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Database: UniProt
Entry: B0B9Y4
LinkDB: B0B9Y4
Original site: B0B9Y4 
ID   LPXA_CHLTB              Reviewed;         280 AA.
AC   B0B9Y4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   01-OCT-2014, entry version 53.
DE   RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE            Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000255|HAMAP-Rule:MF_00387};
DE            EC=2.3.1.129 {ECO:0000255|HAMAP-Rule:MF_00387};
GN   Name=lpxA {ECO:0000255|HAMAP-Rule:MF_00387};
GN   OrderedLocusNames=CTLon_0788;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J.,
RA   Marsh P., Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H.,
RA   Harris B., Ormond D., Rance R., Quail M.A., Parkhill J.,
RA   Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of lipid A, a
CC       phosphorylated glycolipid that anchors the lipopolysaccharide to
CC       the outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC   -!- CATALYTIC ACTIVITY: (R)-3-hydroxytetradecanoyl-[acyl-carrier-
CC       protein] + UDP-N-acetyl-alpha-D-glucosamine = [acyl-carrier-
CC       protein] + UDP-3-O-(3-hydroxytetradecanoyl)-N-acetyl-alpha-D-
CC       glucosamine. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC   -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid
CC       IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and
CC       UDP-N-acetyl-alpha-D-glucosamine: step 1/6. {ECO:0000255|HAMAP-
CC       Rule:MF_00387}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00387}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       LpxA subfamily. {ECO:0000255|HAMAP-Rule:MF_00387}.
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DR   EMBL; AM884177; CAP07185.1; -; Genomic_DNA.
DR   RefSeq; YP_001653876.1; NC_010280.2.
DR   ProteinModelPortal; B0B9Y4; -.
DR   STRING; 471473.CTLon_0788; -.
DR   EnsemblBacteria; CAP07185; CAP07185; CTLon_0788.
DR   GeneID; 5859493; -.
DR   KEGG; ctl:CTLon_0788; -.
DR   PATRIC; 20383265; VBIChlTra68089_0853.
DR   eggNOG; COG1043; -.
DR   HOGENOM; HOG000294326; -.
DR   KO; K00677; -.
DR   OMA; DCQDKKY; -.
DR   OrthoDB; EOG6F81P1; -.
DR   BioCyc; CTRA471473:GHJK-827-MONOMER; -.
DR   UniPathway; UPA00359; UER00477.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1180.10; -; 1.
DR   HAMAP; MF_00387; LpxA; 1.
DR   InterPro; IPR029098; Acetyltransf_C.
DR   InterPro; IPR001451; Hexapep_transf.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR010137; Lipid_A_LpxA.
DR   InterPro; IPR011004; Trimer_LpxA-like.
DR   Pfam; PF13720; Acetyltransf_11; 1.
DR   Pfam; PF00132; Hexapep; 4.
DR   PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01852; lipid_A_lpxA; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Complete proteome; Cytoplasm; Lipid A biosynthesis;
KW   Lipid biosynthesis; Lipid metabolism; Repeat; Transferase.
FT   CHAIN         1    280       Acyl-[acyl-carrier-protein]--UDP-N-
FT                                acetylglucosamine O-acyltransferase.
FT                                /FTId=PRO_1000122696.
SQ   SEQUENCE   280 AA;  30724 MW;  362F2E9AC33A4F34 CRC64;
     MTNIHPTAIV EDGARIGNNV TIEPYAIVKK SVTLCDDVVV KSYAYIDGFT TIGRGTTVWP
     SAMIGNKPQD LKFKGEKTFV EIGEHCEIRE FAMITSSTFE GTTVSIGNNC LIMPWAHIAH
     NCSVGNNVVF STHVQLAGHV QVGDCVTIGS MVGVHQFVRI GSYSMVGAMS GIRRDIPPFT
     IGTGNPYALG GINKVGLQRR QVSFETRLAL IKTFKRVFRS DESFQASLES VLEDFGEVPE
     VRHFVEFCRQ PSKRGIERGV DCEASLEEPI DKKEGAFVES
//
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