ID A0A1S1NTL2_9GAMM Unreviewed; 255 AA.
AC A0A1S1NTL2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE EC=2.3.1.129 {ECO:0000256|HAMAP-Rule:MF_00387};
GN Name=lpxA {ECO:0000256|HAMAP-Rule:MF_00387,
GN ECO:0000313|EMBL:QEL11967.1};
GN ORFNames=BH688_08650 {ECO:0000313|EMBL:OHV10481.1}, FY550_13020
GN {ECO:0000313|EMBL:QEL11967.1};
OS Kushneria phosphatilytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Kushneria.
OX NCBI_TaxID=657387 {ECO:0000313|EMBL:OHV10481.1, ECO:0000313|Proteomes:UP000179907};
RN [1] {ECO:0000313|EMBL:OHV10481.1, ECO:0000313|Proteomes:UP000179907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCWA18 {ECO:0000313|EMBL:OHV10481.1,
RC ECO:0000313|Proteomes:UP000179907};
RA Wang C., Qu L.;
RT "The draft genome suquence of Kushneria sp. YCWA18.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEL11967.1, ECO:0000313|Proteomes:UP000322553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCWA18 {ECO:0000313|EMBL:QEL11967.1,
RC ECO:0000313|Proteomes:UP000322553};
RA Du G.-X., Qu L.-Y.;
RT "Complete genome sequence of Kushneria sp. YCWA18, a halophilic phosphate-
RT solubilizing bacterium isolated from Daqiao saltern in China.";
RL Submitted (AUG-2019) 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:0000256|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:0000256|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:0000256|HAMAP-
CC Rule:MF_00387}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00387}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKZT01000012; OHV10481.1; -; Genomic_DNA.
DR EMBL; CP043420; QEL11967.1; -; Genomic_DNA.
DR RefSeq; WP_070978456.1; NZ_MKZT01000012.1.
DR AlphaFoldDB; A0A1S1NTL2; -.
DR STRING; 657387.BH688_08650; -.
DR KEGG; kuy:FY550_13020; -.
DR OrthoDB; 9807278at2; -.
DR UniPathway; UPA00359; UER00477.
DR Proteomes; UP000179907; Unassembled WGS sequence.
DR Proteomes; UP000322553; 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; 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; 2.
DR PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_00387}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_00387};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00387};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00387}; Reference proteome {ECO:0000313|Proteomes:UP000179907};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00387};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00387}.
FT DOMAIN 174..253
FT /note="UDP N-acetylglucosamine O-acyltransferase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF13720"
SQ SEQUENCE 255 AA; 27467 MW; DD3A2B4E0F1F98ED CRC64;
MIHPTAIIDP GARLADDVEV GPFSVIGADV EIGSGCVIGS HVVIKGPTTL GCNNRVFQFA
SLGEECQDKK YHGEPTRLVV GDNNVFREGV TVHRGTIQDR GETTIGDHGW FMAYAHVAHD
CVIGDHVIMA NQATLGGHVT LGDHVILGGL AAVHQFCHVG AHSMCGGGSI VTKDIAAFVM
VTGNPARTHG LNAEGLKRRG FESESISELR RAYREVFRSR RTLAEVLEEF DQQSLSPTMQ
QFVDSLKAAK RGLTR
//