): P02387, Q2M6Y2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    This protein can be partially replaced in vivo by its H.marismortui (HmaL2) or human (L8, from the 60S cytoplasmic ribosome) homolog.

    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