ID F9ZYC0_METMM Unreviewed; 256 AA.
AC F9ZYC0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=Metme_2639 {ECO:0000313|EMBL:AEG01025.1};
OS Methylomonas methanica (strain MC09).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG01025.1, ECO:0000313|Proteomes:UP000008888};
RN [1] {ECO:0000313|EMBL:AEG01025.1, ECO:0000313|Proteomes:UP000008888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC09 {ECO:0000313|EMBL:AEG01025.1,
RC ECO:0000313|Proteomes:UP000008888};
RX PubMed=22123758; DOI=10.1128/JB.06267-11;
RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA Stein L., Murrell J.C.;
RT "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT methanica MC09.";
RL J. Bacteriol. 193:7001-7002(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MC09;
RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA Stein L.Y., Murrell C.;
RT "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT methanica MC09.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000008888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT "Complete sequence of Methylomonas methanica MC09.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; CP002738; AEG01025.1; -; Genomic_DNA.
DR RefSeq; WP_013819261.1; NC_015572.1.
DR AlphaFoldDB; F9ZYC0; -.
DR STRING; 857087.Metme_2639; -.
DR KEGG; mmt:Metme_2639; -.
DR eggNOG; COG1043; Bacteria.
DR HOGENOM; CLU_061249_0_0_6; -.
DR OrthoDB; 9807278at2; -.
DR UniPathway; UPA00359; UER00477.
DR Proteomes; UP000008888; 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; 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; 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:UP000008888};
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..254
FT /note="UDP N-acetylglucosamine O-acyltransferase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF13720"
SQ SEQUENCE 256 AA; 28058 MW; 027CC6376AA96578 CRC64;
MIDARAVINP KAELAEDVTV GPFSIIGPDV QIDAGTEIGP HVVIKGPTSI GKDNQIYQFT
SIGEDPQDKK YADEVTRLEI GDRNVIREFC TMHRGTLQDQ GLTKIGDDNL FMAYTHVAHD
CMIGDHVIMA NGASIAGHVH VGDHAILGGF TLVHQFTQIG EYSFSAMGSA ITQDIPPFVM
VGGRPTRPHG INSVGMERNG KSPEVIRQIR QAYKILYKNN LRLEDAIEEM EGMAGESNEL
SNMVSFLRNV TRGILR
//