ID   LPXA_SYNAS              Reviewed;         258 AA.
AC   Q2LVL6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=SYNAS_22470;
GN   ORFNames=SYN_01567;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC78126.1; -; Genomic_DNA.
DR   RefSeq; WP_011418146.1; NC_007759.1.
DR   AlphaFoldDB; Q2LVL6; -.
DR   SMR; Q2LVL6; -.
DR   STRING; 56780.SYN_01567; -.
DR   EnsemblBacteria; ABC78126; ABC78126; SYN_01567.
DR   KEGG; sat:SYN_01567; -.
DR   eggNOG; COG1043; Bacteria.
DR   HOGENOM; CLU_061249_0_0_7; -.
DR   OMA; ECVTINR; -.
DR   OrthoDB; 971098at2; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000001933; Chromosome.
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.
PE   3: Inferred from homology;
KW   Acyltransferase; Cytoplasm; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..258
FT                   /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT                   O-acyltransferase"
FT                   /id="PRO_1000013181"
SQ   SEQUENCE   258 AA;  27942 MW;  258E670E7779401A CRC64;
     MTVHPTAIVS PDARLAQGVE IGAYSVIGPG VTVGRNTFLG SHVVIERDTD IGEGCRISSF
     CSLGGDPQDL KYEGEKTRVI IGNYNVLREY VTVNRATSAD IGVTIIGDHN LIMAYCHVAH
     NCKLGNHIVI SNGSHLAGHI HVDDYAIISG MVGIHQFTRI GAHSIIGGAS AVTQDVPPYV
     TAAGNHAKLY GLNLIGLERR GFSKETISAL KEAYRIIFRS SSLRREDALE KVRQTVADTP
     EVRHFIDFIQ TSERGVCH