LPXA_BURTA
ID LPXA_BURTA Reviewed; 262 AA.
AC Q2SWY6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387};
GN Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387}; OrderedLocusNames=BTH_I2039;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated
CC glycolipid that anchors the lipopolysaccharide to the outer membrane of
CC the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + UDP-N-acetyl-alpha-D-glucosamine =
CC a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + holo-
CC [ACP]; Xref=Rhea:RHEA:67812, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:57705, ChEBI:CHEBI:64479, ChEBI:CHEBI:78827,
CC ChEBI:CHEBI:173225; EC=2.3.1.129; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00387};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 1/6. {ECO:0000255|HAMAP-
CC Rule:MF_00387}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00387}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}.
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DR EMBL; CP000086; ABC38675.1; -; Genomic_DNA.
DR RefSeq; WP_009890458.1; NZ_CP008785.1.
DR PDB; 4EQY; X-ray; 1.80 A; A/B/C/E/F/G=1-262.
DR PDBsum; 4EQY; -.
DR AlphaFoldDB; Q2SWY6; -.
DR SMR; Q2SWY6; -.
DR PRIDE; Q2SWY6; -.
DR EnsemblBacteria; ABC38675; ABC38675; BTH_I2039.
DR GeneID; 66547473; -.
DR KEGG; bte:BTH_I2039; -.
DR HOGENOM; CLU_061249_0_0_4; -.
DR OMA; ECVTINR; -.
DR OrthoDB; 971098at2; -.
DR UniPathway; UPA00359; UER00477.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd03351; LbH_UDP-GlcNAc_AT; 1.
DR Gene3D; 1.20.1180.10; -; 1.
DR HAMAP; MF_00387; LpxA; 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 PANTHER; PTHR43480; PTHR43480; 1.
DR Pfam; PF13720; Acetyltransf_11; 1.
DR Pfam; PF00132; Hexapep; 2.
DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01852; lipid_A_lpxA; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Repeat; Transferase.
FT CHAIN 1..262
FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT O-acyltransferase"
FT /id="PRO_1000013160"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4EQY"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4EQY"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:4EQY"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:4EQY"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:4EQY"
FT HELIX 225..235
FT /evidence="ECO:0007829|PDB:4EQY"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4EQY"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:4EQY"
SQ SEQUENCE 262 AA; 27874 MW; 189A5441A77BB522 CRC64;
MSRIHPTAII EPGAQLHETV EVGPYAIVGS NVTIGARTTI GSHSVIEGHT TIGEDNRIGH
YASVGGRPQD MKYKDEPTRL VIGDRNTIRE FTTIHTGTVQ DAGVTTLGDD NWIMAYVHIG
HDCRVGSHVV LSSNAQMAGH VEIGDWAIVG GMSGVHQYVR IGAHSMLGGA SALVQDIPPF
VIAAGNKAEP HGINVEGLRR RGFSPDAISA LRSAYRILYK NSLSLEEAKV QLSELAQAGG
DGDAAVKALV DFVESSQRGI IR
