ID F6G917_RALS8 Unreviewed; 187 AA.
AC F6G917;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 Name=pagL {ECO:0000313|EMBL:AEG71457.1};
GN OrderedLocusNames=RSPO_m00819 {ECO:0000313|EMBL:AEG71457.1};
OS Ralstonia solanacearum (strain Po82).
OG Plasmid {ECO:0000313|Proteomes:UP000007953}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1031711 {ECO:0000313|EMBL:AEG71457.1, ECO:0000313|Proteomes:UP000007953};
RN [1] {ECO:0000313|EMBL:AEG71457.1, ECO:0000313|Proteomes:UP000007953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Po82 {ECO:0000313|Proteomes:UP000007953};
RX PubMed=21685279; DOI=10.1128/JB.05384-11;
RA Xu J., Zheng H.J., Liu L., Pan Z.C., Prior P., Tang B., Xu J.S., Zhang H.,
RA Tian Q., Zhang L.Q., Feng J.;
RT "Complete genome sequence of the plant pathogen Ralstonia solanacearum
RT strain Po82.";
RL J. Bacteriol. 193:4261-4262(2011).
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; CP002820; AEG71457.1; -; Genomic_DNA.
DR RefSeq; WP_003261236.1; NC_017575.1.
DR AlphaFoldDB; F6G917; -.
DR GeneID; 69783783; -.
DR KEGG; rsn:RSPO_m00819; -.
DR PATRIC; fig|1031711.3.peg.4033; -.
DR HOGENOM; CLU_093405_0_0_4; -.
DR Proteomes; UP000007953; Plasmid megaplasmid.
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 Plasmid {ECO:0000313|EMBL:AEG71457.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..187
FT /note="Lipid A deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003334588"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-1"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-1"
FT ACT_SITE 177
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-1"
FT SITE 166
FT /note="Critical for activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-2"
SQ SEQUENCE 187 AA; 20858 MW; BA11B8547B59053D CRC64;
MIRSALPRSA KPLAAALAAA TLLAAAPAQA DPSVRAIYGR DNRHGIEKYG VDIDFDSGFH
WGNPQGWFLN LDWEIALGQW RSTKGTNRQN LTEFGVTPLF RLEKRGGSWV PFIEAGIGPR
LLSHTRTSDE HNFSTAFQFS DMIGVGVAFG SRQQFQVGYR FEHLSNASIK RPNPGTDLNE
LYLRYTF
//
