LIP1_STRCO
ID LIP1_STRCO Reviewed; 268 AA.
AC Q9S2A5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Lipase 1;
DE EC=3.1.1.3;
DE AltName: Full=Arylesterase;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN OrderedLocusNames=SCO1725; ORFNames=SCI11.14c;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19041687; DOI=10.1016/j.biochi.2008.10.018;
RA Bielen A., Cetkovic H., Long P.F., Schwab H., Abramic M., Vujaklija D.;
RT "The SGNH-hydrolase of Streptomyces coelicolor has (aryl)esterase and a
RT true lipase activity.";
RL Biochimie 91:390-400(2009).
CC -!- FUNCTION: Catalyzes the hydrolysis of fatty acid esters with a
CC preference for mid-length acyl chain (C10-C16). Is able to hydrolyze
CC the triacylglycerol triolein and mixed triacylglycerols from a wide
CC range of natural oils; better activity is obtained with corn-, wheat
CC germ- and olive oil that have higher content of linoleic and/or oleic
CC acid (C18:2; C18:1, cis). Tween detergents are also substrates for this
CC enzyme. Displays arylesterase activity towards p-nitrophenyl alkanoate
CC esters and alpha- and beta-naphthyl esters.
CC {ECO:0000269|PubMed:19041687, 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 Evidence={ECO:0000269|PubMed:19041687};
CC -!- ACTIVITY REGULATION: Strongly inhibited by Ag(+). The cations Ca(2+),
CC Mg(2+), Co(2+) and Cu(2+) do not significantly reduce the lipolytic
CC activity of SCO1725. Is also inhibited by DTT in vitro, but not by EDTA
CC or by the reagent masking SH-groups, p-hydroxymercuribenzoate (pHMB).
CC Is resistant to PMSF inhibition, except in the presence of Ca(2+). Is
CC also strongly inhibited by 3,4-dichloroisocoumarin (DCI), another
CC inhibitor of serine hydrolases. Addition of tetrahydrofuran and 1,4-
CC dioxane significantly increases (2- and 4- fold, respectively)
CC hydrolytic activity of lipase towards p-nitrophenyl caprylate.
CC {ECO:0000269|PubMed:19041687, ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. Shows high stability over a broad range of pH 4-
CC 9.5 (80-100% of enzyme activity). Becomes unstable at pH over 10,
CC where the activity drops to 34% at pH 10.5 and to 8% at pH 11.
CC {ECO:0000269|PubMed:19041687, ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 20-30 degrees Celsius
CC (DOI=10.1016/j.enzmictec.2008.01.009). The His-tagged protein shows a
CC higher optimum temperature of 55 degrees Celsius, and a thermal
CC denaturation midpoint (Tm) of 66.63 degrees Celsius
CC (PubMed:19041687). Is stable when incubated for 30 minutes at
CC temperatures in the range of 30-70 degrees Celsius at pH 7
CC (DOI=10.1016/j.enzmictec.2008.01.009). {ECO:0000269|PubMed:19041687,
CC ECO:0000269|Ref.2};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19041687}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19041687,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL939110; CAB50940.1; -; Genomic_DNA.
DR PIR; T36747; T36747.
DR RefSeq; NP_625998.1; NC_003888.3.
DR RefSeq; WP_003977101.1; NZ_VNID01000018.1.
DR AlphaFoldDB; Q9S2A5; -.
DR SMR; Q9S2A5; -.
DR STRING; 100226.SCO1725; -.
DR GeneID; 1097156; -.
DR KEGG; sco:SCO1725; -.
DR PATRIC; fig|100226.15.peg.1742; -.
DR eggNOG; COG2755; Bacteria.
DR HOGENOM; CLU_038449_3_0_11; -.
DR InParanoid; Q9S2A5; -.
DR OMA; NIGESYH; -.
DR PhylomeDB; Q9S2A5; -.
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; IDA:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA:UniProtKB.
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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..268
FT /note="Lipase 1"
FT /id="PRO_0000407311"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 250
FT /evidence="ECO:0000250"
FT DISULFID 61..86
FT /evidence="ECO:0000250"
FT DISULFID 127..135
FT /evidence="ECO:0000250"
FT DISULFID 185..231
FT /evidence="ECO:0000250"
SQ SEQUENCE 268 AA; 27394 MW; 31B58E9F134941E3 CRC64;
MRRFRLVGFL SSLVLAAGAA LTGAATAQAA QPAAADGYVA LGDSYSSGVG AGSYISSSGD
CKRSTKAHPY LWAAAHSPST FDFTACSGAR TGDVLSGQLG PLSSGTGLVS ISIGGNDAGF
ADTMTTCVLQ SESSCLSRIA TAEAYVDSTL PGKLDGVYSA ISDKAPNAHV VVIGYPRFYK
LGTTCIGLSE TKRTAINKAS DHLNTVLAQR AAAHGFTFGD VRTTFTGHEL CSGSPWLHSV
NWLNIGESYH PTAAGQSGGY LPVLNGAA
