ID G0AFA0_COLFT Unreviewed; 182 AA.
AC G0AFA0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=CFU_4005 {ECO:0000313|EMBL:AEK63827.1};
OS Collimonas fungivorans (strain Ter331).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK63827.1, ECO:0000313|Proteomes:UP000008392};
RN [1] {ECO:0000313|EMBL:AEK63827.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63827.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT expression of ribosomal RNA genes by large-insert library fluorescent in
RT situ hybridization (LIL-FISH).";
RL Environ. Microbiol. 6:990-998(2004).
RN [2] {ECO:0000313|EMBL:AEK63827.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63827.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT "Genomic flank-sequencing of plasposon insertion sites for rapid
RT identification of functional genes.";
RL J. Microbiol. Methods 66:276-285(2006).
RN [3] {ECO:0000313|EMBL:AEK63827.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63827.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA Leveau J.H.;
RT "Identification and characterization of genes underlying chitinolysis in
RT Collimonas fungivorans Ter331.";
RL FEMS Microbiol. Ecol. 66:123-135(2008).
RN [4] {ECO:0000313|EMBL:AEK63827.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63827.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA Leveau J.H., Uroz S., de Boer W.;
RT "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT solutions to life in oligotrophic soil environments.";
RL Environ. Microbiol. 12:281-292(2010).
RN [5] {ECO:0000313|EMBL:AEK63827.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK63827.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA van den Berg M., Leveau J.H.;
RT "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT Collimonas fungivorans versus Aspergillus niger.";
RL ISME J. 5:1494-1504(2011).
RN [6] {ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA Leveau J.H.;
RT "Complete sequence of Collimonas fungivorans Ter331.";
RL Submitted (MAY-2011) 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; CP002745; AEK63827.1; -; Genomic_DNA.
DR RefSeq; WP_014007979.1; NC_015856.1.
DR AlphaFoldDB; G0AFA0; -.
DR STRING; 1005048.CFU_4005; -.
DR KEGG; cfu:CFU_4005; -.
DR eggNOG; COG3637; Bacteria.
DR HOGENOM; CLU_093405_1_0_4; -.
DR Proteomes; UP000008392; 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|ARBA:ARBA00023237,
KW ECO:0000256|PIRNR:PIRNR029681}; Hydrolase {ECO:0000256|PIRNR:PIRNR029681};
KW Membrane {ECO:0000256|PIRNR:PIRNR029681};
KW Reference proteome {ECO:0000313|Proteomes:UP000008392};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..182
FT /note="Lipid A deacylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003396855"
FT SITE 161
FT /note="Critical for activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR029681-2"
SQ SEQUENCE 182 AA; 19905 MW; 6F3B52B92A43914F CRC64;
MQKKHTGLKL LAAAGLLAGV HSTSFAVDSA SFELGTGNKS QLARVAAQWN WNTALWQGSS
TQLGGYWDLS LAEFRQNQYQ NIPGQKKNLT DIGFTPVFRF QANDKKGLYG EAGIGVHLMS
HLYDNNSRRF STAFEFGDHI GTGYVFSNGL DIGLKLQHFS NGGIKKPNSG ANFAVLRVAY
PF
//
