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P0ADY7

- RL16_ECOLI

UniProt

P0ADY7 - RL16_ECOLI

Protein

50S ribosomal protein L16

Gene

rplP

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

    This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs. It has an essential role in subunit assembly, which is not well understood.

    GO - Molecular functioni

    1. rRNA binding Source: EcoCyc
    2. structural constituent of ribosome Source: InterPro
    3. tRNA binding Source: EcoCyc

    GO - Biological processi

    1. translation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    RNA-binding, rRNA-binding, tRNA-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10877-MONOMER.
    ECOL316407:JW3275-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L16
    Gene namesi
    Name:rplP
    Ordered Locus Names:b3313, JW3275
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10877. rplP.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosolic large ribosomal subunit Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13613650S ribosomal protein L16PRO_0000062101Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-methylmethionine
    Modified residuei81 – 811(3R)-3-hydroxyarginine1 Publication

    Post-translational modificationi

    Is hydroxylated on Arg-81 by YcfD. The modification is nearly suppressed when E.coli is grown in anoxia.1 Publication

    Keywords - PTMi

    Hydroxylation, Methylation

    Proteomic databases

    PaxDbiP0ADY7.
    PRIDEiP0ADY7.

    PTM databases

    PhosSiteiP0810431.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ADY7.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    DIPiDIP-35976N.
    IntActiP0ADY7. 34 interactions.
    MINTiMINT-1302401.
    STRINGi511145.b3313.

    Structurei

    Secondary structure

    1
    136
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103
    Beta strandi28 – 347
    Beta strandi39 – 424
    Helixi43 – 5715
    Beta strandi59 – 613
    Beta strandi63 – 653
    Beta strandi71 – 755
    Beta strandi82 – 854
    Beta strandi93 – 964
    Beta strandi101 – 1055
    Helixi110 – 12112
    Beta strandi124 – 1263
    Beta strandi129 – 1324

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P85electron microscopy12.30K1-136[»]
    1P86electron microscopy11.50K1-136[»]
    1VS6X-ray3.46M1-136[»]
    1VS8X-ray3.46M1-136[»]
    1VT2X-ray3.30M1-136[»]
    2AW4X-ray3.46M1-136[»]
    2AWBX-ray3.46M1-136[»]
    2GYAelectron microscopy15.00K3-133[»]
    2GYCelectron microscopy15.00K3-133[»]
    2I2TX-ray3.22M1-136[»]
    2I2VX-ray3.22M1-136[»]
    2J28electron microscopy8.00M1-136[»]
    2QAMX-ray3.21M1-136[»]
    2QAOX-ray3.21M1-136[»]
    2QBAX-ray3.54M1-136[»]
    2QBCX-ray3.54M1-136[»]
    2QBEX-ray3.30M1-136[»]
    2QBGX-ray3.30M1-136[»]
    2QBIX-ray4.00M1-136[»]
    2QBKX-ray4.00M1-136[»]
    2QOVX-ray3.93M1-136[»]
    2QOXX-ray3.93M1-136[»]
    2QOZX-ray3.50M1-136[»]
    2QP1X-ray3.50M1-136[»]
    2RDOelectron microscopy9.10M1-136[»]
    2VHMX-ray3.74M1-136[»]
    2VHNX-ray3.74M1-136[»]
    2WWQelectron microscopy5.80M1-136[»]
    2Z4LX-ray4.45M1-136[»]
    2Z4NX-ray4.45M1-136[»]
    3BBXelectron microscopy10.00M1-136[»]
    3E1Belectron microscopy-F1-136[»]
    3E1Delectron microscopy-F1-136[»]
    3FIKelectron microscopy6.70M1-136[»]
    3I1NX-ray3.19M1-136[»]
    3I1PX-ray3.19M1-136[»]
    3I1RX-ray3.81M1-136[»]
    3I1TX-ray3.81M1-136[»]
    3I20X-ray3.71M1-136[»]
    3I22X-ray3.71M1-136[»]
    3IZTelectron microscopy-N1-136[»]
    3IZUelectron microscopy-N1-136[»]
    3J01electron microscopy-M1-136[»]
    3J0Telectron microscopy12.10O1-136[»]
    3J0Welectron microscopy14.70O1-136[»]
    3J0Yelectron microscopy13.50O1-136[»]
    3J11electron microscopy13.10O1-136[»]
    3J12electron microscopy11.50O1-136[»]
    3J14electron microscopy11.50O1-136[»]
    3J19electron microscopy8.30M1-136[»]
    3J37electron microscopy9.80Q1-136[»]
    3J4Xelectron microscopy12.00M1-136[»]
    3J50electron microscopy20.00M1-136[»]
    3J51electron microscopy17.00M1-136[»]
    3J52electron microscopy12.00M1-136[»]
    3J54electron microscopy13.00M1-136[»]
    3J56electron microscopy15.00M1-136[»]
    3J58electron microscopy17.00M1-136[»]
    3J5Aelectron microscopy12.00M1-136[»]
    3J5Celectron microscopy17.00M1-136[»]
    3J5Eelectron microscopy17.00M1-136[»]
    3J5Gelectron microscopy20.00M1-136[»]
    3J5Ielectron microscopy15.00M1-136[»]
    3J5Kelectron microscopy9.00M1-136[»]
    3J5Lelectron microscopy6.60M1-136[»]
    3J5Oelectron microscopy6.80M1-136[»]
    3J5Uelectron microscopy7.60O1-136[»]
    3J5Welectron microscopy7.60P1-136[»]
    3KCRelectron microscopy-M1-136[»]
    3OASX-ray3.25M1-136[»]
    3OATX-ray3.25M1-136[»]
    3OFCX-ray3.19M1-136[»]
    3OFDX-ray3.19M1-136[»]
    3OFQX-ray3.10M1-136[»]
    3OFRX-ray3.10M1-136[»]
    3OFZX-ray3.29M1-136[»]
    3OG0X-ray3.29M1-136[»]
    3ORBX-ray3.30M1-136[»]
    3R8SX-ray3.00M1-136[»]
    3R8TX-ray3.00M1-136[»]
    3SGFX-ray3.20Q1-136[»]
    3UOSX-ray3.70Q1-136[»]
    4CSUelectron microscopy5.50M1-136[»]
    4GARX-ray3.30M1-136[»]
    4GAUX-ray3.30M1-136[»]
    4KIXX-ray2.90M1-136[»]
    4KIZX-ray2.90M1-136[»]
    4KJ1X-ray2.90M1-136[»]
    4KJ3X-ray2.90M1-136[»]
    4KJ5X-ray2.90M1-136[»]
    4KJ7X-ray2.90M1-136[»]
    4KJ9X-ray2.90M1-136[»]
    4KJBX-ray2.90M1-136[»]
    ProteinModelPortaliP0ADY7.
    SMRiP0ADY7. Positions 1-136.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ADY7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L16P family.Curated

