ID   LPXB_CHLAB              Reviewed;         627 AA.
AC   Q5L586;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=CAB759;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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. {ECO:0000250}.
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;
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the LpxB family.
CC       {ECO:0000305}.
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DR   EMBL; CR848038; CAH64206.1; -; Genomic_DNA.
DR   RefSeq; WP_011097318.1; NC_004552.2.
DR   AlphaFoldDB; Q5L586; -.
DR   SMR; Q5L586; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; CAH64206; CAH64206; CAB759.
DR   KEGG; cab:CAB759; -.
DR   eggNOG; COG0763; Bacteria.
DR   eggNOG; COG3952; Bacteria.
DR   HOGENOM; CLU_430672_0_0_0; -.
DR   OMA; KIIHYVC; -.
DR   OrthoDB; 149100at2; -.
DR   UniPathway; UPA00973; -.
DR   Proteomes; UP000001012; 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   InterPro; IPR011499; Lipid_A_biosynth_N.
DR   PANTHER; PTHR30372; PTHR30372; 1.
DR   Pfam; PF07578; LAB_N; 2.
DR   Pfam; PF02684; LpxB; 1.
DR   SMART; SM01259; LAB_N; 2.
DR   TIGRFAMs; TIGR00215; lpxB; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Transferase.
FT   CHAIN           1..627
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000255172"
FT   REGION          1..224
FT                   /note="Unknown"
FT   REGION          225..627
FT                   /note="Lipid-A-disaccharide synthase"
SQ   SEQUENCE   627 AA;  71610 MW;  C9A28E903F7C80A1 CRC64;
     MFPLYLVRLL YPIGLIANLF FGFAFTLQWF LSERHKRACV PKAFWIFSSI GAILMIAHGF
     IQSQFPIALL HGANLVIYFR NLNISSSRKL SLKTTLIILA VTLLLTALPF ALEAYYHPNM
     QWMASPNIFH LPLPPPNMYW HMIGCLGLFT FSCRFFIQWC HLEMNNQSTL PVLFWQVGFV
     GGFLAFLYFI RTGDPVNILS YGCGLFPSIA NLRIIYKKSR LSEFHNPSYF ISAGEASGDT
     LGSDLLRHIK ALHPDKRCFG VGGPLMRQEG LEPLIHMEEF QVSGFLEILT SIFTLIKKYR
     KLYKAILKEN PEIVFCIDFP DFHFFLIKKL RKCGYTGKIV HYVCPSIWAW RPKRKKILEK
     YLDTLLLILP FENELFINSP LKTIYLGHPL VKTISNFQHC PSWKQALAIS DQPIVALFPG
     SRPGDILRNL QVHIRAFLAS SLAESHQLLV SSYNLKHDQT ILDLLEKEGC CGKTVPAMYR
     YHLMRDCDCA LAKCGTIALE AALNQTPTIV TCLLRPFDIF LAKYIFKIFM SAYSLPNIIT
     KSIIFPEFIG GKSDFTPEEV AAAIDILANP KSREKQKRAC QTLLETMETN VVTVQECLQT
     IHSLKSRFHT ENDCLGNYVQ KNVRPSF