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Q56148

- CPT_STRVP

UniProt

Q56148 - CPT_STRVP

Protein

Chloramphenicol 3-O phosphotransferase

Gene

SVEN_4064

Organism
Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 70 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Inactivates chloramphenicol by catalyzing the transfer of the gamma-phosphate of ATP to the antibiotic's C-3' hydroxyl group.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei37 – 371

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 178ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Antibiotic resistance

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSVEN953739-WGS:GSXO-4129-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chloramphenicol 3-O phosphotransferase (EC:2.7.1.-)
    Short name:
    CPT
    Gene namesi
    Ordered Locus Names:SVEN_4064
    OrganismiStreptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745)
    Taxonomic identifieri953739 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
    ProteomesiUP000006854: Chromosome

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 178178Chloramphenicol 3-O phosphotransferasePRO_0000079295Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    178
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Helixi16 – 2611
    Beta strandi27 – 293
    Beta strandi31 – 355
    Helixi36 – 427
    Helixi45 – 484
    Beta strandi53 – 564
    Turni58 – 603
    Beta strandi62 – 643
    Helixi66 – 8419
    Beta strandi88 – 936
    Turni96 – 983
    Helixi99 – 10911
    Beta strandi114 – 1207
    Helixi123 – 13210
    Beta strandi134 – 1363
    Helixi140 – 1445
    Helixi147 – 1493
    Beta strandi155 – 1595
    Turni160 – 1623
    Helixi165 – 1739

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GRQX-ray2.90A1-178[»]
    1GRRX-ray2.90A1-178[»]
    1QHNX-ray2.70A1-178[»]
    1QHSX-ray2.80A1-178[»]
    1QHXX-ray2.50A1-178[»]
    1QHYX-ray2.60A1-178[»]
    ProteinModelPortaliQ56148.
    SMRiQ56148. Positions 1-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ56148.

    Family & Domainsi

    Sequence similaritiesi

    To M.tuberculosis Rv2636.Curated

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR012853. CPT.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF07931. CPT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF007531. CPT. 1 hit.
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q56148-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTRMIILNG GSSAGKSGIV RCLQSVLPEP WLAFGVDSLI EAMPLKMQSA    50
    EGGIEFDADG GVSIGPEFRA LEGAWAEGVV AMARAGARII IDDVFLGGAA 100
    AQERWRSFVG DLDVLWVGVR CDGAVAEGRE TARGDRVAGM AAKQAYVVHE 150
    GVEYDVEVDT THKESIECAW AIAAHVVP 178
    Length:178
    Mass (Da):18,816
    Last modified:November 1, 1996 - v1
    Checksum:iFC12D650A1C5D51A
    GO

    Sequence cautioni

    The sequence CCA57350.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09991 Genomic DNA. Translation: AAB36569.1.
    FR845719 Genomic DNA. Translation: CCA57350.1. Different initiation.
    RefSeqiYP_006879609.1. NC_018750.1.

    Genome annotation databases

    EnsemblBacteriaiCCA57350; CCA57350; SVEN_4064.
    GeneIDi13819222.
    KEGGisve:SVEN_4064.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09991 Genomic DNA. Translation: AAB36569.1 .
    FR845719 Genomic DNA. Translation: CCA57350.1 . Different initiation.
    RefSeqi YP_006879609.1. NC_018750.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GRQ X-ray 2.90 A 1-178 [» ]
    1GRR X-ray 2.90 A 1-178 [» ]
    1QHN X-ray 2.70 A 1-178 [» ]
    1QHS X-ray 2.80 A 1-178 [» ]
    1QHX X-ray 2.50 A 1-178 [» ]
    1QHY X-ray 2.60 A 1-178 [» ]
    ProteinModelPortali Q56148.
    SMRi Q56148. Positions 1-178.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB00446. Chloramphenicol.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CCA57350 ; CCA57350 ; SVEN_4064 .
    GeneIDi 13819222.
    KEGGi sve:SVEN_4064.

    Enzyme and pathway databases

    BioCyci SVEN953739-WGS:GSXO-4129-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q56148.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR012853. CPT.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF07931. CPT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF007531. CPT. 1 hit.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Inactivation of chloramphenicol by O-phosphorylation. A novel resistance mechanism in Streptomyces venezuelae ISP5230, a chloramphenicol producer."
      Mosher R.H., Camp D.J., Yang K., Brown M.P., Shaw W.V., Vining L.C.
      J. Biol. Chem. 270:27000-27006(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745.
    2. "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae provides new insights into global nitrogen regulation in actinomycetes."
      Pullan S.T., Chandra G., Bibb M.J., Merrick M.
      BMC Genomics 12:175-175(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745.
    3. "The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism."
      Izard T., Ellis J.
      EMBO J. 19:2690-2700(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
      Strain: ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745.

    Entry informationi

    Entry nameiCPT_STRVP
    AccessioniPrimary (citable) accession number: Q56148
    Secondary accession number(s): F2RH22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 70 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, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3