ID   OTRF1_STAAS             Reviewed;         604 AA.
AC   Q6GAV2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Putative O-acetyltransferase SAS0844;
DE            EC=2.3.1.-;
GN   OrderedLocusNames=SAS0844;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR   EMBL; BX571857; CAG42619.1; -; Genomic_DNA.
DR   RefSeq; WP_001044230.1; NC_002953.3.
DR   AlphaFoldDB; Q6GAV2; -.
DR   SMR; Q6GAV2; -.
DR   KEGG; sas:SAS0844; -.
DR   HOGENOM; CLU_005679_11_2_9; -.
DR   OMA; AFIWPAF; -.
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..604
FT                   /note="Putative O-acetyltransferase SAS0844"
FT                   /id="PRO_0000208095"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        459
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV54"
FT   ACT_SITE        581
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV54"
FT   ACT_SITE        584
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV54"
SQ   SEQUENCE   604 AA;  69414 MW;  99536B4D42A27017 CRC64;
     MNKTKGFTKY KKMRYMPGLD GLRAIAVLGI IIYHLNKQWL TGGFLGVDTF FVISGYLITS
     LLLKEYDDTG IIKLKSFWIR RLKRLLPAVI VLLMVVGTAT LLLKSDNIIR VKHDIIAAIF
     YVSNWWYIAK DVNYFEQFSF MPLKHLWSLA IEEQFYIFFP VILVTLLLTI KKRYKIGFIF
     WGVSIISLGL MMFIYSINGD HSRVYFGTDT RLQTLLLGVI LAFLWPPFKL KNDPPKVVKY
     VIDSIGSLSF IVLILLFFII NDETNWIYDG GFYLISILTL FIIASVVHPS TWIAKIFSNP
     VLVFIGKRSY SLYLWHFAVI SFVHSYYVDG QIPVYVYFID ISLTIIFAEL SYRFIETPFR
     KEGIKALNWR PSYIPQFIRM AIVVTLLIPF MLILVGAFNK YGKDIIGEKA NSFDTTIEDN
     YLMRIAPIDN IHIDGLVSEK KKESSDVYNN IKPLLIGDSV MVDIGESFKS SVPKSRIDGK
     VGRQLYQTLP LVKANYSQYK KSSDQVVLEL GTNGDFTVKQ LDDLLNQFGK AKIYLVNTRV
     PRIYEANVNR LLADAAKRKS NVTLIDWNKR SQGHSEYFAP DGVHLEYKGV LALKDEILKA
     LKKK