PAGL_BORBR
ID PAGL_BORBR Reviewed; 178 AA.
AC Q7WD07;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Lipid A deacylase PagL {ECO:0000303|PubMed:21764941};
DE EC=3.1.1.77 {ECO:0000269|PubMed:21764941};
DE AltName: Full=LPS 3-O-deacylase PagL {ECO:0000303|PubMed:21764941};
DE AltName: Full=Outer membrane enzyme PagL {ECO:0000250|UniProtKB:Q9HVD1};
DE Flags: Precursor;
GN Name=pagL {ECO:0000250|UniProtKB:Q9HVD1}; OrderedLocusNames=BB3771;
OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS (Alcaligenes bronchisepticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257310;
RN [1] {ECO:0000312|EMBL:CAE35745.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50 {ECO:0000269|PubMed:21764941};
RX PubMed=21764941; DOI=10.1128/jb.01502-10;
RA MacArthur I., Jones J.W., Goodlett D.R., Ernst R.K., Preston A.;
RT "Role of pagL and lpxO in Bordetella bronchiseptica lipid A biosynthesis.";
RL J. Bacteriol. 193:4726-4735(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:0000269|PubMed:21764941}.
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:0000269|PubMed:21764941};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9HVD1}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:Q9HVD1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9HVD1}.
CC -!- DOMAIN: Consists mainly of an outer membrane-spanning beta-barrel
CC formed by beta-strands both N- and C-terminus residing in the
CC periplasm. {ECO:0000250|UniProtKB:Q9HVD1, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Increase in relative abundance of 3-OH C10 in
CC lipid A. The most abundant ion detected in lipid A structure contains
CC the addition of a 3-OH C10 acyl chain and a second phosphate group
CC compared to the most abundant ion observed from wild-type lipid A.
CC {ECO:0000269|PubMed:21764941}.
CC -!- SIMILARITY: Belongs to the PagL family. {ECO:0000250|UniProtKB:Q9HVD1}.
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DR EMBL; BX640448; CAE35745.1; -; Genomic_DNA.
DR RefSeq; WP_003813842.1; NC_002927.3.
DR AlphaFoldDB; Q7WD07; -.
DR SMR; Q7WD07; -.
DR STRING; 257310.BB3771; -.
DR EnsemblBacteria; CAE35745; CAE35745; BB3771.
DR GeneID; 56477746; -.
DR GeneID; 66439652; -.
DR KEGG; bbr:BB3771; -.
DR eggNOG; COG3637; Bacteria.
DR HOGENOM; CLU_093405_1_0_4; -.
DR OMA; ELRGHWD; -.
DR OrthoDB; 1863236at2; -.
DR Proteomes; UP000001027; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050528; F:acyloxyacyl hydrolase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0046493; P:lipid A metabolic process; IDA:UniProtKB.
DR GO; GO:0008653; P:lipopolysaccharide metabolic process; IDA:UniProtKB.
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; SSF56925; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Hydrolase; Membrane; Signal; Transmembrane;
KW Transmembrane beta strand.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..178
FT /note="Lipid A deacylase PagL"
FT /evidence="ECO:0000255"
FT /id="PRO_0000422913"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9HVD1"
FT ACT_SITE 156
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9HVD1"
FT ACT_SITE 168
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q9HVD1"
FT SITE 157
FT /note="Critical for activity"
FT /evidence="ECO:0000250|UniProtKB:Q9HVD1"
SQ SEQUENCE 178 AA; 19824 MW; ABAD2385F64AEDBF CRC64;
MQFLKKNKPL FGIVTLALAC ATAQAQPTQG GVSLHYGIGD HYQRVTLNYE TPTLWSHQFG
GNWGRLDLTP ELGASYWWAD GSRSPGHVWQ ASAIPMFRWW TGERFYIEAG IGATVFSSTS
FADKRIGSAF QFGDHIGLGF LLTPSNRIGL RYSHFSNAGI KEPNPGLDIV QLTYTYQF
