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)

P0A7K6

- RL19_ECOLI

UniProt

P0A7K6 - RL19_ECOLI

Protein

50S ribosomal protein L19

Gene

rplS

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

    This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome (PubMed:12809609) it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8. In the 3.5 A resolved structures (PubMed:16272117) L14 and L19 interact and together make contact with the 16S rRNA. The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation.2 Publications

    GO - Molecular functioni

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

    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:EG10880-MONOMER.
    ECOL316407:JW2587-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    50S ribosomal protein L19
    Gene namesi
    Name:rplS
    Ordered Locus Names:b2606, JW2587
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10880. rplS.

    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 – 11511450S ribosomal protein L19PRO_0000163451Add
    BLAST

    Proteomic databases

    PaxDbiP0A7K6.
    PRIDEiP0A7K6.

    PTM databases

    PhosSiteiP0810432.

    Expressioni

    Inductioni

    Part of the rpsP-rimM-trmD-rplS operon.

    Gene expression databases

    GenevestigatoriP0A7K6.

    Interactioni

    Subunit structurei

    Part of the 50S ribosomal subunit. Contacts L14 (PubMed:2665813 and PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    nanEP0A7611EBI-543891,EBI-561432

    Protein-protein interaction databases

    DIPiDIP-35793N.
    IntActiP0A7K6. 101 interactions.
    MINTiMINT-1245288.
    STRINGi511145.b2606.

    Structurei

    Secondary structure

    1
    115
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 107
    Beta strandi27 – 337
    Turni34 – 363
    Beta strandi38 – 447
    Beta strandi46 – 505
    Helixi54 – 563
    Beta strandi58 – 625
    Beta strandi66 – 683
    Beta strandi70 – 756
    Beta strandi76 – 783
    Helixi79 – 813
    Beta strandi83 – 853
    Beta strandi86 – 883
    Beta strandi93 – 953
    Helixi98 – 1025
    Helixi105 – 1073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P85electron microscopy12.30N2-115[»]
    1P86electron microscopy11.50N2-115[»]
    1VS6X-ray3.46P1-115[»]
    1VS8X-ray3.46P1-115[»]
    1VT2X-ray3.30P1-115[»]
    2AW4X-ray3.46P2-115[»]
    2AWBX-ray3.46P2-115[»]
    2GYAelectron microscopy15.00N2-115[»]
    2GYCelectron microscopy15.00N2-115[»]
    2I2TX-ray3.22P2-115[»]
    2I2VX-ray3.22P2-115[»]
    2J28electron microscopy8.00P2-115[»]
    2QAMX-ray3.21P2-115[»]
    2QAOX-ray3.21P2-115[»]
    2QBAX-ray3.54P2-115[»]
    2QBCX-ray3.54P2-115[»]
    2QBEX-ray3.30P2-115[»]
    2QBGX-ray3.30P2-115[»]
    2QBIX-ray4.00P2-115[»]
    2QBKX-ray4.00P2-115[»]
    2QOVX-ray3.93P2-115[»]
    2QOXX-ray3.93P2-115[»]
    2QOZX-ray3.50P2-115[»]
    2QP1X-ray3.50P2-115[»]
    2RDOelectron microscopy9.10P2-115[»]
    2VHMX-ray3.74P2-115[»]
    2VHNX-ray3.74P2-115[»]
    2WWQelectron microscopy5.80P2-115[»]
    2Z4LX-ray4.45P2-115[»]
    2Z4NX-ray4.45P2-115[»]
    3BBXelectron microscopy10.00P2-115[»]
    3DF2X-ray3.50P2-114[»]
    3DF4X-ray3.50P2-114[»]
    3E1Belectron microscopy-I1-115[»]
    3E1Delectron microscopy-I1-115[»]
    3FIKelectron microscopy6.70P2-115[»]
    3I1NX-ray3.19P1-115[»]
    3I1PX-ray3.19P1-115[»]
    3I1RX-ray3.81P1-115[»]
    3I1TX-ray3.81P1-115[»]
    3I20X-ray3.71P1-115[»]
    3I22X-ray3.71P1-115[»]
    3IZTelectron microscopy-Q1-115[»]
    3IZUelectron microscopy-Q1-115[»]
    3J01electron microscopy-P2-115[»]
    3J0Telectron microscopy12.10R2-115[»]
    3J0Welectron microscopy14.70R2-115[»]
    3J0Yelectron microscopy13.50R2-115[»]
    3J11electron microscopy13.10R2-115[»]
    3J12electron microscopy11.50R2-115[»]
    3J14electron microscopy11.50R2-115[»]
    3J19electron microscopy8.30P2-115[»]
    3J37electron microscopy9.80T2-115[»]
    3J4Xelectron microscopy12.00P1-115[»]
    3J50electron microscopy20.00P1-115[»]
    3J51electron microscopy17.00P1-115[»]
    3J52electron microscopy12.00P1-115[»]
    3J54electron microscopy13.00P1-115[»]
    3J56electron microscopy15.00P1-115[»]
    3J58electron microscopy17.00P1-115[»]
    3J5Aelectron microscopy12.00P1-115[»]
    3J5Celectron microscopy17.00P1-115[»]
    3J5Eelectron microscopy17.00P1-115[»]
    3J5Gelectron microscopy20.00P1-115[»]
    3J5Ielectron microscopy15.00P1-115[»]
    3J5Kelectron microscopy9.00P1-115[»]
    3J5Lelectron microscopy6.60P2-115[»]
    3J5Oelectron microscopy6.80P1-115[»]
    3J5Uelectron microscopy7.60R2-115[»]
    3J5Welectron microscopy7.60S2-115[»]
    3KCRelectron microscopy-P1-115[»]
    3OASX-ray3.25P2-115[»]
    3OATX-ray3.25P2-115[»]
    3OFCX-ray3.19P2-115[»]
    3OFDX-ray3.19P2-115[»]
    3OFQX-ray3.10P2-115[»]
    3OFRX-ray3.10P2-115[»]
    3OFZX-ray3.29P2-115[»]
    3OG0X-ray3.29P2-115[»]
    3ORBX-ray3.30P1-115[»]
    3R8SX-ray3.00P2-115[»]
    3R8TX-ray3.00P2-115[»]
    3SGFX-ray3.20T1-115[»]
    3UOSX-ray3.70T1-115[»]
    4CSUelectron microscopy5.50P2-115[»]
    4GARX-ray3.30P1-115[»]
    4GAUX-ray3.30P1-115[»]
    4KIXX-ray2.90P1-115[»]
    4KIZX-ray2.90P1-115[»]
    4KJ1X-ray2.90P1-115[»]
    4KJ3X-ray2.90P1-115[»]
    4KJ5X-ray2.90P1-115[»]
    4KJ7X-ray2.90P1-115[»]
    4KJ9X-ray2.90P1-115[»]
    4KJBX-ray2.90P1-115[»]
    ProteinModelPortaliP0A7K6.
    SMRiP0A7K6. Positions 2-115.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A7K6.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein L19P family.Curated

