CPT_STRVP
ID CPT_STRVP Reviewed; 178 AA.
AC Q56148; F2RH22;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Chloramphenicol 3-O phosphotransferase;
DE Short=CPT;
DE EC=2.7.1.-;
GN OrderedLocusNames=SVEN_4064;
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=953739;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=7592948; DOI=10.1074/jbc.270.45.27000;
RA Mosher R.H., Camp D.J., Yang K., Brown M.P., Shaw W.V., Vining L.C.;
RT "Inactivation of chloramphenicol by O-phosphorylation. A novel resistance
RT mechanism in Streptomyces venezuelae ISP5230, a chloramphenicol producer.";
RL J. Biol. Chem. 270:27000-27006(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Chandra G., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=10835366; DOI=10.1093/emboj/19.11.2690;
RA Izard T., Ellis J.;
RT "The crystal structures of chloramphenicol phosphotransferase reveal a
RT novel inactivation mechanism.";
RL EMBO J. 19:2690-2700(2000).
CC -!- FUNCTION: Inactivates chloramphenicol by catalyzing the transfer of the
CC gamma-phosphate of ATP to the antibiotic's C-3' hydroxyl group.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: To M.tuberculosis Rv2636. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCA57350.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U09991; AAB36569.1; -; Genomic_DNA.
DR EMBL; FR845719; CCA57350.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_063844287.1; NG_047672.1.
DR PDB; 1GRQ; X-ray; 2.90 A; A=1-178.
DR PDB; 1GRR; X-ray; 2.90 A; A=1-178.
DR PDB; 1QHN; X-ray; 2.70 A; A=1-178.
DR PDB; 1QHS; X-ray; 2.80 A; A=1-178.
DR PDB; 1QHX; X-ray; 2.50 A; A=1-178.
DR PDB; 1QHY; X-ray; 2.60 A; A=1-178.
DR PDBsum; 1GRQ; -.
DR PDBsum; 1GRR; -.
DR PDBsum; 1QHN; -.
DR PDBsum; 1QHS; -.
DR PDBsum; 1QHX; -.
DR PDBsum; 1QHY; -.
DR AlphaFoldDB; Q56148; -.
DR SMR; Q56148; -.
DR STRING; 953739.SVEN_4064; -.
DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate.
DR DrugBank; DB04411; Alpha-N-Dichloroacetyl-P-Aminophenylserinol.
DR DrugBank; DB00446; Chloramphenicol.
DR DrugBank; DB02608; N-[(1R,2R)-1,3-Dihydroxy-1-(4-nitrophenyl)-2-propanyl]acetamide.
DR EnsemblBacteria; CCA57350; CCA57350; SVEN_4064.
DR KEGG; ag:AAB36569; -.
DR KEGG; sve:SVEN_4064; -.
DR PATRIC; fig|953739.5.peg.6564; -.
DR eggNOG; COG3896; Bacteria.
DR HOGENOM; CLU_101381_0_0_11; -.
DR EvolutionaryTrace; Q56148; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd00227; CPT; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012853; CPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR PIRSF; PIRSF007531; CPT; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..178
FT /note="Chloramphenicol 3-O phosphotransferase"
FT /id="PRO_0000079295"
FT ACT_SITE 37
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1QHX"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1QHX"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1QHX"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1QHX"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1QHX"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1QHX"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1QHX"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1GRQ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1QHX"
FT HELIX 66..84
FT /evidence="ECO:0007829|PDB:1QHX"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1QHX"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1QHX"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:1QHX"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:1QHX"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:1QHX"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1QHX"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:1QHX"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1QHX"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:1QHX"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1GRQ"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:1QHX"
SQ SEQUENCE 178 AA; 18816 MW; FC12D650A1C5D51A CRC64;
MTTRMIILNG GSSAGKSGIV RCLQSVLPEP WLAFGVDSLI EAMPLKMQSA EGGIEFDADG
GVSIGPEFRA LEGAWAEGVV AMARAGARII IDDVFLGGAA AQERWRSFVG DLDVLWVGVR
CDGAVAEGRE TARGDRVAGM AAKQAYVVHE GVEYDVEVDT THKESIECAW AIAAHVVP
