ID   OATA_STAAW              Reviewed;         603 AA.
AC   Q79ZY2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=O-acetyltransferase OatA;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q2FV54};
GN   Name=oatA; OrderedLocusNames=MW2488;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
CC   -!- FUNCTION: Responsible for O-acetylation at the C(6)-hydroxyl group of
CC       N-acetylmuramyl residues, forming the corresponding N,6-O-
CC       diacetylmuramic acid of the peptidoglycan. O-acetylation of the
CC       peptidoglycan is the major determinant for lysozyme resistance.
CC       {ECO:0000250|UniProtKB:Q2FV54}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR   EMBL; BA000033; BAB96353.1; -; Genomic_DNA.
DR   RefSeq; WP_000379821.1; NC_003923.1.
DR   AlphaFoldDB; Q79ZY2; -.
DR   SMR; Q79ZY2; -.
DR   EnsemblBacteria; BAB96353; BAB96353; BAB96353.
DR   KEGG; sam:MW2488; -.
DR   HOGENOM; CLU_005679_11_2_9; -.
DR   OMA; NRWLTNP; -.
DR   Proteomes; UP000000418; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell membrane; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..603
FT                   /note="O-acetyltransferase OatA"
FT                   /id="PRO_0000208090"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        453
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV54"
FT   ACT_SITE        575
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV54"
FT   ACT_SITE        578
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV54"
SQ   SEQUENCE   603 AA;  69099 MW;  B9050E0DE20B8DF1 CRC64;
     MDTKDFKRLE KMYSPRYLPG LDGLRAFAVI GIIIYHLNAQ WLSGGFLGVD TFFVISGYLI
     TSLLISEYYR TQKIDLLEFW KRRLKRLIPA VLFLICVVLT FTLIFKPELI IQMKRDAIAA
     IFYVSNWWYI SQNVDYFNQF AIEPLKHLWS LAIEEQFYLL FPLVITFLLH RFKPRNIIQT
     LFIVSLISLG LMIVIHFITG DNSRVYFGTD TRLQTLLLGC ILAFIWPPFA LKKDISKKIV
     VSLDIIGISG FAVLMTLFFI VGDQDQWIYN GGFYIISFAT LFIIAIAVHP SSLFAKFLSM
     KPLLIIGKRS YSLYLWHYPI IVFVNSYYVQ GQIPVYVYII EILLTALMAE ISYRFIETPI
     RKKGFKAFAF LPKKKGQFAR TVLVILLLVP SIVVLSGQFD ALGKQHEAEK KEKKTEFKTT
     KKKVVKKDKQ EDKQTANSKE DIKKSSPLLI GDSVMVDIGN VFTKKIPNAQ IDGKVGRQLV
     DATPIVKSQY KDYAKKGQKV VVELGTNGAF TKDQLNELLD SFGKADIYLV SIRVPRDYEG
     RINKLIYEAA EKRSNVHLVD WYKASAGHPE YFAYDGIHLE YAGSKALTDL IVKTMETHAT
     NKK