LPXB_CHLMU
ID LPXB_CHLMU Reviewed; 607 AA.
AC Q9PJY4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Lipid-A-disaccharide synthase;
DE EC=2.4.1.182;
GN Name=lpxB; OrderedLocusNames=TC_0692;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE002160; AAF39508.1; -; Genomic_DNA.
DR PIR; E81676; E81676.
DR RefSeq; WP_010231237.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PJY4; -.
DR SMR; Q9PJY4; -.
DR STRING; 243161.TC_0692; -.
DR CAZy; GT19; Glycosyltransferase Family 19.
DR EnsemblBacteria; AAF39508; AAF39508; TC_0692.
DR GeneID; 1246053; -.
DR KEGG; cmu:TC_0692; -.
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; UP000000800; 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..607
FT /note="Lipid-A-disaccharide synthase"
FT /id="PRO_0000190159"
FT REGION 1..224
FT /note="Unknown"
FT REGION 225..607
FT /note="Lipid-A-disaccharide synthase"
SQ SEQUENCE 607 AA; 69198 MW; F794FD9B10FBB259 CRC64;
MFPQKITLWL YPLGLFANLF FGTAFCVQWF LIKKRGCSFV PKIFWHLSCS GAVLMICHGF
IQSQYPIALL HSFNLIIYFR NLNIASSTPL PISKIVSLLV VSATAITLSF AIGTQYLPHM
TWMASPNILH LNLPEANFLW QLIGCIGLTI FSLRFFIQWF YLEYKNQSSL PTPFWKASLV
GGSICLIYFL RTGDIVNVLC YGCGLFPSLA NLRIASREAI QKPFSCSCFI SAGEHSGDTL
GGNLLKEIHA KYPDIHCFGV GGPQMRAQNF CTLFSMEKFQ ISGFWEVLLA LPKLWYRRRI
LYKTILKRNP QAVICIDFPD FHFLLIKKLR SLGYKGKIVH YVCPSIWAWR PSRKTTLEKY
LDLLLLILPF EQKLFKDSPL RTVYIGHPLS ETIKLFCPKQ NWKERLHLPT DKPFVAAFPG
SRHSDILRNL TIQVQAFQAS DFASTHHLLV SSANPAYDHL ILEILQQNRC LHSNIVPSQF
RYELMRECDC ALAKCGTIVL ETALNLTPTI VTCQLRPLDT FLAKYIFNII LPAYSLPNII
LGRTIFPEFI GGKKDFRYED VAAALNILKT SQAQEKQKNA CKDVYQAINE SASTIKECLP
FIFEASY