ESTB_BACSU
ID ESTB_BACSU Reviewed; 210 AA.
AC Q79F14; Q796Z3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Extracellular esterase EstB;
DE EC=3.1.1.3 {ECO:0000269|PubMed:11029590};
DE AltName: Full=Extracellular esterase LipB {ECO:0000303|PubMed:11029590};
DE AltName: Full=Lipase B;
DE AltName: Full=Triacylglycerol lipase;
DE Flags: Precursor;
GN Name=estB;
GN Synonyms=lipB {ECO:0000303|PubMed:11029590},
GN yfiP {ECO:0000303|PubMed:8973323}; OrderedLocusNames=BSU08350;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=8973323; DOI=10.1016/s0378-1119(96)00495-7;
RA Yamamoto H., Uchiyama S., Sekiguchi J.;
RT "The Bacillus subtilis chromosome region near 78 degrees contains the genes
RT encoding a new two-component system, three ABC transporters and a lipase.";
RL Gene 181:147-151(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP PROTEIN SEQUENCE OF 29-38, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF ALA-104; SER-106; ASP-162 AND HIS-185.
RC STRAIN=168 / BCL 1050;
RX PubMed=11029590; DOI=10.1046/j.1432-1327.2000.01736.x;
RA Eggert T., Pencreac'h G., Douchet I., Verger R., Jaeger K.-E.;
RT "A novel extracellular esterase from Bacillus subtilis and its conversion
RT to a monoacylglycerol hydrolase.";
RL Eur. J. Biochem. 267:6459-6469(2000).
RN [4]
RP SUBCELLULAR LOCATION, INDUCTION, AND MUTAGENESIS OF ALA-104.
RC STRAIN=168 / BCL 1050;
RX PubMed=11583117; DOI=10.1016/s0014-5793(01)02665-5;
RA Eggert T., van Pouderoyen G., Dijkstra B.W., Jaeger K.-E.;
RT "Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in
RT regulation of gene expression, biochemical properties, and three-
RT dimensional structure.";
RL FEBS Lett. 502:89-92(2001).
CC -!- FUNCTION: An esterase which preferentially hydrolyzes triacylglyceride
CC substrates with short chain fatty acids (C3-C10) with the maximum
CC activity towards tricaprylin (C8:0); essentially inactive on C18:1 or
CC C18:4 substrates. Active against p-nitrophenylesters with fatty acid
CC chain lengths from C6 to C18. {ECO:0000269|PubMed:11029590}.
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:11029590};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 11-12. {ECO:0000269|PubMed:11029590};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. Stable up to 45 degrees
CC Celsius. {ECO:0000269|PubMed:11029590};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11029590,
CC ECO:0000269|PubMed:11583117}.
CC -!- INDUCTION: Induced in rich but not minimal media with glucose as carbon
CC source (at protein level). Induced by growth on n-hexadecane and
CC tributyrin. {ECO:0000269|PubMed:11583117}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; D78508; BAA11406.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12664.1; -; Genomic_DNA.
DR RefSeq; NP_388716.1; NC_000964.3.
DR RefSeq; WP_003243184.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; Q79F14; -.
DR SMR; Q79F14; -.
DR STRING; 224308.BSU08350; -.
DR ESTHER; bacsu-LIPB; Lipase_2.
DR PaxDb; Q79F14; -.
DR PRIDE; Q79F14; -.
DR EnsemblBacteria; CAB12664; CAB12664; BSU_08350.
DR GeneID; 939715; -.
DR KEGG; bsu:BSU08350; -.
DR PATRIC; fig|224308.179.peg.903; -.
DR eggNOG; COG1075; Bacteria.
DR InParanoid; Q79F14; -.
DR OMA; IQLYGIG; -.
DR PhylomeDB; Q79F14; -.
DR BioCyc; BSUB:BSU08350-MON; -.
DR BRENDA; 3.1.1.23; 658.
DR SABIO-RK; Q79F14; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002918; Lipase_EstA/Esterase_EstB.
DR PANTHER; PTHR32015; PTHR32015; 1.
DR Pfam; PF01674; Lipase_2; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:11029590"
FT CHAIN 29..210
FT /note="Extracellular esterase EstB"
FT /id="PRO_0000361687"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:11029590"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:11029590"
FT ACT_SITE 185
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:11029590"
FT MUTAGEN 104
FT /note="A->G: Enzyme activity changes to monoacylglycerol
FT hydrolase. Marked decrease in temperature stability,
FT decreased stability at pH 11 but increased stability at pH
FT 5."
FT /evidence="ECO:0000269|PubMed:11029590,
FT ECO:0000269|PubMed:11583117"
FT MUTAGEN 106
FT /note="S->C: Complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11029590"
FT MUTAGEN 162
FT /note="D->N: Complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11029590"
FT MUTAGEN 185
FT /note="H->N: Complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:11029590"
SQ SEQUENCE 210 AA; 22363 MW; 4358843F882C690A CRC64;
MKKVLMAFII CLSLILSVLA APPSGAKAES VHNPVVLVHG ISGASYNFFA IKNYLISQGW
QSNKLYAIDF YDKTGNNLNN GPQLASYVDR VLKETGAKKV DIVAHSMGGA NTLYYIKYLG
GGNKIQNVVT LGGANGLVSS TALPGTDPNQ KILYTSIYSL NDQIVINSLS RLQGARNIQL
YGIGHIGLLS NSQVNGYIKE GLNGGGLNTN
