LPXA_CAMJE
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 03-AUG-2022, entry version 127.
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 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; 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; NC_002163.1.
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; Q9PIM1; -.
DR PRIDE; Q9PIM1; -.
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 OMA; ECVTINR; -.
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; 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; 3.
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; 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
