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Lipid A deacylase PagL (EC 3.1.1.77) (LPS 3-O-deacylase PagL) (Outer membrane enzyme PagL)

 PAGL_BORBR              Reviewed;         178 AA.
Q7WD07;
26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
28-FEB-2018, entry version 65.
RecName: Full=Lipid A deacylase PagL {ECO:0000303|PubMed:21764941};
EC=3.1.1.77 {ECO:0000269|PubMed:21764941};
AltName: Full=LPS 3-O-deacylase PagL {ECO:0000303|PubMed:21764941};
AltName: Full=Outer membrane enzyme PagL {ECO:0000250|UniProtKB:Q9HVD1};
Flags: Precursor;
Name=pagL {ECO:0000250|UniProtKB:Q9HVD1}; OrderedLocusNames=BB3771;
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
(Alcaligenes bronchisepticus).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=257310;
[1] {ECO:0000312|EMBL:CAE35745.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
PubMed=12910271; DOI=10.1038/ng1227;
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis,
Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
[2] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
STRAIN=ATCC BAA-588 / NCTC 13252 / RB50 {ECO:0000269|PubMed:21764941};
PubMed=21764941; DOI=10.1128/JB.01502-10;
MacArthur I., Jones J.W., Goodlett D.R., Ernst R.K., Preston A.;
"Role of pagL and lpxO in Bordetella bronchiseptica lipid A
biosynthesis.";
J. Bacteriol. 193:4726-4735(2011).
-!- FUNCTION: Has lipid A 3-O-deacylase activity. Hydrolyzes the ester
bond at the 3 position of lipid A, a bioactive component of
lipopolysaccharide (LPS), thereby releasing the primary fatty acyl
moiety. {ECO:0000269|PubMed:21764941}.
-!- CATALYTIC ACTIVITY: 3-(acyloxy)acyl group of bacterial toxin = 3-
hydroxyacyl group of bacterial toxin + a fatty acid.
{ECO:0000269|PubMed:21764941}.
-!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9HVD1}.
-!- SUBCELLULAR LOCATION: Cell outer membrane
{ECO:0000250|UniProtKB:Q9HVD1}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q9HVD1}.
-!- DOMAIN: Consists mainly of an outer membrane-spanning beta-barrel
formed by beta-strands both N- and C-terminus residing in the
periplasm. {ECO:0000250|UniProtKB:Q9HVD1, ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Increase in relative abundance of 3-OH C10
in lipid A. The most abundant ion detected in lipid A structure
contains the addition of a 3-OH C10 acyl chain and a second
phosphate group compared to the most abundant ion observed from
wild-type lipid A. {ECO:0000269|PubMed:21764941}.
-!- SIMILARITY: Belongs to the PagL family.
{ECO:0000250|UniProtKB:Q9HVD1}.
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EMBL; BX640448; CAE35745.1; -; Genomic_DNA.
RefSeq; WP_003813842.1; NC_002927.3.
ProteinModelPortal; Q7WD07; -.
SMR; Q7WD07; -.
STRING; 257310.BB3771; -.
EnsemblBacteria; CAE35745; CAE35745; BB3771.
KEGG; bbr:BB3771; -.
eggNOG; ENOG41061N2; Bacteria.
eggNOG; ENOG4112AQW; LUCA.
HOGENOM; HOG000264842; -.
OMA; RYNFASH; -.
OrthoDB; POG091H0M9N; -.
Proteomes; UP000001027; Chromosome.
GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0050528; F:acyloxyacyl hydrolase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0046493; P:lipid A metabolic process; IDA:UniProtKB.
GO; GO:0008653; P:lipopolysaccharide metabolic process; IDA:UniProtKB.
InterPro; IPR018550; Lipid-A_deacylase-rel.
InterPro; IPR011250; OMP/PagP_b-brl.
Pfam; PF09411; PagL; 1.
PIRSF; PIRSF029681; PagL; 1.
SUPFAM; SSF56925; SSF56925; 1.
1: Evidence at protein level;
Cell outer membrane; Complete proteome; Hydrolase; Membrane; Signal;
Transmembrane; Transmembrane beta strand.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 178 Lipid A deacylase PagL. {ECO:0000255}.
/FTId=PRO_0000422913.
ACT_SITE 154 154 Charge relay system.
{ECO:0000250|UniProtKB:Q9HVD1}.
ACT_SITE 156 156 Charge relay system.
{ECO:0000250|UniProtKB:Q9HVD1}.
ACT_SITE 168 168 Charge relay system.
{ECO:0000250|UniProtKB:Q9HVD1}.
SITE 157 157 Critical for activity.
{ECO:0000250|UniProtKB:Q9HVD1}.
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


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