ID   LIP2_STRCO              Reviewed;         295 AA.
AC   Q93J06;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Lipase 2;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   OrderedLocusNames=SCO7513; ORFNames=SCBAC25F8.05c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   FUNCTION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   DOI=10.1016/j.enzmictec.2008.01.009;
RA   Cote A., Shareck F.;
RT   "Cloning, purification and characterization of two lipases from
RT   Streptomyces coelicolor A3(2).";
RL   Enzyme Microb. Technol. 42:381-388(2008).
CC   -!- FUNCTION: Catalyzes the hydrolysis of fatty acid esters with a
CC       preference for long chain fatty acids (C16-C18). {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC   -!- ACTIVITY REGULATION: Strongly inhibited by Ag(+). The cations Ca(2+)
CC       and Mg(2+) do not significantly reduce the lipolytic activity of
CC       SCO7513, whereas high concentrations of Co(2+) and Cu(2+) partially
CC       inhibit it. Is not inhibited by DTT in vitro. Is resistant to PMSF
CC       inhibition, except in the presence of Ca(2+). {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5-9. Active from pH 8 to 10. Rapidly loses its
CC         activity when incubated at pH in the range between 6.5 and 11 for 24
CC         hours. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 45-55 degrees Celsius. The activity drops
CC         quickly at temperatures below 30 degrees Celsius.
CC         {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AL939131; CAC42140.1; -; Genomic_DNA.
DR   RefSeq; NP_631558.1; NC_003888.3.
DR   RefSeq; WP_011031714.1; NZ_VNID01000005.1.
DR   AlphaFoldDB; Q93J06; -.
DR   SMR; Q93J06; -.
DR   STRING; 100226.SCO7513; -.
DR   GeneID; 1102951; -.
DR   KEGG; sco:SCO7513; -.
DR   PATRIC; fig|100226.15.peg.7626; -.
DR   eggNOG; COG2755; Bacteria.
DR   HOGENOM; CLU_038449_4_1_11; -.
DR   InParanoid; Q93J06; -.
DR   OMA; CLRSTAN; -.
DR   PhylomeDB; Q93J06; -.
DR   BRENDA; 3.1.1.3; 5998.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR   GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR   CDD; cd01823; SEST_like; 1.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR037460; SEST-like.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR37981; PTHR37981; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..295
FT                   /note="Lipase 2"
FT                   /id="PRO_0000407312"
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        138..152
FT                   /evidence="ECO:0000250"
FT   DISULFID        205..254
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   295 AA;  30494 MW;  F56F8FE80DEA167F CRC64;
     MPKPALRRVM TATVAAVGTL ALGLTDATAH AAPAQATPTL DYVALGDSYS AGSGVLPVDP
     ANLLCLRSTA NYPHVIADTT GARLTDVTCG AAQTADFTRA QYPGVAPQLD ALGTGTDLVT
     LTIGGNDNST FINAITACGT AGVLSGGKGS PCKDRHGTSF DDEIEANTYP ALKEALLGVR
     ARAPHARVAA LGYPWITPAT ADPSCFLKLP LAAGDVPYLR AIQAHLNDAV RRAAEETGAT
     YVDFSGVSDG HDACEAPGTR WIEPLLFGHS LVPVHPNALG ERRMAEHTMD VLGLD