ID   LPXB_PERMH              Reviewed;         379 AA.
AC   C0QR27;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Lipid-A-disaccharide synthase {ECO:0000255|HAMAP-Rule:MF_00392};
DE            EC=2.4.1.182 {ECO:0000255|HAMAP-Rule:MF_00392};
GN   Name=lpxB {ECO:0000255|HAMAP-Rule:MF_00392};
GN   OrderedLocusNames=PERMA_1354;
OS   Persephonella marina (strain DSM 14350 / EX-H1).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Persephonella.
OX   NCBI_TaxID=123214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14350 / EX-H1;
RX   PubMed=19136599; DOI=10.1128/jb.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
CC   -!- FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-
CC       diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor
CC       of lipid A, a phosphorylated glycolipid that anchors the
CC       lipopolysaccharide to the outer membrane of the cell.
CC       {ECO:0000255|HAMAP-Rule:MF_00392}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-
CC         glucosamine = a lipid A disaccharide + H(+) + UDP;
CC         Xref=Rhea:RHEA:67828, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:137748, ChEBI:CHEBI:176338, ChEBI:CHEBI:176343;
CC         EC=2.4.1.182; Evidence={ECO:0000255|HAMAP-Rule:MF_00392};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00392}.
CC   -!- SIMILARITY: Belongs to the LpxB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00392}.
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DR   EMBL; CP001230; ACO03161.1; -; Genomic_DNA.
DR   RefSeq; WP_012675400.1; NC_012440.1.
DR   AlphaFoldDB; C0QR27; -.
DR   SMR; C0QR27; -.
DR   STRING; 123214.PERMA_1354; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   PaxDb; 123214-PERMA_1354; -.
DR   KEGG; pmx:PERMA_1354; -.
DR   eggNOG; COG0763; Bacteria.
DR   HOGENOM; CLU_036577_3_1_0; -.
DR   OrthoDB; 9801642at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001366; Chromosome.
DR   GO; GO:0008915; F:lipid-A-disaccharide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00392; LpxB; 1.
DR   InterPro; IPR003835; Glyco_trans_19.
DR   NCBIfam; TIGR00215; lpxB; 1.
DR   PANTHER; PTHR30372; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   PANTHER; PTHR30372:SF7; LIPID-A-DISACCHARIDE SYNTHASE; 1.
DR   Pfam; PF02684; LpxB; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..379
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_1000191488"
SQ   SEQUENCE   379 AA;  42965 MW;  185E5B6D6CE3335D CRC64;
     MKKAFISVGE ISGDNYASQL VKALPDFMWV GITGPKMREA GVETVEKLEN ISVVGLMEAL
     PKYFKIKETF KRSVEILDKG IDLLVVVDFP GFNLKLLKEA KKRGIKTVYF IAPQVWAWGK
     GRIPKIAQYT DLLIAIWPFE KEIYTDYISD SFRVEYVGHP ILDIIKTEET EESFKEKIGI
     EKDKKIFGLL PGSRESEVKT LLPILLSSAE IIYRKREDLH FVIPSTPNME ENVKQIAGSK
     KVPLSVITVK DFRHPSYEVM KHSVFLNVAS GTATLETAIF GNPFLLVYKV SPVTFFIGKM
     LVSIDYLGLP NIIAGREIIK ELLQKECNPE SIARWSLRYL EDPEVYERTK NDLEKVKKAL
     GEKGAIKRSA DLIKELSLS
//