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Database: UniProt
Entry: A0A1H4SQ61_9ACTN
LinkDB: A0A1H4SQ61_9ACTN
Original site: A0A1H4SQ61_9ACTN 
ID   A0A1H4SQ61_9ACTN        Unreviewed;       402 AA.
AC   A0A1H4SQ61;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains {ECO:0000313|EMBL:SEC46266.1};
GN   ORFNames=SAMN05216489_00802 {ECO:0000313|EMBL:SEC46266.1};
OS   Streptomyces sp. 3213.3.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855348 {ECO:0000313|EMBL:SEC46266.1, ECO:0000313|Proteomes:UP000198754};
RN   [1] {ECO:0000313|EMBL:SEC46266.1, ECO:0000313|Proteomes:UP000198754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3213 {ECO:0000313|EMBL:SEC46266.1,
RC   ECO:0000313|Proteomes:UP000198754};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNTK01000001; SEC46266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4SQ61; -.
DR   STRING; 1855348.SAMN05216489_00802; -.
DR   Proteomes; UP000198754; Unassembled WGS sequence.
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   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR23028:SF53; O-ACYLTRANSFERASE HOMOLOG; 1.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:SEC46266.1};
KW   Hydrolase {ECO:0000313|EMBL:SEC46266.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198754};
KW   Transferase {ECO:0000313|EMBL:SEC46266.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        230..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        356..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..372
FT                   /note="Acyltransferase 3"
FT                   /evidence="ECO:0000259|Pfam:PF01757"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  43845 MW;  AD21B8989DD150A4 CRC64;
     MSTLHRSAVD EATGQSPEAR DVRRGFASAL RGGGRVAGLD GLRTVAVVLV IVYHVEPDLV
     PGGSVGVDVF FTISGFVITR LLVTEYARSG HIGLWSFYRR RWLRLMPALL VMCAVTAVLS
     VTFALPLFQG AWVAAVLAAG SVVNLVRAGS AGTYSDLTAP LSHTWSLGVE EQFYLAWPLL
     LLVLLRHARA RVVLGWVAVL CVLPVLWRTV LWDPSAAHRI YNGPDTRADQ LLVGALLALV
     LARLRADDPR LAQLRRWAGR LCCPALVLLG LIAWQIPITE VSGWNPVWYT AGFLAAAVLT
     ACVVAALDLC PESWPTRLLS LSVPVWIGRN LSYGMYLWHY PVIRLLHDLG VRGDLLLPAG
     LAATLAAALA SYAFVERPLL RRGRFRVRRL EPVVVPGRSP AL
//
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