LPXA_PROMH
ID LPXA_PROMH Reviewed; 267 AA.
AC B4F258;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 88.
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=PMI2273;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AM942759; CAR44497.1; -; Genomic_DNA.
DR RefSeq; WP_004245460.1; NC_010554.1.
DR PDB; 6OSS; X-ray; 2.19 A; A/B/C=1-267.
DR PDBsum; 6OSS; -.
DR AlphaFoldDB; B4F258; -.
DR SMR; B4F258; -.
DR STRING; 529507.PMI2273; -.
DR EnsemblBacteria; CAR44497; CAR44497; PMI2273.
DR GeneID; 6802184; -.
DR KEGG; pmr:PMI2273; -.
DR eggNOG; COG1043; Bacteria.
DR HOGENOM; CLU_061249_0_0_6; -.
DR OMA; ECVTINR; -.
DR UniPathway; UPA00359; UER00477.
DR Proteomes; UP000008319; 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; 2.
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..267
FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT O-acyltransferase"
FT /id="PRO_1000122719"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6OSS"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6OSS"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6OSS"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6OSS"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6OSS"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:6OSS"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:6OSS"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6OSS"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6OSS"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:6OSS"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6OSS"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:6OSS"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:6OSS"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:6OSS"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:6OSS"
SQ SEQUENCE 267 AA; 28944 MW; 1E874BE87E6FE3B3 CRC64;
MIDKSAVIHP SSIIEEGAVI GANVRIGPFC VIGSHVEIGE GTDIKSHVVI NGHTRIGRDN
QIYQFASIGE VNQDLKYRGE PTQVIIGDRN LIRESVTIHR GTTQGGNITK IGNDNLLMIN
THVAHDCIIG DRCIIANNGT LGGHVTLGDY VIIGGMSAVH QFCQIGSHVM VGGCSGVAQD
VPPFVIAQGN HATPYGLNIE GLKRRGFAKE DLHAIRNAYK ILYRNGKTLE EAREEIAQLA
ADNNNQYVKI FSDFLENSAK SNRGIIR
