(data stored in SCRATCH zone)

SWISSPROT: Q145Y4_PARXL

ID   Q145Y4_PARXL            Unreviewed;       187 AA.
AC   Q145Y4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 66.
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=Bxe_A4145 {ECO:0000313|EMBL:ABE28855.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28855.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28855.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28855.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Has lipid A 3-O-deacylase activity. Hydrolyzes the ester
CC       bond 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 =
CC         3-hydroxyacyl derivative of bacterial toxin + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:136853,
CC         ChEBI:CHEBI:140675; EC=3.1.1.77;
CC         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; CP000270; ABE28855.1; -; Genomic_DNA.
DR   RefSeq; WP_011486688.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A4145; -.
DR   EnsemblBacteria; ABE28855; ABE28855; Bxe_A4145.
DR   GeneID; 4002335; -.
DR   KEGG; bxb:DR64_1822; -.
DR   KEGG; bxe:Bxe_A4145; -.
DR   PATRIC; fig|266265.5.peg.336; -.
DR   eggNOG; ENOG41061N2; Bacteria.
DR   eggNOG; ENOG4112AQW; LUCA.
DR   HOGENOM; HOG000264842; -.
DR   OMA; AYTYWDG; -.
DR   OrthoDB; 1863236at2; -.
DR   BioCyc; BXEN266265:BXE_RS01580-MONOMER; -.
DR   Proteomes; UP000001817; 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   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   3: Inferred from homology;
DR   PRODOM; Q145Y4.
DR   SWISS-2DPAGE; Q145Y4.
KW   Cell outer membrane {ECO:0000256|PIRNR:PIRNR029681};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR029681};
KW   Membrane {ECO:0000256|PIRNR:PIRNR029681};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    187       Lipid A deacylase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5004182913.
FT   SITE        166    166       Critical for activity.
FT                                {ECO:0000256|PIRSR:PIRSR029681-2}.
SQ   SEQUENCE   187 AA;  20622 MW;  C9240A35FA954DF2 CRC64;
     MNNKKNVLRD LALKITAGAV LVGASGVASA DQFGVQVAGG LGDRHVKKLD LGFVWDPDLN
     WWQIGDWHFS LIGEAHVAWW HTNEGNVHDN IGEVGVTPII RFIKESGPIR PYAELGAGIR
     LLSSPRISST FTLGTAFQFA DMAGVGMQFG NRQQYQAGYR FQHISNGGIK EPNPGINFHQ
     LYLQYNF
//

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