OATA_STAAR
ID OATA_STAAR Reviewed; 603 AA.
AC Q6GDN2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=O-acetyltransferase OatA;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q2FV54};
GN Name=oatA; OrderedLocusNames=SAR2649;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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 -!- 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; BX571856; CAG41626.1; -; Genomic_DNA.
DR RefSeq; WP_000379825.1; NC_002952.2.
DR AlphaFoldDB; Q6GDN2; -.
DR SMR; Q6GDN2; -.
DR KEGG; sar:SAR2649; -.
DR HOGENOM; CLU_005679_11_2_9; -.
DR OMA; NRWLTNP; -.
DR OrthoDB; 1968136at2; -.
DR Proteomes; UP000000596; 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_0000208088"
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; 69157 MW; 1A38710C19A8EBE8 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 LPKKKSQFAR TVLVILLLIP SIIVLSGQFD ALGKQHEAEK KEKKTEFKTT
KKKVVKKDKQ EDKQTANSKE DIKKSSPLLI GDSVMVDIGN VFTKKIPNAQ IDGKVGRQLV
DATPIVKSQY KDYAKKGQKV VVELGTNGAF TKDQLNELLD SFGKADIYLV SIRVPRDYEG
RINKLIYEAA EKRSNVHLVD WYKASAGHPE YFAYDGIHLE YAGSKALTDL IVKTMETHAT
NKK