    Phylogenomic databases

    eggNOGiCOG0197.
    HOGENOMiHOG000164573.
    KOiK02878.
    OMAiLKTTFVT.
    OrthoDBiEOG6WHNWS.
    PhylomeDBiP0ADY7.

    Family and domain databases

    Gene3Di3.90.1170.10. 1 hit.
    HAMAPiMF_01342. Ribosomal_L16.
    InterProiIPR016180. Ribosomal_L10e/L16.
    IPR000114. Ribosomal_L16.
    IPR020798. Ribosomal_L16_CS.
    [Graphical view]
    PANTHERiPTHR12220. PTHR12220. 1 hit.
    PfamiPF00252. Ribosomal_L16. 1 hit.
    [Graphical view]
    PRINTSiPR00060. RIBOSOMALL16.
    SUPFAMiSSF54686. SSF54686. 1 hit.
    TIGRFAMsiTIGR01164. rplP_bact. 1 hit.
    PROSITEiPS00586. RIBOSOMAL_L16_1. 1 hit.
    PS00701. RIBOSOMAL_L16_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ADY7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLQPKRTKFR KMHKGRNRGL AQGTDVSFGS FGLKAVGRGR LTARQIEAAR    50
    RAMTRAVKRQ GKIWIRVFPD KPITEKPLAV RMGKGKGNVE YWVALIQPGK 100
    VLYEMDGVPE ELAREAFKLA AAKLPIKTTF VTKTVM 136
    Length:136
    Mass (Da):15,281
    Last modified:July 21, 1986 - v1
    Checksum:i445A9B167F7564D1
    GO

