ID   LPXA_BRUA2              Reviewed;         278 AA.
AC   Q2YRQ5; P54080; Q57CY8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BAB1_1173;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Bearden S.W., Ficht T.A.;
RT   "Isolation and sequence of the group 1 outer membrane protein of Brucella
RT   abortus.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA96791.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U51683; AAA96791.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AM040264; CAJ11129.1; -; Genomic_DNA.
DR   RefSeq; WP_002964279.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YRQ5; -.
DR   SMR; Q2YRQ5; -.
DR   STRING; 359391.BAB1_1173; -.
DR   EnsemblBacteria; CAJ11129; CAJ11129; BAB1_1173.
DR   GeneID; 45124526; -.
DR   GeneID; 55590833; -.
DR   KEGG; bmf:BAB1_1173; -.
DR   PATRIC; fig|359391.11.peg.72; -.
DR   HOGENOM; CLU_061249_0_0_5; -.
DR   OMA; ECVTINR; -.
DR   PhylomeDB; Q2YRQ5; -.
DR   BioCyc; MetaCyc:BAB_RS21540-MON; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000002719; 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; IPR018357; Hexapep_transf_CS.
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   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..278
FT                   /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT                   O-acyltransferase"
FT                   /id="PRO_0000188035"
FT   CONFLICT        129
FT                   /note="D -> GH (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  29386 MW;  DF77C706EEA9F8DF CRC64;
     MKETFIHPTA LVEPGVELGQ GVSVGPFCHV QSGAIIGNDC ELMSHVVITG ATTLGAGTKV
     YPHAILGCDP QNNKHKGGPT RLNVGVNCII REGVTMHKGS DNARGYTSIG DNCSFLAYAH
     VAHDCDIGDY VTFSNNVMIG GHTSIGHHAI LGGGAAVHQF VRVGHHAFIG GLAAVVSDLI
     PYGMAIGVHA HLGGLNIIGM KRSGMERKEI HNLRHAVRML FDRTKPIRQR AQDVLAAIPD
     SPTVSDMISF INVDTKRAYC TPPLDAAHGG AGHDSDED