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Database: UniProt
Entry: D5U927_BRAM5
LinkDB: D5U927_BRAM5
Original site: D5U927_BRAM5 
ID   D5U927_BRAM5            Unreviewed;       264 AA.
AC   D5U927;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Acyl-(Acyl-carrier-protein)--UDP-N-acetylglucosa mineO-acyltransferase {ECO:0000313|EMBL:ADG71200.1};
DE            EC=2.3.1.129 {ECO:0000313|EMBL:ADG71200.1};
GN   OrderedLocusNames=Bmur_1105 {ECO:0000313|EMBL:ADG71200.1};
OS   Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS   murdochii).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG71200.1, ECO:0000313|Proteomes:UP000001915};
RN   [1] {ECO:0000313|EMBL:ADG71200.1, ECO:0000313|Proteomes:UP000001915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC   {ECO:0000313|Proteomes:UP000001915};
RX   PubMed=21304710; DOI=10.4056/sigs.831993;
RA   Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA   Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL   Stand. Genomic Sci. 2:260-269(2010).
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DR   EMBL; CP001959; ADG71200.1; -; Genomic_DNA.
DR   RefSeq; WP_013113624.1; NC_014150.1.
DR   AlphaFoldDB; D5U927; -.
DR   STRING; 526224.Bmur_1105; -.
DR   KEGG; brm:Bmur_1105; -.
DR   eggNOG; COG1043; Bacteria.
DR   HOGENOM; CLU_061249_0_0_12; -.
DR   OrthoDB; 9782926at2; -.
DR   Proteomes; UP000001915; Chromosome.
DR   GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 1.20.1180.10; Udp N-acetylglucosamine O-acyltransferase, C-terminal domain; 1.
DR   InterPro; IPR029098; Acetyltransf_C.
DR   InterPro; IPR037157; Acetyltransf_C_sf.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR010137; Lipid_A_LpxA.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR01852; lipid_A_lpxA; 1.
DR   PANTHER; PTHR43480; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR43480:SF1; ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF13720; Acetyltransf_11; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:ADG71200.1};
KW   Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADG71200.1}.
FT   DOMAIN          177..258
FT                   /note="UDP N-acetylglucosamine O-acyltransferase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13720"
SQ   SEQUENCE   264 AA;  28908 MW;  230A6EF99952C0BE CRC64;
     MSENIHKTAI ISESAKISDS AVIGPYAVIE GEVNIGENTV IGAHSVIKEY TTIGKNNIIH
     DHAVIGNLPQ DIHFDRKTVT FLEIGDGNEI REFANLHRAS KENAKTTIGN NCYIMATGHV
     AHDCEIQDNV IICNGALAAG HVRIEKGAFI SGNCVIHQFC AIGQYAMISG MSAVGRDILP
     FALTAHAGEA IVYKLNLVGM RRAGFTSEQI SQAEAAYDMW YNWNKTKQEF LDTYLNDNSL
     NDIARSIVEF ISKARRGITP KKTV
//
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