    Mass spectrometryi

    Molecular mass is 15326.2 Da from positions 1 - 136. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26467.1.
    U18997 Genomic DNA. Translation: AAA58110.1.
    U00096 Genomic DNA. Translation: AAC76338.1.
    AP009048 Genomic DNA. Translation: BAE77978.1.
    M12490 Genomic DNA. Translation: AAA83901.1.
    PIRiI23129. R5EC16.
    RefSeqiNP_417772.1. NC_000913.3.
    YP_492119.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76338; AAC76338; b3313.
    BAE77978; BAE77978; BAE77978.
    GeneIDi12934115.
    947806.
    KEGGiecj:Y75_p3863.
    eco:b3313.
    PATRICi32122058. VBIEscCol129921_3406.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02613 Genomic DNA. Translation: CAA26467.1 .
    U18997 Genomic DNA. Translation: AAA58110.1 .
    U00096 Genomic DNA. Translation: AAC76338.1 .
    AP009048 Genomic DNA. Translation: BAE77978.1 .
    M12490 Genomic DNA. Translation: AAA83901.1 .
    PIRi I23129. R5EC16.
    RefSeqi NP_417772.1. NC_000913.3.
    YP_492119.1. 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 K 1-136 [» ]
    1P86 electron microscopy 11.50 K 1-136 [» ]
    1VS6 X-ray 3.46 M 1-136 [» ]
    1VS8 X-ray 3.46 M 1-136 [» ]
    1VT2 X-ray 3.30 M 1-136 [» ]
    2AW4 X-ray 3.46 M 1-136 [» ]
    2AWB X-ray 3.46 M 1-136 [» ]
    2GYA electron microscopy 15.00 K 3-133 [» ]
    2GYC electron microscopy 15.00 K 3-133 [» ]
    2I2T X-ray 3.22 M 1-136 [» ]
    2I2V X-ray 3.22 M 1-136 [» ]
    2J28 electron microscopy 8.00 M 1-136 [» ]
    2QAM X-ray 3.21 M 1-136 [» ]
    2QAO X-ray 3.21 M 1-136 [» ]
    2QBA X-ray 3.54 M 1-136 [» ]
    2QBC X-ray 3.54 M 1-136 [» ]
    2QBE X-ray 3.30 M 1-136 [» ]
    2QBG X-ray 3.30 M 1-136 [» ]
    2QBI X-ray 4.00 M 1-136 [» ]
    2QBK X-ray 4.00 M 1-136 [» ]
    2QOV X-ray 3.93 M 1-136 [» ]
    2QOX X-ray 3.93 M 1-136 [» ]
    2QOZ X-ray 3.50 M 1-136 [» ]
    2QP1 X-ray 3.50 M 1-136 [» ]
    2RDO electron microscopy 9.10 M 1-136 [» ]
    2VHM X-ray 3.74 M 1-136 [» ]
    2VHN X-ray 3.74 M 1-136 [» ]
    2WWQ electron microscopy 5.80 M 1-136 [» ]
    2Z4L X-ray 4.45 M 1-136 [» ]
    2Z4N X-ray 4.45 M 1-136 [» ]
    3BBX electron microscopy 10.00 M 1-136 [» ]
    3E1B electron microscopy - F 1-136 [» ]
    3E1D electron microscopy - F 1-136 [» ]
    3FIK electron microscopy 6.70 M 1-136 [» ]
    3I1N X-ray 3.19 M 1-136 [» ]
    3I1P X-ray 3.19 M 1-136 [» ]
    3I1R X-ray 3.81 M 1-136 [» ]
    3I1T X-ray 3.81 M 1-136 [» ]
    3I20 X-ray 3.71 M 1-136 [» ]
    3I22 X-ray 3.71 M 1-136 [» ]
    3IZT electron microscopy - N 1-136 [» ]
    3IZU electron microscopy - N 1-136 [» ]
    3J01 electron microscopy - M 1-136 [» ]
    3J0T electron microscopy 12.10 O 1-136 [» ]
    3J0W electron microscopy 14.70 O 1-136 [» ]
    3J0Y electron microscopy 13.50 O 1-136 [» ]
    3J11 electron microscopy 13.10 O 1-136 [» ]
    3J12 electron microscopy 11.50 O 1-136 [» ]
    3J14 electron microscopy 11.50 O 1-136 [» ]
    3J19 electron microscopy 8.30 M 1-136 [» ]
    3J37 electron microscopy 9.80 Q 1-136 [» ]
    3J4X electron microscopy 12.00 M 1-136 [» ]
    3J50 electron microscopy 20.00 M 1-136 [» ]
    3J51 electron microscopy 17.00 M 1-136 [» ]
    3J52 electron microscopy 12.00 M 1-136 [» ]
    3J54 electron microscopy 13.00 M 1-136 [» ]
    3J56 electron microscopy 15.00 M 1-136 [» ]
    3J58 electron microscopy 17.00 M 1-136 [» ]
    3J5A electron microscopy 12.00 M 1-136 [» ]
    3J5C electron microscopy 17.00 M 1-136 [» ]
    3J5E electron microscopy 17.00 M 1-136 [» ]
    3J5G electron microscopy 20.00 M 1-136 [» ]
    3J5I electron microscopy 15.00 M 1-136 [» ]
    3J5K electron microscopy 9.00 M 1-136 [» ]
    3J5L electron microscopy 6.60 M 1-136 [» ]
    3J5O electron microscopy 6.80 M 1-136 [» ]
    3J5U electron microscopy 7.60 O 1-136 [» ]
    3J5W electron microscopy 7.60 P 1-136 [» ]
    3KCR electron microscopy - M 1-136 [» ]
    3OAS X-ray 3.25 M 1-136 [» ]
    3OAT X-ray 3.25 M 1-136 [» ]
    3OFC X-ray 3.19 M 1-136 [» ]
    3OFD X-ray 3.19 M 1-136 [» ]
    3OFQ X-ray 3.10 M 1-136 [» ]
    3OFR X-ray 3.10 M 1-136 [» ]
    3OFZ X-ray 3.29 M 1-136 [» ]
    3OG0 X-ray 3.29 M 1-136 [» ]
    3ORB X-ray 3.30 M 1-136 [» ]
    3R8S X-ray 3.00 M 1-136 [» ]
    3R8T X-ray 3.00 M 1-136 [» ]
    3SGF X-ray 3.20 Q 1-136 [» ]
    3UOS X-ray 3.70 Q 1-136 [» ]
    4CSU electron microscopy 5.50 M 1-136 [» ]
    4GAR X-ray 3.30 M 1-136 [» ]
    4GAU X-ray 3.30 M 1-136 [» ]
    4KIX X-ray 2.90 M 1-136 [» ]
    4KIZ X-ray 2.90 M 1-136 [» ]
    4KJ1 X-ray 2.90 M 1-136 [» ]
    4KJ3 X-ray 2.90 M 1-136 [» ]
    4KJ5 X-ray 2.90 M 1-136 [» ]
    4KJ7 X-ray 2.90 M 1-136 [» ]
    4KJ9 X-ray 2.90 M 1-136 [» ]
    4KJB X-ray 2.90 M 1-136 [» ]
    ProteinModelPortali P0ADY7.
    SMRi P0ADY7. Positions 1-136.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35976N.
    IntActi P0ADY7. 34 interactions.
    MINTi MINT-1302401.
    STRINGi 511145.b3313.

