ID K7ZY88_9ENTR Unreviewed; 262 AA.
AC K7ZY88;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 55.
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 ORFNames=BN137_813 {ECO:0000313|EMBL:CCJ71473.1};
OS Cronobacter condimenti 1330.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=1073999 {ECO:0000313|EMBL:CCJ71473.1, ECO:0000313|Proteomes:UP000009340};
RN [1] {ECO:0000313|EMBL:CCJ71473.1, ECO:0000313|Proteomes:UP000009340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330 {ECO:0000313|EMBL:CCJ71473.1,
RC ECO:0000313|Proteomes:UP000009340};
RX PubMed=23166675; DOI=10.1371/journal.pone.0049455;
RA Joseph S., Desai P., Ji Y., Cummings C.A., Shih R., Degoricija L., Rico A.,
RA Brzoska P., Hamby S.E., Masood N., Hariri S., Sonbol H., Chuzhanova N.,
RA McClelland M., Furtado M.R., Forsythe S.J.;
RT "Comparative analysis of genome sequences covering the seven cronobacter
RT species.";
RL PLoS ONE 7:e49455-e49455(2012).
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:CCJ71473.1}.
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DR EMBL; CAKW01000035; CCJ71473.1; -; Genomic_DNA.
DR RefSeq; WP_007666665.1; NZ_CP012264.1.
DR AlphaFoldDB; K7ZY88; -.
DR STRING; 1073999.AFK62_04070; -.
DR KEGG; ccon:AFK62_04070; -.
DR PATRIC; fig|1073999.7.peg.829; -.
DR eggNOG; COG1043; Bacteria.
DR OrthoDB; 9807278at2; -.
DR UniPathway; UPA00359; UER00477.
DR Proteomes; UP000009340; 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; 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; IPR018357; Hexapep_transf_CS.
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.
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="UDP N-acetylglucosamine O-acyltransferase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF13720"
SQ SEQUENCE 262 AA; 28148 MW; 671FD0B275CFF7B7 CRC64;
MIDKTAFIHP TAIVEDGAVI GANAHIGPFC IVGPHVEIGE GTVLKSHVVV NGHTKIGRDN
EIYQFASIGE VNQDLKYAGE PTRVEIGDRN RIRESVTIHR GTEQGGGLTK VGSDNLLMIN
AHIAHDCTVG SRCILANNAT LAGHVSVDDF AIIGGMTAVH QFCIIGAHVM VGGCSGVAQD
VPPYVIAQGN HATPFGVNIE GLKRRGFSKE ALHAIRNAYK LLYRSGKTLD EVKPEIAEIA
AKHPEVQPFY DFFARSTRGL IR
//
