ID B3R4D8_CUPTR Unreviewed; 191 AA.
AC B3R4D8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=RALTA_A1206 {ECO:0000313|EMBL:CAQ69170.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ69170.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ69170.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ69170.1; -; Genomic_DNA.
DR RefSeq; WP_012352498.1; NC_010528.1.
DR AlphaFoldDB; B3R4D8; -.
DR GeneID; 29760626; -.
DR KEGG; cti:RALTA_A1206; -.
DR eggNOG; COG3637; Bacteria.
DR HOGENOM; CLU_093405_0_0_4; -.
DR BioCyc; CTAI977880:RALTA_RS05770-MONOMER; -.
DR Proteomes; UP000001692; Chromosome 1.
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 Lipoprotein {ECO:0000313|EMBL:CAQ69170.1};
KW Membrane {ECO:0000256|PIRNR:PIRNR029681}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..191
FT /note="Lipid A deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002797840"
FT SITE 170
FT /note="Critical for activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-2"
SQ SEQUENCE 191 AA; 20682 MW; D9513300AF100B9F CRC64;
MSVKIKNAAR WSPAAAAVSF ATCLLALPGA AGAAGFSLQA GYGRDNRHGV EKYEVSARWD
EIVQWQLSNR LALALDGEVN VANWRALSSR PSSQLTEFGV SPIFRLSYAG EHVTPFVEAS
VGLRVLSHTE IAGGHRMGSA FQFSDMIGVG VAFGKARRLT VGYRFQHLSN AGIQDPNPGT
NFSMGYVRYR F
//
