ID   CAT2_ECOLX              Reviewed;         213 AA.
AC   P22615;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Chloramphenicol acetyltransferase 2;
DE            EC=2.3.1.28;
DE   AltName: Full=Chloramphenicol acetyltransferase II;
DE            Short=CAT-II;
GN   Name=cmlA;
OS   Escherichia coli.
OG   Plasmid IncW pSa.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2268278; DOI=10.1042/bj2720505;
RA   Murray I.A., Martinez-Suarez J.V., Close T.J., Shaw W.V.;
RT   "Nucleotide sequences of genes encoding the type II chloramphenicol
RT   acetyltransferases of Escherichia coli and Haemophilus influenzae, which
RT   are sensitive to inhibition by thiol-reactive reagents.";
RL   Biochem. J. 272:505-510(1990).
CC   -!- FUNCTION: This enzyme is an effector of chloramphenicol resistance in
CC       bacteria.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate +
CC         CoA; Xref=Rhea:RHEA:18421, ChEBI:CHEBI:16730, ChEBI:CHEBI:17698,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.28;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10021};
CC   -!- SUBUNIT: Homotrimer.
CC   -!- MISCELLANEOUS: Type II chloramphenicol acetyltransferases are sensitive
CC       to inhibition by thiol-reactive reagents. The inactivation occurs as a
CC       result of chemical modification of Cys-26.
CC   -!- SIMILARITY: Belongs to the chloramphenicol acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X53796; CAA37805.1; -; Genomic_DNA.
DR   PIR; S13398; S13398.
DR   AlphaFoldDB; P22615; -.
DR   SMR; P22615; -.
DR   KEGG; ag:CAA37805; -.
DR   GO; GO:0008811; F:chloramphenicol O-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR018372; Chloramphenicol_AcTrfase_AS.
DR   InterPro; IPR001707; Cmp_AcTrfase.
DR   PANTHER; PTHR38474; PTHR38474; 1.
DR   Pfam; PF00302; CAT; 1.
DR   PIRSF; PIRSF000440; CAT; 1.
DR   SMART; SM01059; CAT; 1.
DR   PROSITE; PS00100; CAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Antibiotic resistance; Direct protein sequencing; Plasmid;
KW   Transferase.
FT   CHAIN           1..213
FT                   /note="Chloramphenicol acetyltransferase 2"
FT                   /id="PRO_0000165875"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10021"
SQ   SEQUENCE   213 AA;  24778 MW;  2E0D7F150A730AF7 CRC64;
     MNFTRIDLNT WNRREHFALY RQQIKCGFSL TTKLDITALR TALAETGYKF YPLMIYLISR
     AVNQFPEFRM ALKDNELIYW DQSDPVFTVF HKETETFSAL SCRYFPDLSE FMAGYNAVTA
     EYQHDTRLFP QGNLPENHLN ISSLPWVSFD GFNLNITGND DYFAPVFTMA KFQQEGDRVL
     LPVSVQVHHA VCDGFHAARF INTLQLMCDN ILK