(data stored in ACNUC1104 zone)

SWISSPROT: Q7WA48_BORPA

ID   Q7WA48_BORPA            Unreviewed;       264 AA.
AC   Q7WA48;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 117.
DE   RecName: Full=Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS00720087};
DE            Short=UDP-N-acetylglucosamine acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387};
DE            EC=2.3.1.129 {ECO:0000256|HAMAP-Rule:MF_00387, ECO:0000256|SAAS:SAAS01080267};
GN   Name=lpxA {ECO:0000256|HAMAP-Rule:MF_00387,
GN   ECO:0000313|EMBL:CAE36841.1};
GN   OrderedLocusNames=BPP1539 {ECO:0000313|EMBL:CAE36841.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS00720116}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-N-acetyl-alpha-D-
CC         glucosamine = holo-[ACP] + UDP-3-O-[(3R)-3-
CC         hydroxytetradecanoyl]-N-acetyl-alpha-D-glucosamine;
CC         Xref=Rhea:RHEA:13925, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:61494, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78474; EC=2.3.1.129; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00387, ECO:0000256|SAAS:SAAS01117058};
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:0000256|HAMAP-
CC       Rule:MF_00387, ECO:0000256|SAAS:SAAS01080285}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS01080283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS00720119}.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
CC       LpxA subfamily. {ECO:0000256|HAMAP-Rule:MF_00387,
CC       ECO:0000256|SAAS:SAAS01080288}.
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DR   EMBL; BX640427; CAE36841.1; -; Genomic_DNA.
DR   RefSeq; WP_010928085.1; NC_002928.3.
DR   EnsemblBacteria; CAE36841; CAE36841; BPP1539.
DR   KEGG; bpa:BPP1539; -.
DR   HOGENOM; HOG000294326; -.
DR   KO; K00677; -.
DR   OMA; ECVTINR; -.
DR   BioCyc; BPAR257311:G1GSY-1579-MONOMER; -.
DR   UniPathway; UPA00359; UER00477.
DR   Proteomes; UP000001421; Chromosome.
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-UniRule.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03351; LbH_UDP-GlcNAc_AT; 1.
DR   Gene3D; 1.20.1180.10; -; 1.
DR   HAMAP; MF_00387; LpxA; 1.
DR   InterPro; IPR029098; Acetyltransf_C.
DR   InterPro; IPR037157; Acetyltransf_C_sf.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR010137; Lipid_A_LpxA.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR43480; PTHR43480; 1.
DR   Pfam; PF13720; Acetyltransf_11; 1.
DR   Pfam; PF00132; Hexapep; 2.
DR   PIRSF; PIRSF000456; UDP-GlcNAc_acltr; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
DR   TIGRFAMs; TIGR01852; lipid_A_lpxA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7WA48.
DR   SWISS-2DPAGE; Q7WA48.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080269, ECO:0000313|EMBL:CAE36841.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS00720062};
KW   Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080263};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080278};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080268};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS00720072};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00387,
KW   ECO:0000256|SAAS:SAAS01080266, ECO:0000313|EMBL:CAE36841.1}.
FT   DOMAIN      177    262       Acetyltransf_11. {ECO:0000259|Pfam:
FT                                PF13720}.
SQ   SEQUENCE   264 AA;  27969 MW;  5387BDF63BBB9E02 CRC64;
     MSGNIHPTAV VDPAAQIDSS VVIGPYSVVG PGVSIAAGTE VGAHCVLDGV TSIGRDNRFY
     RFCSIGGMPQ DKKYSGEPTR LVIGDRNTVR EFTTFNTGTV QDGGVTSIGD DNWIMAYVHI
     AHDCHIGNNT ILANSVQLGG HVQVGDWAIV GGLTGVHQFA KIGAHSMTGS NSSLMQDAPP
     FVLAAGNPCR PVGVNVEGLK RRGFSAAAIS ALRDAYKSIY RRGLSLDEAR AELRARQQAE
     PDVAEHLQTM LDFLDASTRG IIRP
//

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