    Chemistry

    ChEMBLi CHEMBL2363135.

    PTM databases

    PhosSitei P0810431.

    Proteomic databases

    PaxDbi P0ADY7.
    PRIDEi P0ADY7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76338 ; AAC76338 ; b3313 .
    BAE77978 ; BAE77978 ; BAE77978 .
    GeneIDi 12934115.
    947806.
    KEGGi ecj:Y75_p3863.
    eco:b3313.
    PATRICi 32122058. VBIEscCol129921_3406.

    Organism-specific databases

    EchoBASEi EB0870.
    EcoGenei EG10877. rplP.

    Phylogenomic databases

    eggNOGi COG0197.
    HOGENOMi HOG000164573.
    KOi K02878.
    OMAi LKTTFVT.
    OrthoDBi EOG6WHNWS.
    PhylomeDBi P0ADY7.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10877-MONOMER.
    ECOL316407:JW3275-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ADY7.
    PROi P0ADY7.

    Gene expression databases

    Genevestigatori P0ADY7.

    Family and domain databases

    Gene3Di 3.90.1170.10. 1 hit.
    HAMAPi MF_01342. Ribosomal_L16.
    InterProi IPR016180. Ribosomal_L10e/L16.
    IPR000114. Ribosomal_L16.
    IPR020798. Ribosomal_L16_CS.
    [Graphical view ]
    PANTHERi PTHR12220. PTHR12220. 1 hit.
    Pfami PF00252. Ribosomal_L16. 1 hit.
    [Graphical view ]
    PRINTSi PR00060. RIBOSOMALL16.
    SUPFAMi SSF54686. SSF54686. 1 hit.
    TIGRFAMsi TIGR01164. rplP_bact. 1 hit.
    PROSITEi PS00586. RIBOSOMAL_L16_1. 1 hit.
    PS00701. RIBOSOMAL_L16_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of protein L16 located at the peptidyltransferase center of Escherichia coli ribosomes."
      Brosius J., Chen R.
      FEBS Lett. 68:105-109(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Strain: K.
    2. "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].
    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. "DNA sequence of the promoter region for the alpha ribosomal protein operon in Escherichia coli."
      Post L.E., Arfsten A.E., Davis G.R., Nomura M.
      J. Biol. Chem. 255:4653-4659(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-80.
    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. "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.
    8. "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.
    9. "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.
    10. Cited for: HYDROXYLATION AT ARG-81 BY YCFD.
      Strain: K12.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL16_ECOLI
    AccessioniPrimary (citable) accession number: P0ADY7
    Secondary accession number(s): P02414, Q2M6X8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 91 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