LPXA_PSEA7
ID LPXA_PSEA7 Reviewed; 258 AA.
AC A6V1E4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=PSPA7_1495;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR84073.1; -; Genomic_DNA.
DR RefSeq; WP_003092373.1; NC_009656.1.
DR PDB; 5DEM; X-ray; 1.81 A; A/B/C/D/E/F=1-258.
DR PDB; 5DEP; X-ray; 2.16 A; A/B/C/D/E/F=1-258.
DR PDB; 5DG3; X-ray; 2.30 A; A/B/C/D/E/F=1-258.
DR PDB; 6UEE; X-ray; 2.10 A; A/B/C/D/E/F=1-258.
DR PDB; 6UEG; X-ray; 2.00 A; A/B/C/D/E/F=1-258.
DR PDB; 7OJ6; X-ray; 1.84 A; A/B/C=1-258.
DR PDB; 7OJP; X-ray; 2.84 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-258.
DR PDB; 7OJQ; X-ray; 1.87 A; A/B/C=1-258.
DR PDB; 7OJW; X-ray; 1.72 A; A/B/C=1-258.
DR PDB; 7OJY; X-ray; 2.00 A; A/B/C=1-258.
DR PDB; 7OK1; X-ray; 1.92 A; A/B/C=1-258.
DR PDB; 7OK2; X-ray; 2.89 A; 1/2/3/4/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z=1-258.
DR PDB; 7OKA; X-ray; 2.74 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-258.
DR PDBsum; 5DEM; -.
DR PDBsum; 5DEP; -.
DR PDBsum; 5DG3; -.
DR PDBsum; 6UEE; -.
DR PDBsum; 6UEG; -.
DR PDBsum; 7OJ6; -.
DR PDBsum; 7OJP; -.
DR PDBsum; 7OJQ; -.
DR PDBsum; 7OJW; -.
DR PDBsum; 7OJY; -.
DR PDBsum; 7OK1; -.
DR PDBsum; 7OK2; -.
DR PDBsum; 7OKA; -.
DR AlphaFoldDB; A6V1E4; -.
DR SMR; A6V1E4; -.
DR PRIDE; A6V1E4; -.
DR EnsemblBacteria; ABR84073; ABR84073; PSPA7_1495.
DR KEGG; pap:PSPA7_1495; -.
DR HOGENOM; CLU_061249_0_0_6; -.
DR OMA; ECVTINR; -.
DR OrthoDB; 971098at2; -.
DR BRENDA; 2.3.1.129; 5087.
DR UniPathway; UPA00359; UER00477.
DR Proteomes; UP000001582; 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; 2.
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; Repeat; Transferase.
FT CHAIN 1..258
FT /note="Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine
FT O-acyltransferase"
FT /id="PRO_1000013171"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:7OK2"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5DEM"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7OJW"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:7OJW"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:7OJW"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:7OJW"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:7OJW"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:7OJW"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:7OJW"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:7OJW"
SQ SEQUENCE 258 AA; 28010 MW; B40E9923058E259E CRC64;
MSLIDPRAII DPSARLAADV QVGPWSIVGA EVEIGEGTVI GPHVVLKGPT KIGKHNRIYQ
FSSVGEDTPD LKYKGEPTRL VIGDHNVIRE GVTIHRGTVQ DRAETTIGDH NLIMAYAHIG
HDSVIGNHCI LVNNTALAGH VHVDDWAILS GYTLVHQYCR IGAHSFSGMG SAIGKDVPAY
VTVFGNPAEA RSMNFEGMRR RGFSSEAIHA LRRAYKVVYR QGHTVEEALA ELAESAAQFP
EVAVFRDSIQ SATRGITR
