ID J3EKK8_9PSED Unreviewed; 172 AA.
AC J3EKK8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=PMI21_03757 {ECO:0000313|EMBL:EJM14400.1};
OS Pseudomonas sp. GM18.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144324 {ECO:0000313|EMBL:EJM14400.1, ECO:0000313|Proteomes:UP000007280};
RN [1] {ECO:0000313|EMBL:EJM14400.1, ECO:0000313|Proteomes:UP000007280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM18 {ECO:0000313|EMBL:EJM14400.1,
RC ECO:0000313|Proteomes:UP000007280};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM14400.1}.
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DR EMBL; AKJT01000072; EJM14400.1; -; Genomic_DNA.
DR RefSeq; WP_007939764.1; NZ_AKJT01000072.1.
DR AlphaFoldDB; J3EKK8; -.
DR PATRIC; fig|1144324.3.peg.3674; -.
DR OrthoDB; 9797122at2; -.
DR Proteomes; UP000007280; 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|PIRNR:PIRNR029681};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR029681};
KW Membrane {ECO:0000256|PIRNR:PIRNR029681}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..172
FT /note="Lipid A deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003765919"
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; 18862 MW; 8D3D86765992D4E5 CRC64;
MKRLFCLAAI ATALMGHSFT AQAAGVEFGV GQTSDSTMTY RLGMQFDWDK SWLQSDVGRL
TGYWSGAYTY WDGDKTASNH SLSFSPVLVY EFAGQTIKPY VEAGIGVAVF ANTEYEDNKL
GSAFQFEDRF GFGLRFAGGH EVGIRATHYS NAGISNPNDG VESYALHYTM PL
//
