ID   PLDB_ECOL6              Reviewed;         340 AA.
AC   P59588;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Lysophospholipase L2;
DE            EC=3.1.1.5;
DE   AltName: Full=Lecithinase B;
GN   Name=pldB; OrderedLocusNames=c4747;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014075; AAN83180.1; -; Genomic_DNA.
DR   RefSeq; WP_000487654.1; NC_004431.1.
DR   AlphaFoldDB; P59588; -.
DR   SMR; P59588; -.
DR   STRING; 199310.c4747; -.
DR   ESTHER; ecoli-pldb; Monoglyceridelipase_lysophospholip.
DR   EnsemblBacteria; AAN83180; AAN83180; c4747.
DR   GeneID; 66672267; -.
DR   KEGG; ecc:c4747; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_026209_10_1_6; -.
DR   OMA; AFDWRGQ; -.
DR   BioCyc; ECOL199310:C4747-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR022742; Hydrolase_4.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Lipid biosynthesis;
KW   Lipid metabolism; Membrane.
FT   CHAIN           1..340
FT                   /note="Lysophospholipase L2"
FT                   /id="PRO_0000058455"
SQ   SEQUENCE   340 AA;  38978 MW;  A032DB05FD203C05 CRC64;
     MFQQQKDWET RENAFAAFTM GPLTDFWRQR DEAEFTGVDD IPVRFVRFRA QHHDRVVVIC
     PGRIESYVKY AELAYDLFHL GFDVLIIDHR GQGRSGRLLA DPHLGHVNRF NDYVDDLAAF
     WQQEVQPGPW RKRYILAHSM GGAISTLFLQ RHPGVCDAIA LTAPMFGIVI RMPSFMARQI
     LNWAEAHPRF RDGYAIGTGR WRALPFAINV LTHSRQRYRR NLRFYADDPT IRVGGPTYHW
     VRESILAGEQ VLAGAGDDAT PTLLLQAEEE RVVDNRMHDR FCELRTAAGH PVEGGRPLVI
     KGAYHEILFE KDAMRSVALH AIVDFFNRHN SPSGNRSTEV