SBLE_STABO
ID SBLE_STABO Reviewed; 410 AA.
AC S5ZJC7;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Lactone esterase;
DE Short=SBLE;
DE EC=3.1.1.-;
DE AltName: Full=Lactonase;
DE AltName: Full=Lipase-like enzyme SBLE;
DE Flags: Precursor;
GN Name=sble; Synonyms=lip1;
OS Starmerella bombicola (Yeast) (Candida bombicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Starmerella.
OX NCBI_TaxID=75736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RA Van Bogaert I., Ciesielska K., Roelants S., Devreese B., Soeatert W.;
RT "A lactonase derived from Candida bombicola and uses thereof.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 22214 / CBS 6009 / JCM 9596 / NBRC 10243 / NRRL Y-17069;
RX PubMed=24418522; DOI=10.1016/j.jprot.2013.12.026;
RA Ciesielska K., Van Bogaert I.N., Chevineau S., Li B., Groeneboer S.,
RA Soetaert W., Van de Peer Y., Devreese B.;
RT "Exoproteome analysis of Starmerella bombicola results in the discovery of
RT an esterase required for lactonization of sophorolipids.";
RL J. Proteomics 98:159-174(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP SER-194, AND GLYCOSYLATION.
RX PubMed=27251547; DOI=10.1007/s00253-016-7633-2;
RA Ciesielska K., Roelants S.L., Van Bogaert I.N., De Waele S.,
RA Vandenberghe I., Groeneboer S., Soetaert W., Devreese B.;
RT "Characterization of a novel enzyme -- Starmerella bombicola lactone
RT esterase (SBLE) -- responsible for sophorolipid lactonization.";
RL Appl. Microbiol. Biotechnol. 100:9529-9541(2016).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=26301720; DOI=10.1002/bit.25815;
RA Roelants S.L., Ciesielska K., De Maeseneire S.L., Moens H., Everaert B.,
RA Verweire S., Denon Q., Vanlerberghe B., Van Bogaert I.N.,
RA Van der Meeren P., Devreese B., Soetaert W.;
RT "Towards the industrialization of new biosurfactants: Biotechnological
RT opportunities for the lactone esterase gene from Starmerella bombicola.";
RL Biotechnol. Bioeng. 113:550-559(2016).
CC -!- FUNCTION: Responsible for the lactonization of acidic sophorolipids
CC (SLs). Catalyzes the intramolecular esterification (ring closure)
CC between the carboxyl group of the hydroxy fatty acid and the hydroxyl
CC group of sophorose C6'' of acidic SLs. Lactonizes acetylated acidic
CC SLs, producing di-acetylated C18:2, C18:1 and C18:0 lactonic SL, and
CC mono-acetylated C18:1 lactonic SL. Does not catalyze the reverse
CC reaction, the hydrolysis of lactonic SL into acidic SL, nor hydrolysis
CC of triglycerides or paranitrophenyl esters.
CC {ECO:0000269|PubMed:27251547}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 mM for acidic sophorolipids {ECO:0000269|PubMed:27251547};
CC pH dependence:
CC Optimum pH is 3.5-6. Stable from pH 3.5 to pH 8.
CC {ECO:0000269|PubMed:27251547};
CC Temperature dependence:
CC Optimum temperature is 20-50 degrees Celsius.
CC {ECO:0000269|PubMed:27251547};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24418522}.
CC -!- PTM: Glycosylated. {ECO:0000305|PubMed:27251547}.
CC -!- DISRUPTION PHENOTYPE: Results in the production of exclusively acidic
CC sophorolipids and a complete absence of any lactonic sophorolipids.
CC {ECO:0000269|PubMed:24418522}.
CC -!- BIOTECHNOLOGY: Sophorolipids (SLs) are a family of fungal
CC biosurfactants that have been commercialized as biodegradable
CC detergents in ecological cleaning solutions. They naturally exist in
CC two forms, a closed lactone and an open acidic form. Each form has
CC distinct properties, acidic SLs have better foaming properties, while
CC lactonic SLs are better in surface tension reduction and have
CC antimicrobial activity. Lactone esterase, catalyzing the final
CC conversion of the open acidic to the closed lactonic form, provides a
CC biotechnological opportunity to engineer and regulate the production of
CC SLs in S.bombicola, which naturally produces a mixture of acidic and
CC lactonic SLs. {ECO:0000305|PubMed:26301720}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000255|PIRNR:PIRNR029171}.
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; KC121031; AGT29866.1; -; Genomic_DNA.
DR AlphaFoldDB; S5ZJC7; -.
DR SMR; S5ZJC7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005152; Lipase_secreted.
DR PANTHER; PTHR34853; PTHR34853; 1.
DR Pfam; PF03583; LIP; 1.
DR PIRSF; PIRSF029171; Esterase_LipA; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Lipid biosynthesis; Lipid metabolism; Secreted;
KW Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..410
FT /note="Lactone esterase"
FT /id="PRO_0000443095"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT ACT_SITE 346
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT ACT_SITE 378
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:W3VKA4"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 194
FT /note="S->A: Abolishes ability to lactonise sophorolipids."
FT /evidence="ECO:0000269|PubMed:27251547"
SQ SEQUENCE 410 AA; 45561 MW; F5498E02B94D0B23 CRC64;
MLALFFSLAP LLSQALPLGY TAAPAESFYF WPENISSLQA GEIFRKRELL TLPDIFDFGP
NLEKVVQVAY KTRLTDGNDS FSIASIFIPK NPSPELKLYS YQTFEDAVQL DCAPSYALEV
GNKSSNYLPV TSNLSAISRE LEKGRHCIIP DHEGYISGFF AGRQEGYAGL DGIRAARNYL
NGTNETPIGI FGYSGGAQAT AWIVDLHDEY APDLNFVGTV SGGTLVDAWG TFQYIDYPKV
YLKGSILIMY TGLFSGYPAQ FEVIWPYIEP VIQENMLLLR LAPNDCNQSP ILQGYNNSIM
AGIHVDLPEF PASKYIFQHE SLLANYSVVP VSTPKFPRYM YHGGSDELAK LSLVEQYVDQ
QWNTGANLTF VVYPGLLHDE TAYRGFDAAM DWLDAQLDSG YLPPVNSTHT
