PLDB_ECOLI
ID PLDB_ECOLI Reviewed; 340 AA.
AC P07000; P78127; Q2M8D0;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 4.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Lysophospholipase L2;
DE EC=3.1.1.5;
DE AltName: Full=Lecithinase B;
GN Name=pldB; OrderedLocusNames=b3825, JW5584;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / KL16-99;
RX PubMed=3908445; DOI=10.1093/oxfordjournals.jbchem.a135347;
RA Kobayashi T., Kudo I., Karasawa K., Mizushima H., Inoue K., Nojima S.;
RT "Nucleotide sequence of the pldB gene and characteristics of deduced amino
RT acid sequence of lysophospholipase L2 in Escherichia coli.";
RL J. Biochem. 98:1017-1025(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 164.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 315.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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 -!- INTERACTION:
CC P07000; Q46864: mqsA; NbExp=2; IntAct=EBI-9134416, EBI-1120353;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
CC -!- MISCELLANEOUS: In addition this protein catalyzes a transacylation
CC reaction to produce acyl phosphatidylglycerol by transfer of the acidyl
CC residue of 2-acyl lysophospholipid to phosphatidylglycerol.
CC -!- MISCELLANEOUS: Lysophospholipases from various sources vary widely in
CC molecular weight, substrate specificity, and subcellular localization.
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DR EMBL; X03155; CAA26932.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67621.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48224.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77476.1; -; Genomic_DNA.
DR PIR; B65187; PSECL2.
DR RefSeq; WP_000487654.1; NZ_STEB01000021.1.
DR RefSeq; YP_026266.1; NC_000913.3.
DR AlphaFoldDB; P07000; -.
DR SMR; P07000; -.
DR BioGRID; 4262616; 219.
DR BioGRID; 852611; 11.
DR IntAct; P07000; 11.
DR STRING; 511145.b3825; -.
DR ESTHER; ecoli-pldb; Monoglyceridelipase_lysophospholip.
DR PaxDb; P07000; -.
DR PRIDE; P07000; -.
DR EnsemblBacteria; AAT48224; AAT48224; b3825.
DR EnsemblBacteria; BAE77476; BAE77476; BAE77476.
DR GeneID; 66672267; -.
DR GeneID; 948314; -.
DR KEGG; ecj:JW5584; -.
DR KEGG; eco:b3825; -.
DR PATRIC; fig|1411691.4.peg.2882; -.
DR EchoBASE; EB0732; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_026209_10_1_6; -.
DR InParanoid; P07000; -.
DR OMA; AFDWRGQ; -.
DR PhylomeDB; P07000; -.
DR BioCyc; EcoCyc:EG10739-MON; -.
DR BioCyc; MetaCyc:EG10739-MON; -.
DR PRO; PR:P07000; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:EcoCyc.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Hydrolase; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome.
FT CHAIN 1..340
FT /note="Lysophospholipase L2"
FT /id="PRO_0000058456"
FT CONFLICT 164
FT /note="P -> A (in Ref. 2; AAA67621)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="R -> A (in Ref. 2; AAA67621)"
FT /evidence="ECO:0000305"
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
