OTRF1_STAAR
ID OTRF1_STAAR Reviewed; 604 AA.
AC Q6GIB3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Putative O-acetyltransferase SAR0937;
DE EC=2.3.1.-;
GN OrderedLocusNames=SAR0937;
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 -!- 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; BX571856; CAG39943.1; -; Genomic_DNA.
DR RefSeq; WP_001044234.1; NC_002952.2.
DR AlphaFoldDB; Q6GIB3; -.
DR SMR; Q6GIB3; -.
DR KEGG; sar:SAR0937; -.
DR HOGENOM; CLU_005679_11_2_9; -.
DR OMA; AFIWPAF; -.
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..604
FT /note="Putative O-acetyltransferase SAR0937"
FT /id="PRO_0000208094"
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; 69455 MW; 390E24FDCFA51081 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 SSYIPQFIRM VIVVTLLIPF MLILVGAFNK YGKDIIGEKA NSFDTTIEDN
YSMRIAPIDN IHIDGLVSEK KKESSDVYNN IKPLLIGDSV MVDIGESFKS SVPKSRIDGK
VGRQLYQTLP LVKANYSQYK KSSDQVVLEL GTNGDFTVKQ LDDLLNQFGK AKIYLVNTRV
PRIYEANVNR LLADAAKRKS NVTLIDWYKR SQGHSEYFAP DGVHLEYKGV LALKDEILKA
LKKK