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Database: UniProt
Entry: A0A1V3NXY4_9GAMM
LinkDB: A0A1V3NXY4_9GAMM
Original site: A0A1V3NXY4_9GAMM 
ID   A0A1V3NXY4_9GAMM        Unreviewed;       367 AA.
AC   A0A1V3NXY4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Acyltransferase {ECO:0000313|EMBL:OOG37583.1};
GN   ORFNames=B0E52_14955 {ECO:0000313|EMBL:OOG37583.1};
OS   Rhodanobacter sp. C06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1945854 {ECO:0000313|EMBL:OOG37583.1, ECO:0000313|Proteomes:UP000189228};
RN   [1] {ECO:0000313|EMBL:OOG37583.1, ECO:0000313|Proteomes:UP000189228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C06 {ECO:0000313|EMBL:OOG37583.1,
RC   ECO:0000313|Proteomes:UP000189228};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOG37583.1}.
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DR   EMBL; MUNP01000070; OOG37583.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3NXY4; -.
DR   OrthoDB; 9767863at2; -.
DR   Proteomes; UP000189228; 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   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:OOG37583.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189228};
KW   Transferase {ECO:0000313|EMBL:OOG37583.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        83..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        249..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        319..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..331
FT                   /note="Acyltransferase 3"
FT                   /evidence="ECO:0000259|Pfam:PF01757"
SQ   SEQUENCE   367 AA;  40498 MW;  8EDD4BA662DA2531 CRC64;
     MPRLPGLDLL RAIAIVWVML FHSWMIGGLG TPLFQPVADY GWMGVDLFFV LSGYLIGFQL
     LAPLSRGEPL RFGAFYLRRA FRILPVFFVV LAVYVSFPAW REAPGMQPAW QFLTFTLNLL
     IDYRHNQALS HAWSLCVEEH FYLLFPLLAW WLARRASRAR VIGAVALVVL AGLGLRAYAV
     LHGKDWLESI YYPTWTRLDG LLAGVLLATI QAYRPRWWAA AQRRANTLAV AGLLVVGAAI
     WLFRDKTAFA ASVFGFPLLA LGLALLVAAA AGPAGWLGRW RIPGAGWIAG ISYSLYLSHK
     LAMHAVHDAL SNWPAVHGPA AFVVYVLAIA ATGALLHYAI ERPFLRLRTR LAGGGVRPLA
     ETQTASA
//
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