ID   A0A826TPH7_ECOLX        Unreviewed;       262 AA.
AC   A0A826TPH7;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   12-OCT-2022, entry version 5.
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:EFB6605879.1};
GN   ORFNames=CX938_000221 {ECO:0000313|EMBL:EFB6348634.1}, FQF29_01470
GN   {ECO:0000313|EMBL:EFB6605879.1};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:EFB6605879.1, ECO:0000313|Proteomes:UP000590071};
RN   [1] {ECO:0000313|EMBL:EFB6605879.1, ECO:0000313|Proteomes:UP000590071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CVM N18EC1352 {ECO:0000313|EMBL:EFB6605879.1,
RC   ECO:0000313|Proteomes:UP000590071}, and FSIS11706019
RC   {ECO:0000313|EMBL:EFB6348634.1, ECO:0000313|Proteomes:UP000539866};
RG   NARMS: The National Antimicrobial Resistance Monitoring System;
RL   Submitted (JUL-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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFB6605879.1}.
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; AASGIQ010000002; EFB6348634.1; -; Genomic_DNA.
DR   EMBL; AASGJX010000002; EFB6605879.1; -; Genomic_DNA.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000539866; Unassembled WGS sequence.
DR   Proteomes; UP000590071; Unassembled WGS sequence.
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; 2.
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};
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          180..261
FT                   /note="Acetyltransf_11"
FT                   /evidence="ECO:0000259|Pfam:PF13720"
SQ   SEQUENCE   262 AA;  28061 MW;  748A7B1ED6922219 CRC64;
     MIDKSAFVHP TAIVEEGASI GANAHIGPFC IVGPHVEIGE GTVLKSHVVV NGHTKIGRDN
     EIYQFASIGE VNQDLKYAGE PTRVEIGDHN RIRESVTIHR GTVQGGGLTK VGSDNLLMIN
     AHIAHDCTVG NRCILANNAT LAGHVSVDDF AIIGGMTAVH QFCIIGAHVM VGGCSGVAQD
     VPPYVIAQGN HATPFGVNIE GLKRRGFSRE AITAIRNAYK LIYRSGKTLD EVKPEIAELA
     ETYPEVKAFT DFFARSTRGL IR
//