ID   LPXA_CAMJE              Reviewed;         263 AA.
AC   Q9PIM1; Q0PBN1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 135.
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=Cj0274;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL34428.1; -; Genomic_DNA.
DR   PIR; A81446; A81446.
DR   RefSeq; WP_002851756.1; NZ_SZUC01000004.1.
DR   RefSeq; YP_002343716.1; NC_002163.1.
DR   PDB; 3R0S; X-ray; 2.30 A; A=1-263.
DR   PDBsum; 3R0S; -.
DR   AlphaFoldDB; Q9PIM1; -.
DR   SMR; Q9PIM1; -.
DR   IntAct; Q9PIM1; 29.
DR   STRING; 192222.Cj0274; -.
DR   PaxDb; 192222-Cj0274; -.
DR   EnsemblBacteria; CAL34428; CAL34428; Cj0274.
DR   GeneID; 904599; -.
DR   KEGG; cje:Cj0274; -.
DR   PATRIC; fig|192222.6.peg.268; -.
DR   eggNOG; COG1043; Bacteria.
DR   HOGENOM; CLU_061249_0_0_7; -.
DR   OrthoDB; 9807278at2; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000000799; 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; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 1.20.1180.10; Udp N-acetylglucosamine O-acyltransferase, C-terminal domain; 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   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; 1.
DR   PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 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; Reference proteome; Repeat;
KW   Transferase.
FT   CHAIN           1..263
FT                   /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT                   O-acyltransferase"
FT                   /id="PRO_0000188038"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   TURN            100..103
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   STRAND          104..108
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   STRAND          190..194
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   HELIX           196..202
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   HELIX           205..219
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   HELIX           224..232
FT                   /evidence="ECO:0007829|PDB:3R0S"
FT   HELIX           238..249
FT                   /evidence="ECO:0007829|PDB:3R0S"
SQ   SEQUENCE   263 AA;  28651 MW;  C3D17D1BE12F9F01 CRC64;
     MKKIHPSAVI EEGAQLGDDV VIEAYAYVSK DAKIGNNVVI KQGARILSDT TIGDHSRVFS
     YAIVGDIPQD ISYKEEQKSG VVIGKNATIR EFATINSGTA KGDGFTRIGD NAFIMAYCHI
     AHDCLLGNNI ILANNATLAG HVELGDFTVV GGLTPIHQFV KVGEGCMIAG ASALSQDIVP
     FCLAEGNRAS IRSLNLVGIR RRFDKDEVDR LSRAFKTLFR QGDLKENAKN LLENQESENV
     KKMCHFILET KRGIPVYRGK NNA
//