ID   OAC_BPSFV               Reviewed;         333 AA.
AC   P23214;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   23-FEB-2022, entry version 68.
DE   RecName: Full=O-acetyl transferase;
DE            EC=2.3.1.-;
DE   AltName: Full=O-antigen acetylase;
GN   Name=OAC;
OS   Shigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage
OS   SfVI).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Lederbergvirus.
OX   NCBI_TaxID=10761;
OH   NCBI_TaxID=623; Shigella flexneri.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2014005; DOI=10.1111/j.1365-2958.1991.tb01827.x;
RA   Verma N.K., Brandt J.M., Verma D.J., Lindberg A.A.;
RT   "Molecular characterization of the O-acetyl transferase gene of converting
RT   bacteriophage SF6 that adds group antigen 6 to Shigella flexneri.";
RL   Mol. Microbiol. 5:71-75(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1720755; DOI=10.1016/0378-1119(91)90295-m;
RA   Clark C.A., Beltrame J., Manning P.A.;
RT   "The oac gene encoding a lipopolysaccharide O-antigen acetylase maps
RT   adjacent to the integrase-encoding gene on the genome of Shigella flexneri
RT   bacteriophage Sf6.";
RL   Gene 107:43-52(1991).
CC   -!- FUNCTION: Antigenically converts S.flexneri serotype X to 3a, Y to 3b,
CC       1a to 1b and 4a to 4b by O-acetylating the O-antigenic polysaccharide
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000305};
CC       Peripheral membrane protein {ECO:0000305}. Note=Inner membrane-
CC       associated. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR   EMBL; X56800; CAA40136.1; -; Genomic_DNA.
DR   EMBL; X59553; CAA42132.1; -; Genomic_DNA.
DR   SMR; P23214; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Host cell inner membrane; Host cell membrane;
KW   Host membrane; Membrane; Transferase.
FT   CHAIN           1..333
FT                   /note="O-acetyl transferase"
FT                   /id="PRO_0000208084"
FT   CONFLICT        158
FT                   /note="H -> L (in Ref. 2; CAA42132)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="L -> Q (in Ref. 2; CAA42132)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   333 AA;  37186 MW;  7DF71DFC17C6CF07 CRC64;
     MHKSNCFDTA RLVAAMMVLV SHHYALSGQP EPYLFGFESA GGIAVIIFFS ISGYLISKSA
     IRSDSFIDFM AKRARRIFPA LVPCSILTYF LFGWILNDFS AEYFSHDIVR KTISSIFMSQ
     APDADITSHL IHAGINGSLW TLPLEFLCYI ITGVAVAHLK NGKAFIVILL VFVSLSLIGS
     VSENRDVMFS IPLWLYPLRG LAFFFGATMA MYEKSWNVSN VKITVVSLLA MYAYASYGKG
     IDYTMTCYIL VSFSTIAICT SVGDPLVKGR FDYSYGVYIY AFPVQQVVIN TLHMGFYPSM
     LLSAVTVLFL SHLSWNLVEK RFLTRSSPKL SLD