ESTA_BACSU
ID ESTA_BACSU Reviewed; 212 AA.
AC P37957; O34644; Q2XU59;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Lipase EstA;
DE AltName: Full=Lipase A;
DE EC=3.1.1.3 {ECO:0000269|PubMed:11029590, ECO:0000269|PubMed:8396026};
DE AltName: Full=Triacylglycerol lipase;
DE Flags: Precursor;
GN Name=estA;
GN Synonyms=lip {ECO:0000303|PubMed:1320940},
GN lipA {ECO:0000303|PubMed:11029590}; OrderedLocusNames=BSU02700;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=168;
RX PubMed=1320940; DOI=10.1016/0167-4781(92)90023-s;
RA Dartois V., Baulard A., Schanck K., Colson C.;
RT "Cloning, nucleotide sequence and expression in Escherichia coli of a
RT lipase gene from Bacillus subtilis 168.";
RL Biochim. Biophys. Acta 1131:253-260(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9274031; DOI=10.1099/00221287-143-8-2775;
RA Kumano M., Tamakoshi A., Yamane K.;
RT "A 32 kb nucleotide sequence from the region of the lincomycin-resistance
RT gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and
RT identification of the site of the lin-2 mutation.";
RL Microbiology 143:2775-2782(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Peerzada K., Johri S., Rasool S., Qazi G.N.;
RT "Molecular characterization of a lipase from a strain of Bacillus
RT subtilis.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, INDUCTION, AND N-TERMINAL END.
RC STRAIN=168;
RX PubMed=8396026; DOI=10.1111/j.1432-1033.1993.tb18127.x;
RA Lesuisse E., Schanck K., Colson C.;
RT "Purification and preliminary characterization of the extracellular lipase
RT of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme.";
RL Eur. J. Biochem. 216:155-160(1993).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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 [7]
RP PROBABLE ACTIVE SITE, SUBCELLULAR LOCATION, AND INDUCTION.
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).
RN [8] {ECO:0007744|PDB:1I6W}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 32-212, PROBABLE ACTIVE SITE, AND
RP PROBABLE SUBUNIT.
RC STRAIN=168;
RX PubMed=11491291; DOI=10.1006/jmbi.2001.4659;
RA van Pouderoyen G., Eggert T., Jaeger K.-E., Dijkstra B.W.;
RT "The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta
RT hydrolase fold enzyme.";
RL J. Mol. Biol. 309:215-226(2001).
RN [9] {ECO:0007744|PDB:1ISP}
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 32-212, PROBABLE ACTIVE SITE, AND
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=12077437; DOI=10.1107/s090744490200714x;
RA Kawasaki K., Kondo H., Suzuki M., Ohgiya S., Tsuda S.;
RT "Alternate conformations observed in catalytic serine of Bacillus subtilis
RT lipase determined at 1.3 A resolution.";
RL Acta Crystallogr. D 58:1168-1174(2002).
CC -!- FUNCTION: Active toward triacylglycerides with a preference for esters
CC with C8:0 acyl groups; barely active on C18:1 or C18:4 substrates.
CC Active against p-nitrophenylesters with fatty acid chain lengths from
CC C6 to C18. {ECO:0000269|PubMed:11029590, ECO:0000269|PubMed:8396026,
CC ECO:0000305|PubMed:1320940}.
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, ECO:0000269|PubMed:8396026};
CC -!- ACTIVITY REGULATION: Strongly inhibited when incubated with the serine
CC reagent phenylmethylsulfonyl fluoride. Activated by the addition of
CC calcium to the reaction mixture. When calcium was incubated with the
CC lipase but not added to the reaction mixture, its effect is lower but
CC still observable. Magnesium, manganese and strontium are not able to
CC replace calcium with full retention of activity.
CC {ECO:0000269|PubMed:8396026}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10 (PubMed:11029590). The activity decreases strongly
CC above pH 10.5 or below pH 6.5. The enzyme is remarkably stable at
CC alkaline pH, showing maximum stability at pH 12 and retaining more
CC than 65% of its activity after 24 hours at pH 13 (PubMed:8396026).
CC {ECO:0000269|PubMed:11029590, ECO:0000269|PubMed:8396026};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. Stable for at least 30
CC minutes at 40 degrees Celsius. Virtually no activity remains after 30
CC minutes at 55 degrees Celsius. {ECO:0000269|PubMed:11029590,
CC ECO:0000269|PubMed:8396026};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11491291,
CC ECO:0000269|PubMed:12077437}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11583117,
CC ECO:0000269|PubMed:8396026}.
CC -!- INDUCTION: Maximally expressed in late exponential growth phase.
