ID   LPXD2_GLOVI             Reviewed;         373 AA.
AC   Q7NJ21;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00523};
DE            EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
GN   Name=lpxD2 {ECO:0000255|HAMAP-Rule:MF_00523}; OrderedLocusNames=glr2011;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
CC   -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-
CC       hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of
CC       lipid A, a phosphorylated glycolipid that anchors the
CC       lipopolysaccharide to the outer membrane of the cell.
CC       {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-
CC         alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine + H(+) + holo-[ACP]; Xref=Rhea:RHEA:53836, Rhea:RHEA-
CC         COMP:9685, Rhea:RHEA-COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78827, ChEBI:CHEBI:137740, ChEBI:CHEBI:137748;
CC         EC=2.3.1.191; Evidence={ECO:0000255|HAMAP-Rule:MF_00523};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}.
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DR   EMBL; BA000045; BAC89952.1; -; Genomic_DNA.
DR   RefSeq; NP_924957.1; NC_005125.1.
DR   RefSeq; WP_011142009.1; NC_005125.1.
DR   AlphaFoldDB; Q7NJ21; -.
DR   SMR; Q7NJ21; -.
DR   STRING; 251221.35212578; -.
DR   EnsemblBacteria; BAC89952; BAC89952; BAC89952.
DR   KEGG; gvi:glr2011; -.
DR   PATRIC; fig|251221.4.peg.2045; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_049865_0_0_3; -.
DR   InParanoid; Q7NJ21; -.
DR   OrthoDB; 1602061at2; -.
DR   PhylomeDB; Q7NJ21; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProt.
DR   GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0043886; F:structural constituent of carboxysome; IEA:UniProt.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03352; LbH_LpxD; 1.
DR   HAMAP; MF_00523; LpxD; 1.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR007691; LpxD.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   InterPro; IPR020573; UDP_GlcNAc_AcTrfase_non-rep.
DR   PANTHER; PTHR43378; PTHR43378; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   Pfam; PF04613; LpxD; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..373
FT                   /note="UDP-3-O-acylglucosamine N-acyltransferase 2"
FT                   /id="PRO_0000059674"
FT   REGION          345..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        239
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
SQ   SEQUENCE   373 AA;  39027 MW;  27EB88BF750174D8 CRC64;
     MKLSDISAKL GCALEGDGQV DIVGIAGIEE AEAGHLTFLS NPKYKAKLRH TKASAAIVPA
     DFEASAAWPL PLLRHANPYL TFAHAIELFY SPPPAPHGVH PTAVVAPTAV CGHNVRIGAS
     SVIGEGVVLA DGVTVYPNCT IYPGVRIGRN STIHSNCVVR EHVVIGEDCI VQNGAVIGAD
     GFGYAKQADG TWYKIVQSGS VVLENRVEIG ACTTVDRATI GETRIKSGSK LDNLVMIGHG
     SSVGENTLLC GQVGLAGSST VGRNVMLAGQ VGVAGHLHIG DNVVATVKSC IWKSVEANQV
     LYGNIPASDS HTWLKASAVF RQLPHMQKSV QQMQKRIAVL EEPFKTNGKS GQADAPPKVA
     LECHGTTGDA PQG