    Phylogenomic databases

    eggNOGiCOG0335.
    HOGENOMiHOG000016264.
    KOiK02884.
    OMAiGGRERIQ.
    OrthoDBiEOG6DZF5W.
    PhylomeDBiP0A7K6.

    Family and domain databases

    HAMAPiMF_00402. Ribosomal_L19.
    InterProiIPR001857. Ribosomal_L19.
    IPR018257. Ribosomal_L19_CS.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view]
    PANTHERiPTHR15680. PTHR15680. 1 hit.
    PfamiPF01245. Ribosomal_L19. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002191. Ribosomal_L19. 1 hit.
    PRINTSiPR00061. RIBOSOMALL19.
    SUPFAMiSSF50104. SSF50104. 1 hit.
    TIGRFAMsiTIGR01024. rplS_bact. 1 hit.
    PROSITEiPS01015. RIBOSOMAL_L19. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P0A7K6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNIIKQLEQ EQMKQDVPSF RPGDTVEVKV WVVEGSKKRL QAFEGVVIAI    50
    RNRGLHSAFT VRKISNGEGV ERVFQTHSPV VDSISVKRRG AVRKAKLYYL 100
    RERTGKAARI KERLN 115
    Length:115
    Mass (Da):13,133
    Last modified:January 23, 2007 - v2
    Checksum:i7BD9F2EFB9DDB06B
    GO

