ID A0A0Q5PD94_9BURK Unreviewed; 188 AA.
AC A0A0Q5PD94;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Lipid A deacylase {ECO:0000256|PIRNR:PIRNR029681};
DE EC=3.1.1.77 {ECO:0000256|PIRNR:PIRNR029681};
DE AltName: Full=LPS 3-O-deacylase {ECO:0000256|PIRNR:PIRNR029681};
DE AltName: Full=Outer membrane enzyme {ECO:0000256|PIRNR:PIRNR029681};
GN ORFNames=ASG35_06235 {ECO:0000313|EMBL:KQR79497.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR79497.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR79497.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR79497.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR79497.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR79497.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has lipid A 3-O-deacylase activity. Hydrolyzes the ester bond
CC at the 3 position of lipid A, a bioactive component of
CC lipopolysaccharide (LPS), thereby releasing the primary fatty acyl
CC moiety. {ECO:0000256|PIRNR:PIRNR029681}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-
CC hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+);
CC Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:136853, ChEBI:CHEBI:140675;
CC EC=3.1.1.77; Evidence={ECO:0000256|PIRNR:PIRNR029681};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR029681}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|PIRNR:PIRNR029681}; Multi-pass membrane protein
CC {ECO:0000256|PIRNR:PIRNR029681}.
CC -!- SIMILARITY: Belongs to the PagL family.
CC {ECO:0000256|PIRNR:PIRNR029681}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQR79497.1}.
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DR EMBL; LMPF01000020; KQR79497.1; -; Genomic_DNA.
DR RefSeq; WP_056357999.1; NZ_LMPF01000020.1.
DR AlphaFoldDB; A0A0Q5PD94; -.
DR OrthoDB; 5297282at2; -.
DR Proteomes; UP000051826; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050528; F:acyloxyacyl hydrolase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.160.20; -; 1.
DR InterPro; IPR018550; Lipid-A_deacylase-rel.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR Pfam; PF09411; PagL; 1.
DR PIRSF; PIRSF029681; PagL; 1.
DR SUPFAM; SSF56925; OMPA-like; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237,
KW ECO:0000256|PIRNR:PIRNR029681}; Hydrolase {ECO:0000256|PIRNR:PIRNR029681};
KW Membrane {ECO:0000256|PIRNR:PIRNR029681};
KW Reference proteome {ECO:0000313|Proteomes:UP000051826};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..188
FT /note="Lipid A deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006258691"
FT SITE 167
FT /note="Critical for activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-2"
SQ SEQUENCE 188 AA; 21060 MW; 64E5D0559B595F36 CRC64;
MQKNKSVWQK RSFYGALLGA LALVSASAKA DQFGVQVAGG VADHDVRKAD VGVVWDPNLT
WWEIGGFHFT VVGEAHVAYW DIRESNAAHP NIWEFGLTPV FRFIKSSGWF RPYVEAGVGV
RLLSHVRETQ DRTFSSSFQF ADMVGVGAQF GARQNYQAGF RFQHLSNAGI EHPNPGINFS
QIYLQYNF
//
