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Database: UniProt
Entry: A0A238USR3_9ACTN
LinkDB: A0A238USR3_9ACTN
Original site: A0A238USR3_9ACTN 
ID   A0A238USR3_9ACTN        Unreviewed;       423 AA.
AC   A0A238USR3;
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:SNR24914.1};
GN   ORFNames=SAMN06265355_101350 {ECO:0000313|EMBL:SNR24914.1};
OS   Actinomadura mexicana.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=134959 {ECO:0000313|EMBL:SNR24914.1, ECO:0000313|Proteomes:UP000198420};
RN   [1] {ECO:0000313|EMBL:SNR24914.1, ECO:0000313|Proteomes:UP000198420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44485 {ECO:0000313|EMBL:SNR24914.1,
RC   ECO:0000313|Proteomes:UP000198420};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FZNP01000001; SNR24914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238USR3; -.
DR   OrthoDB; 9807745at2; -.
DR   Proteomes; UP000198420; 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:SF136; ACETYLATION OF THE O-ANTIGEN (LPS); 1.
DR   PANTHER; PTHR23028; ACETYLTRANSFERASE; 1.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:SNR24914.1};
KW   Hydrolase {ECO:0000313|EMBL:SNR24914.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:SNR24914.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        50..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        169..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..389
FT                   /note="Acyltransferase 3"
FT                   /evidence="ECO:0000259|Pfam:PF01757"
SQ   SEQUENCE   423 AA;  44521 MW;  EC6995F19772766E CRC64;
     MIPALGVSPA SSRLGWLDAL RGAAALAVAL HHASYVYLPD LRVRLADRFD PGLFGVLVFF
     LVSGYIVPAS LERRGSVREF WFGRFFRIYP LLAVTCLLAV LPFLLGVLGL RAGLERYSPA
     TAVLAHMTML QDVLNVPNAM NVLWTLSYEM AFYLLVVALF VVGGHRRSAP AAVVLTVVAL
     VAVALTACGL LTGAYAPAAL LSRTAGTGPV VAVTVAALAV AIPAASSRRS APRVAGGLLG
     GLLALALVAV NGRVGAWEGL LMLAAMFTGT AVHRAEHGQI SRRAAGATGA AVLTGALAAG
     TWNAAPYGRN AQLVWCGAVL AAAATFAAGW RLRHRRFPAW TTGLGTISFS VYLLHPLLLM
     AAAQFLGVSG REDAVGLAFF LLVLIAASWA SQRWIEAPAQ RLGRRLTRPS PPDRRLEQHA
     LAS
//
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