    Mass spectrometryi

    Molecular mass is 13001.7 Da from positions 2 - 115. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01818 Genomic DNA. Translation: CAA25960.1.
    U00096 Genomic DNA. Translation: AAC75655.1.
    AP009048 Genomic DNA. Translation: BAA16491.1.
    PIRiS07951. R5EC19.
    RefSeqiNP_417097.1. NC_000913.3.
    YP_490829.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75655; AAC75655; b2606.
    BAA16491; BAA16491; BAA16491.
    GeneIDi12931612.
    947096.
    KEGGiecj:Y75_p2554.
    eco:b2606.
    PATRICi32120611. VBIEscCol129921_2704.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01818 Genomic DNA. Translation: CAA25960.1 .
    U00096 Genomic DNA. Translation: AAC75655.1 .
    AP009048 Genomic DNA. Translation: BAA16491.1 .
    PIRi S07951. R5EC19.
    RefSeqi NP_417097.1. NC_000913.3.
    YP_490829.1. 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 N 2-115 [» ]
    1P86 electron microscopy 11.50 N 2-115 [» ]
    1VS6 X-ray 3.46 P 1-115 [» ]
    1VS8 X-ray 3.46 P 1-115 [» ]
    1VT2 X-ray 3.30 P 1-115 [» ]
    2AW4 X-ray 3.46 P 2-115 [» ]
    2AWB X-ray 3.46 P 2-115 [» ]
    2GYA electron microscopy 15.00 N 2-115 [» ]
    2GYC electron microscopy 15.00 N 2-115 [» ]
    2I2T X-ray 3.22 P 2-115 [» ]
    2I2V X-ray 3.22 P 2-115 [» ]
    2J28 electron microscopy 8.00 P 2-115 [» ]
    2QAM X-ray 3.21 P 2-115 [» ]
    2QAO X-ray 3.21 P 2-115 [» ]
    2QBA X-ray 3.54 P 2-115 [» ]
    2QBC X-ray 3.54 P 2-115 [» ]
    2QBE X-ray 3.30 P 2-115 [» ]
    2QBG X-ray 3.30 P 2-115 [» ]
    2QBI X-ray 4.00 P 2-115 [» ]
    2QBK X-ray 4.00 P 2-115 [» ]
    2QOV X-ray 3.93 P 2-115 [» ]
    2QOX X-ray 3.93 P 2-115 [» ]
    2QOZ X-ray 3.50 P 2-115 [» ]
    2QP1 X-ray 3.50 P 2-115 [» ]
    2RDO electron microscopy 9.10 P 2-115 [» ]
    2VHM X-ray 3.74 P 2-115 [» ]
    2VHN X-ray 3.74 P 2-115 [» ]
    2WWQ electron microscopy 5.80 P 2-115 [» ]
    2Z4L X-ray 4.45 P 2-115 [» ]
    2Z4N X-ray 4.45 P 2-115 [» ]
    3BBX electron microscopy 10.00 P 2-115 [» ]
    3DF2 X-ray 3.50 P 2-114 [» ]
    3DF4 X-ray 3.50 P 2-114 [» ]
    3E1B electron microscopy - I 1-115 [» ]
    3E1D electron microscopy - I 1-115 [» ]
    3FIK electron microscopy 6.70 P 2-115 [» ]
    3I1N X-ray 3.19 P 1-115 [» ]
    3I1P X-ray 3.19 P 1-115 [» ]
    3I1R X-ray 3.81 P 1-115 [» ]
    3I1T X-ray 3.81 P 1-115 [» ]
    3I20 X-ray 3.71 P 1-115 [» ]
    3I22 X-ray 3.71 P 1-115 [» ]
    3IZT electron microscopy - Q 1-115 [» ]
    3IZU electron microscopy - Q 1-115 [» ]
    3J01 electron microscopy - P 2-115 [» ]
    3J0T electron microscopy 12.10 R 2-115 [» ]
    3J0W electron microscopy 14.70 R 2-115 [» ]
    3J0Y electron microscopy 13.50 R 2-115 [» ]
    3J11 electron microscopy 13.10 R 2-115 [» ]
    3J12 electron microscopy 11.50 R 2-115 [» ]
    3J14 electron microscopy 11.50 R 2-115 [» ]
    3J19 electron microscopy 8.30 P 2-115 [» ]
    3J37 electron microscopy 9.80 T 2-115 [» ]
    3J4X electron microscopy 12.00 P 1-115 [» ]
    3J50 electron microscopy 20.00 P 1-115 [» ]
    3J51 electron microscopy 17.00 P 1-115 [» ]
    3J52 electron microscopy 12.00 P 1-115 [» ]
    3J54 electron microscopy 13.00 P 1-115 [» ]
    3J56 electron microscopy 15.00 P 1-115 [» ]
    3J58 electron microscopy 17.00 P 1-115 [» ]
    3J5A electron microscopy 12.00 P 1-115 [» ]
    3J5C electron microscopy 17.00 P 1-115 [» ]
    3J5E electron microscopy 17.00 P 1-115 [» ]
    3J5G electron microscopy 20.00 P 1-115 [» ]
    3J5I electron microscopy 15.00 P 1-115 [» ]
    3J5K electron microscopy 9.00 P 1-115 [» ]
    3J5L electron microscopy 6.60 P 2-115 [» ]
    3J5O electron microscopy 6.80 P 1-115 [» ]
    3J5U electron microscopy 7.60 R 2-115 [» ]
    3J5W electron microscopy 7.60 S 2-115 [» ]
    3KCR electron microscopy - P 1-115 [» ]
    3OAS X-ray 3.25 P 2-115 [» ]
    3OAT X-ray 3.25 P 2-115 [» ]
    3OFC X-ray 3.19 P 2-115 [» ]
    3OFD X-ray 3.19 P 2-115 [» ]
    3OFQ X-ray 3.10 P 2-115 [» ]
    3OFR X-ray 3.10 P 2-115 [» ]
    3OFZ X-ray 3.29 P 2-115 [» ]
    3OG0 X-ray 3.29 P 2-115 [» ]
    3ORB X-ray 3.30 P 1-115 [» ]
    3R8S X-ray 3.00 P 2-115 [» ]
    3R8T X-ray 3.00 P 2-115 [» ]
    3SGF X-ray 3.20 T 1-115 [» ]
    3UOS X-ray 3.70 T 1-115 [» ]
    4CSU electron microscopy 5.50 P 2-115 [» ]
    4GAR X-ray 3.30 P 1-115 [» ]
    4GAU X-ray 3.30 P 1-115 [» ]
    4KIX X-ray 2.90 P 1-115 [» ]
    4KIZ X-ray 2.90 P 1-115 [» ]
    4KJ1 X-ray 2.90 P 1-115 [» ]
    4KJ3 X-ray 2.90 P 1-115 [» ]
    4KJ5 X-ray 2.90 P 1-115 [» ]
    4KJ7 X-ray 2.90 P 1-115 [» ]
    4KJ9 X-ray 2.90 P 1-115 [» ]
    4KJB X-ray 2.90 P 1-115 [» ]
    ProteinModelPortali P0A7K6.
    SMRi P0A7K6. Positions 2-115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35793N.
    IntActi P0A7K6. 101 interactions.
    MINTi MINT-1245288.
    STRINGi 511145.b2606.

