LPXD_SALTY
ID LPXD_SALTY Reviewed; 341 AA.
AC P0A1X4; P18482;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE Short=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
DE EC=2.3.1.191 {ECO:0000255|HAMAP-Rule:MF_00523};
DE AltName: Full=UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase {ECO:0000255|HAMAP-Rule:MF_00523};
GN Name=lpxD {ECO:0000255|HAMAP-Rule:MF_00523}; Synonyms=firA, ssc;
GN OrderedLocusNames=STM0226;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2256935; DOI=10.1016/s0006-291x(05)81020-4;
RA Hirvas L., Koski P., Vaara M.;
RT "Primary structure and expression of the Ssc-protein of Salmonella
RT typhimurium.";
RL Biochem. Biophys. Res. Commun. 173:53-59(1990).
RN [2]
RP ERRATUM OF PUBMED:2256935.
RA Hirvas L., Koski P., Vaara M.;
RL Biochem. Biophys. Res. Commun. 174:1054-1054(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION OF MUTANT SS-C.
RC STRAIN=LT2 / SH5014;
RX PubMed=2009853; DOI=10.1002/j.1460-2075.1991.tb08036.x;
RA Hirvas L., Koski P., Vaara M.;
RT "Identification and sequence analysis of the gene mutated in the
RT conditionally lethal outer membrane permeability mutant SS-C of Salmonella
RT typhimurium.";
RL EMBO J. 10:1017-1023(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [5]
RP MUTAGENESIS OF VAL-291.
RC STRAIN=LT2 / SH5014;
RX PubMed=6378889; DOI=10.1128/jb.159.2.704-712.1984;
RA Sukupolvi S., Vaara M., Helander I.M., Viljanen P., Makela P.H.;
RT "New Salmonella typhimurium mutants with altered outer membrane
RT permeability.";
RL J. Bacteriol. 159:704-712(1984).
CC -!- FUNCTION: Catalyzes the N-acylation of UDP-3-O-
CC (hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as
CC the acyl donor. Is involved in the biosynthesis of lipid A, a
CC phosphorylated glycolipid that anchors the lipopolysaccharide to the
CC outer membrane of the cell. {ECO:0000255|HAMAP-Rule:MF_00523}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00523};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetradecanoyl-[ACP] + UDP-3-O-[(3R)-3-
CC hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + holo-[ACP] + UDP-
CC 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine;
CC Xref=Rhea:RHEA:17817, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:71573,
CC ChEBI:CHEBI:78474, ChEBI:CHEBI:78847; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00523};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 3/6. {ECO:0000255|HAMAP-
CC Rule:MF_00523}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- MISCELLANEOUS: The SS-C mutant is antibiotic supersensitive; its outer
CC membrane permeability barrier against hydrophobic antibiotics is
CC severely deficient.
CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. LpxD
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00523}.
CC -!- CAUTION: Was originally thought to be involved in transcription.
CC {ECO:0000305}.
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DR EMBL; M35193; AAA27229.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19190.1; -; Genomic_DNA.
DR PIR; B37083; B37083.
DR RefSeq; NP_459231.1; NC_003197.2.
DR RefSeq; WP_001139265.1; NC_003197.2.
DR AlphaFoldDB; P0A1X4; -.
DR SMR; P0A1X4; -.
DR STRING; 99287.STM0226; -.
DR PaxDb; P0A1X4; -.
DR EnsemblBacteria; AAL19190; AAL19190; STM0226.
DR GeneID; 1251744; -.
DR KEGG; stm:STM0226; -.
DR PATRIC; fig|99287.12.peg.239; -.
DR HOGENOM; CLU_049865_0_1_6; -.
DR OMA; QIQIAHN; -.
DR PhylomeDB; P0A1X4; -.
DR BioCyc; SENT99287:STM0226-MON; -.
DR UniPathway; UPA00359; UER00479.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016410; F:N-acyltransferase activity; IEA:InterPro.
DR GO; GO:0103118; F:UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR CDD; cd03352; LbH_LpxD; 1.
DR HAMAP; MF_00523; LpxD; 1.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR018357; Hexapep_transf_CS.
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.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 4.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic resistance; Lipid A biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome; Repeat;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..341
FT /note="UDP-3-O-(3-hydroxymyristoyl)glucosamine N-
FT acyltransferase"
FT /id="PRO_0000059702"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00523"
FT MUTAGEN 291
FT /note="V->M: In SS-C; sensitive to hydrophobic antibiotics
FT and compounds."
FT /evidence="ECO:0000269|PubMed:6378889"
SQ SEQUENCE 341 AA; 35930 MW; 4A8383BCF9DA586E CRC64;
MPSIRLADLA EQLDAELHGD GDIVITGVAS MQSATTGHIT FMVNPKYREH LGLCQASAVV
MTQDDLPFAK SAALVVKNPY LTYARMAQIL DTTPQPAQNI APSAVIDATA TLGSNVSVGA
NAVIESGVQL GDNVVIGAGC FVGKNSKIGA GSRLWANVTI YHDIQIGENC LIQSSTVIGA
DGFGYANDRG NWVKIPQLGR VIIGDRVEIG ACTTIDRGAL DDTVIGNGVI IDNQCQIAHN
VVIGDNTAVA GGVIMAGSLK IGRYCMIGGA SVINGHMEIC DKVTVTGMGM VMRPITEPGV
YSSGIPLQPN KVWRKTAALV MNIDDMSKRL KAIERKVNQQ D
