ID   LPXA_AGRRK              Reviewed;         271 AA.
AC   B9JEY0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Arad_2232;
OS   Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=311403;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K84 / ATCC BAA-868;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000628; ACM26471.1; -; Genomic_DNA.
DR   RefSeq; WP_007693431.1; NC_011985.1.
DR   AlphaFoldDB; B9JEY0; -.
DR   SMR; B9JEY0; -.
DR   STRING; 311403.Arad_2232; -.
DR   EnsemblBacteria; ACM26471; ACM26471; Arad_2232.
DR   KEGG; ara:Arad_2232; -.
DR   eggNOG; COG1043; Bacteria.
DR   HOGENOM; CLU_061249_0_0_5; -.
DR   OMA; ECVTINR; -.
DR   OrthoDB; 971098at2; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000001600; Chromosome 1.
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..271
FT                   /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT                   O-acyltransferase"
FT                   /id="PRO_1000134376"
SQ   SEQUENCE   271 AA;  28556 MW;  88F3D088D8A621DD CRC64;
     MSSIAKSARI HKLAVVEDGA VIGENVVVGP FCHVGPKVVL HDSVQLLTHV VVTGRTTIGK
     GTKIFPMAVV GGDPQSVHHG GEETTLDIGE NCTIREGVTI NTGTADYGGK TVVGNNNLFL
     ANSHVAHDCR VGNNVIMSNN VMLAGHVTVE DRAILGGGCA VHQFTRIGRQ AFVGGLSAAS
     YDVIPYGMLN GNPGVLSGLN IVGMTRAGIE RSVIHRVRRA YKSIFEGEGS IRDNATAIRE
     EYADCKEAME ILDFIAADSD RALSSPNRGK G