ID   LPXB_CHLCV              Reviewed;         626 AA.
AC   Q821Z3;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Lipid-A-disaccharide synthase;
DE            EC=2.4.1.182;
GN   Name=lpxB; OrderedLocusNames=CCA_00792;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
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; AE015925; AAP05533.1; -; Genomic_DNA.
DR   RefSeq; WP_011006747.1; NC_003361.3.
DR   AlphaFoldDB; Q821Z3; -.
DR   SMR; Q821Z3; -.
DR   STRING; 227941.CCA_00792; -.
DR   CAZy; GT19; Glycosyltransferase Family 19.
DR   EnsemblBacteria; AAP05533; AAP05533; CCA_00792.
DR   KEGG; cca:CCA_00792; -.
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; UP000002193; 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..626
FT                   /note="Lipid-A-disaccharide synthase"
FT                   /id="PRO_0000190158"
FT   REGION          1..225
FT                   /note="Unknown"
FT   REGION          226..626
FT                   /note="Lipid-A-disaccharide synthase"
SQ   SEQUENCE   626 AA;  71491 MW;  61DEC1BED06E1B38 CRC64;
     MLPLYLVHVL YPIGLIANLF FGSAFTIQWL LSEKRKTAYV PKAFWVLSSI GAVMMIAHGF
     IQSQFPMALL HGANLVIYFR NLNIASSYKL SLTTTLVILV LTLLVTTLPF ALAAYYYPYM
     EWMASPNFFH LPLPPPNIYW HIVGCLGLFT FSSRFFIQWC YLEMNNHSTL PALFWQAGFV
     GGFLAFIYFI RTGDPVNILS YGCGLLPSLA NLRIIYKKSR LPKFHSPSCF LSAGEPSGDT
     LGSDLLRNIK ELNPNIHCFG VGGPLMRKEG LEPLIRMEEF QVSGFLEVFC AVFSLYKKYR
     KLYKAILKEN PETVFCIDFP DFHFFLIRKL RKCGYRGKII HYVCPSIWAW RPNRKKILEK
     HLDTLLLILP FEKEIFKDSP LKTIYLGHPL VKTIANFQDC NAWKQQLEIS DQPSVALFPG
     SRPGDIFRNL QVQARAFRSS SLAKSHQLLV SSCNPKYDKK ILELLDKEGC HNNKIVPSKF
     RYQLMRDCDC ALAKCGTIVL EAALNQTPTI VTCLLRPFDT FLAKYIFKIF IPAYSLPNII
     TGSVIFPEFI GGKHDFSPEE VAAAIDILAN PIGKEKQKYA CQQLLKTMTE NVITPKECLQ
     AIYAQKNRFY LKNDFIKEFH PKSSRA