ID A0A0X1SXT4_PSEAA Unreviewed; 172 AA.
AC A0A0X1SXT4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AWM79_02985 {ECO:0000313|EMBL:AMB84319.1};
OS Pseudomonas agarici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB84319.1, ECO:0000313|Proteomes:UP000063229};
RN [1] {ECO:0000313|EMBL:AMB84319.1, ECO:0000313|Proteomes:UP000063229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB84319.1,
RC ECO:0000313|Proteomes:UP000063229};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) 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}.
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DR EMBL; CP014135; AMB84319.1; -; Genomic_DNA.
DR RefSeq; WP_017130629.1; NZ_JACAQG010000029.1.
DR AlphaFoldDB; A0A0X1SXT4; -.
DR STRING; 46677.AWM79_02985; -.
DR OrthoDB; 9797122at2; -.
DR Proteomes; UP000063229; Chromosome.
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|PIRNR:PIRNR029681};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR029681};
KW Membrane {ECO:0000256|PIRNR:PIRNR029681};
KW Reference proteome {ECO:0000313|Proteomes:UP000063229}.
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-1"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-1"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-1"
FT SITE 151
FT /note="Critical for activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-2"
SQ SEQUENCE 172 AA; 18789 MW; 7E61737C0439F737 CRC64;
MKRLFCLAVL AAATLGYGVT AQAAGLEFSV GQTGDSTEVY RLGLQSDWDK SWLQSNVGRL
TGYWSGAYSY WDGDTKSSNH SLSFSPVFVY EFSGTSIKPY LEAGIGVALF AHTELEDNQL
GSSFQFEDRL GFGLRFAGGH ELGVRATHYS NAGIRMPNDG VESYALHYTM PL
//