    Chemistry

    ChEMBLi CHEMBL2363135.

    PTM databases

    PhosSitei P0810432.

    Proteomic databases

    PaxDbi P0A7K6.
    PRIDEi P0A7K6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75655 ; AAC75655 ; b2606 .
    BAA16491 ; BAA16491 ; BAA16491 .
    GeneIDi 12931612.
    947096.
    KEGGi ecj:Y75_p2554.
    eco:b2606.
    PATRICi 32120611. VBIEscCol129921_2704.

    Organism-specific databases

    EchoBASEi EB0873.
    EcoGenei EG10880. rplS.

    Phylogenomic databases

    eggNOGi COG0335.
    HOGENOMi HOG000016264.
    KOi K02884.
    OMAi GGRERIQ.
    OrthoDBi EOG6DZF5W.
    PhylomeDBi P0A7K6.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10880-MONOMER.
    ECOL316407:JW2587-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0A7K6.
    PROi P0A7K6.

    Gene expression databases

    Genevestigatori P0A7K6.

    Family and domain databases

    HAMAPi MF_00402. Ribosomal_L19.
    InterProi IPR001857. Ribosomal_L19.
    IPR018257. Ribosomal_L19_CS.
    IPR008991. Translation_prot_SH3-like.
    [Graphical view ]
    PANTHERi PTHR15680. PTHR15680. 1 hit.
    Pfami PF01245. Ribosomal_L19. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002191. Ribosomal_L19. 1 hit.
    PRINTSi PR00061. RIBOSOMALL19.
    SUPFAMi SSF50104. SSF50104. 1 hit.
    TIGRFAMsi TIGR01024. rplS_bact. 1 hit.
    PROSITEi PS01015. RIBOSOMAL_L19. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide."
      Bystroem A.S., Hjalmarsson K.J., Wikstroem P.M., Bjoerk G.R.
      EMBO J. 2:899-905(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], OPERON STRUCTURE.
      Strain: K12.
    2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      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. "Primary structure of protein L19 from the large subunit of Escherichia coli ribosomes."
      Brosius J., Arfsten U.
      Biochemistry 17:508-516(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-115.
    6. "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
      Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
      Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: CROSS-LINKING TO L14.
    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), INTERSUBUNIT BRIDGE FORMATION.
      Strain: MRE-600.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
      Strain: MRE-600.

    Entry informationi

    Entry nameiRL19_ECOLI
    AccessioniPrimary (citable) accession number: P0A7K6
    Secondary accession number(s): P02420
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 97 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