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Database: UniProt
Entry: V2J4F0_9BURK
LinkDB: V2J4F0_9BURK
Original site: V2J4F0_9BURK 
ID   V2J4F0_9BURK            Unreviewed;       190 AA.
AC   V2J4F0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   03-MAY-2023, entry version 30.
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=B551_0208230 {ECO:0000313|EMBL:ESJ21945.1};
OS   Cupriavidus sp. HPC(L).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ21945.1, ECO:0000313|Proteomes:UP000053474};
RN   [1] {ECO:0000313|EMBL:ESJ21945.1, ECO:0000313|Proteomes:UP000053474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA   Purohit H.J., Agarwal L.;
RT   "Cupriavidus a Desert isolate.";
RL   Submitted (AUG-2013) 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:ESJ21945.1}.
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DR   EMBL; AMPR02000107; ESJ21945.1; -; Genomic_DNA.
DR   RefSeq; WP_023263830.1; NZ_AMPR02000107.1.
DR   AlphaFoldDB; V2J4F0; -.
DR   OrthoDB; 5297282at2; -.
DR   Proteomes; UP000053474; 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:UP000053474};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..190
FT                   /note="Lipid A deacylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004704617"
FT   SITE            169
FT                   /note="Critical for activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR029681-2"
SQ   SEQUENCE   190 AA;  21012 MW;  21DB02E1D536F807 CRC64;
     MTQQQERTAR SLRRSAALCC AAAALIVAAP AQADPAVHVA YGRDPGHGLN KYEIGLNWDS
     GFAYGNPQGW LAKLQWEVEL ARWNARTGNN RRDVTEIGFS PILRVEKHGW SVVPFAELSV
     GLRLMSATST SDSHDYSTAF QFSDMVGVGV AFGPQKRAEA GFRFQHISNA SIKRPNPGTN
     FYTGYVRYRF
//
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