ID   PLDB_HAEIN              Reviewed;         313 AA.
AC   P44800;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable lysophospholipase L2;
DE            EC=3.1.1.5;
DE   AltName: Full=Lecithinase B;
GN   Name=pldB; OrderedLocusNames=HI_0645;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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}.
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DR   EMBL; L42023; AAC22305.1; -; Genomic_DNA.
DR   PIR; A64084; A64084.
DR   RefSeq; NP_438805.1; NC_000907.1.
DR   RefSeq; WP_005694498.1; NC_000907.1.
DR   AlphaFoldDB; P44800; -.
DR   SMR; P44800; -.
DR   STRING; 71421.HI_0645; -.
DR   ESTHER; haein-pldb; Monoglyceridelipase_lysophospholip.
DR   EnsemblBacteria; AAC22305; AAC22305; HI_0645.
DR   KEGG; hin:HI_0645; -.
DR   PATRIC; fig|71421.8.peg.674; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_026209_10_1_6; -.
DR   OMA; AFDWRGQ; -.
DR   PhylomeDB; P44800; -.
DR   BioCyc; HINF71421:G1GJ1-680-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR   GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..313
FT                   /note="Probable lysophospholipase L2"
FT                   /id="PRO_0000058457"
SQ   SEQUENCE   313 AA;  36658 MW;  891E784FF7F77C2E CRC64;
     MIREPYFHQF ALAELLPFFE QFPTQYLSGK RNIKLAYRHL IQPESAVRKL MILVNGRAEN
     MLKWSELAYD FYHQGYDVLL FDHRGQGYSQ RIIPQKGHLD EFRFYVDDMA KIIEKVTALF
     SYSTQHLLAH SMGALIATYY LANYDHHINK AVLSSPFYGI LLKHPIRDEL IITLMNILGQ
     GERYVFGKGA YQQAHLEYNE LTFCKTRMKW MNRINRKNPA INLGGPTFRW VHLCLNAIKR
     LPKVIPKIEI PILILQAEKE KIVDNKNLEK LTALFPNARC EVILNAKHEV LFEKDNVRRN
     VLKSVNHFLN VQS