ID   A0A1H7SEB2_9GAMM        Unreviewed;       331 AA.
AC   A0A1H7SEB2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Peptidoglycan/LPS O-acetylase OafA/YrhL, contains acyltransferase and SGNH-hydrolase domains {ECO:0000313|EMBL:SEL70962.1};
GN   ORFNames=SAMN05216262_11860 {ECO:0000313|EMBL:SEL70962.1};
OS   Colwellia chukchiensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=641665 {ECO:0000313|EMBL:SEL70962.1, ECO:0000313|Proteomes:UP000199297};
RN   [1] {ECO:0000313|Proteomes:UP000199297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9127 {ECO:0000313|Proteomes:UP000199297};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOBI01000018; SEL70962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7SEB2; -.
DR   STRING; 641665.GCA_002104455_02328; -.
DR   Proteomes; UP000199297; 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:SEL70962.1};
KW   Hydrolase {ECO:0000313|EMBL:SEL70962.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199297};
KW   Transferase {ECO:0000313|EMBL:SEL70962.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        222..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..313
FT                   /note="Acyltransferase 3"
FT                   /evidence="ECO:0000259|Pfam:PF01757"
SQ   SEQUENCE   331 AA;  37510 MW;  31F3C61201B406C4 CRC64;
     MVVVGHIFWL SDFGRFAVFG FYILSGYLMT YIMHTSYGYS SLGRKKFATN RFLRLYPAFW
     AAILCSIVIT LFWGSSSNGF ILPTNLAAII GNTTMIFPHW MPSQIEPRLS PATWALTVEL
     FFYVAIALGI SKTLKRTYIW ISLSVVFIVL SYVMNLYWHA RYFSIPAGSL PFSLGALIFF
     LSKQKSVRYI PEAILASPIK LFFTSFCIAI VTSIAISQSL SFWLMEIIFY FCMAINFLLV
     LSLAKQNTFV NGLSTKLDKK IGDFSYPFYL LHYQAAAIAS VISLGKVASL KENFSLISCM
     LTFLILFIMS LCVIKLIDKP VEKLRQTIKA K
//