LPXD_CHLTR
ID LPXD_CHLTR Reviewed; 354 AA.
AC P0CD76; O84245; Q9S530;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase;
DE EC=2.3.1.191;
GN Name=lpxD; OrderedLocusNames=CT_243;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [2]
RP IDENTIFICATION OF 3-HYDROXYARACHIDOYL-ACP AS PREDICTED SUBSTRATE, AND
RP FUNCTION.
RC STRAIN=L2;
RX PubMed=10358025; DOI=10.1074/jbc.274.24.16819;
RA Rund S., Lindner B., Brade H., Holst O.;
RT "Structural analysis of the lipopolysaccharide from Chlamydia trachomatis
RT serotype L2.";
RL J. Biol. Chem. 274:16819-16824(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH UDP-GLCNAC AND
RP PALMITATE, ACTIVE SITE, AND SUBUNIT.
RC STRAIN=B;
RX PubMed=17360522; DOI=10.1073/pnas.0606356104;
RA Buetow L., Smith T.K., Dawson A., Fyffe S., Hunter W.N.;
RT "Structure and reactivity of LpxD, the N-acyltransferase of lipid A
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4321-4326(2007).
CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-myristoylglucosamine
CC using 3-hydroxyarachidoyl-ACP as the acyl donor. Is involved in the
CC biosynthesis of lipid A, a phosphorylated glycolipid that anchors the
CC lipopolysaccharide to the outer membrane of the cell (Probable).
CC {ECO:0000305|PubMed:10358025}.
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;
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17360522}.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC subfamily. {ECO:0000305}.
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DR EMBL; AE001273; AAC67836.1; -; Genomic_DNA.
DR PIR; D71539; D71539.
DR RefSeq; NP_219748.1; NC_000117.1.
DR RefSeq; WP_009871590.1; NC_000117.1.
DR PDB; 2IU8; X-ray; 2.20 A; A/B/C=1-354.
DR PDB; 2IU9; X-ray; 3.10 A; A/B/C=1-354.
DR PDB; 2IUA; X-ray; 2.70 A; A/B/C=1-354.
DR PDBsum; 2IU8; -.
DR PDBsum; 2IU9; -.
DR PDBsum; 2IUA; -.
DR AlphaFoldDB; P0CD76; -.
DR SMR; P0CD76; -.
DR DIP; DIP-60889N; -.
DR STRING; 813.O172_01320; -.
DR EnsemblBacteria; AAC67836; AAC67836; CT_243.
DR GeneID; 884880; -.
DR KEGG; ctr:CT_243; -.
DR PATRIC; fig|272561.5.peg.260; -.
DR HOGENOM; CLU_049865_0_0_0; -.
DR InParanoid; P0CD76; -.
DR OMA; QIQIAHN; -.
DR BRENDA; 2.3.1.191; 1315.
DR UniPathway; UPA00973; -.
DR EvolutionaryTrace; P0CD76; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
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; 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; 3.
DR Pfam; PF04613; LpxD; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR TIGRFAMs; TIGR01853; lipid_A_lpxD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Reference proteome; Repeat; Transferase.
FT CHAIN 1..354
FT /note="UDP-3-O-acylglucosamine N-acyltransferase"
FT /id="PRO_0000059665"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:17360522"
FT BINDING 190..192
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT BINDING 240
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:17360522"
FT BINDING 244
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:17360522"
FT BINDING 248
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:17360522"
FT BINDING 266
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:17360522"
FT BINDING 284
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000269|PubMed:17360522"
FT SITE 43
FT /note="Participates in a stacking interaction with the
FT uracil ring of UDP-GlcNAc"
FT SITE 49
FT /note="Participates in a stacking interaction with the
FT uracil ring of UDP-GlcNAc"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:2IU8"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2IU8"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2IU8"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2IU8"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:2IU8"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2IU9"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2IU8"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2IU8"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:2IU8"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:2IU8"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:2IU8"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:2IU8"
SQ SEQUENCE 354 AA; 38404 MW; B9C547C129AE17BB CRC64;
MSQSTYSLEQ LADFLKVEFQ GNGATLLSGV EEIEEAKTAH ITFLDNEKYA KHLKSSEAGA
IIISRTQFQK YRDLNKNFLI TSESPSLVFQ KCLELFITPV DSGFPGIHPT AVIHPTAIIE
DHVCIEPYAV VCQHAHVGSA CHIGSGSVIG AYSTVGEHSY IHPRVVIRER VSIGKRVIIQ
PGAVIGSCGF GYVTSAFGQH KHLKHLGKVI IEDDVEIGAN TTIDRGRFKH SVVREGSKID
NLVQIAHQVE VGQHSMIVAQ AGIAGSTKIG NHVIIGGQAG ITGHICIADH VIMMAQTGVT
KSITSPGIYG GAPARPYQEI HRQVAKVRNL PRLEERIAAL EKLVQKLEAL SEQH