CC Expression decreases rapidly in the stationary phase. Expressed in both
CC rich and minimal media with glucose as carbon source (at protein
CC level). {ECO:0000269|PubMed:11583117, ECO:0000269|PubMed:8396026}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; M74010; AAA22574.1; -; Genomic_DNA.
DR EMBL; AB000617; BAA22231.1; -; Genomic_DNA.
DR EMBL; DQ250714; ABB54395.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12064.1; -; Genomic_DNA.
DR PIR; S23934; S23934.
DR RefSeq; NP_388152.1; NC_000964.3.
DR RefSeq; WP_003246250.1; NZ_JNCM01000030.1.
DR PDB; 1I6W; X-ray; 1.50 A; A/B=32-212.
DR PDB; 1ISP; X-ray; 1.30 A; A=32-212.
DR PDB; 1R4Z; X-ray; 1.80 A; A/B=32-212.
DR PDB; 1R50; X-ray; 1.45 A; A/B=32-212.
DR PDB; 1T2N; X-ray; 1.80 A; A=32-212.
DR PDB; 1T4M; X-ray; 2.00 A; A=32-212.
DR PDB; 2QXT; X-ray; 2.00 A; A/B=34-212.
DR PDB; 2QXU; X-ray; 1.90 A; A/B/C/D/E/F/G/H=34-212.
DR PDB; 3D2A; X-ray; 1.73 A; A=32-212.
DR PDB; 3D2B; X-ray; 1.95 A; A/B=32-212.
DR PDB; 3D2C; X-ray; 2.18 A; A/B/C/D/E/F/G/H/I/J/K/L=32-212.
DR PDB; 3QMM; X-ray; 1.89 A; A/B=32-212.
DR PDB; 3QZU; X-ray; 1.85 A; A/B=32-212.
DR PDB; 5CRI; X-ray; 1.63 A; A/B=32-212.
DR PDB; 5CT4; X-ray; 1.49 A; A/B=33-212.
DR PDB; 5CT5; X-ray; 1.75 A; A/B=33-212.
DR PDB; 5CT6; X-ray; 1.90 A; A/B=33-212.
DR PDB; 5CT8; X-ray; 1.29 A; A=33-212.
DR PDB; 5CT9; X-ray; 1.40 A; A=33-212.
DR PDB; 5CTA; X-ray; 1.24 A; A=33-212.
DR PDB; 5CUR; X-ray; 1.30 A; A=33-212.
DR PDBsum; 1I6W; -.
DR PDBsum; 1ISP; -.
DR PDBsum; 1R4Z; -.
DR PDBsum; 1R50; -.
DR PDBsum; 1T2N; -.
DR PDBsum; 1T4M; -.
DR PDBsum; 2QXT; -.
DR PDBsum; 2QXU; -.
DR PDBsum; 3D2A; -.
DR PDBsum; 3D2B; -.
DR PDBsum; 3D2C; -.
DR PDBsum; 3QMM; -.
DR PDBsum; 3QZU; -.
DR PDBsum; 5CRI; -.
DR PDBsum; 5CT4; -.
DR PDBsum; 5CT5; -.
DR PDBsum; 5CT6; -.
DR PDBsum; 5CT8; -.
DR PDBsum; 5CT9; -.
DR PDBsum; 5CTA; -.
DR PDBsum; 5CUR; -.
DR AlphaFoldDB; P37957; -.
DR BMRB; P37957; -.
DR SMR; P37957; -.
DR STRING; 224308.BSU02700; -.
DR DrugBank; DB08475; [(4R)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl hydrogen hex-5-enylphosphonate.
DR DrugBank; DB08548; [(4S)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl hydrogen hex-5-enylphosphonate.
DR ESTHER; bacsu-lip; Lipase_2.
DR PaxDb; P37957; -.
DR PRIDE; P37957; -.
DR EnsemblBacteria; CAB12064; CAB12064; BSU_02700.
DR GeneID; 938389; -.
DR KEGG; bsu:BSU02700; -.
DR PATRIC; fig|224308.179.peg.280; -.
DR eggNOG; COG1075; Bacteria.
DR InParanoid; P37957; -.
DR OMA; MIVMNYL; -.
DR PhylomeDB; P37957; -.
DR BioCyc; BSUB:BSU02700-MON; -.
DR SABIO-RK; P37957; -.
DR EvolutionaryTrace; P37957; -.
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; IDA:CACAO.
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 3D-structure; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000305|PubMed:8396026"
FT CHAIN 32..212
FT /note="Lipase EstA"
FT /id="PRO_0000017819"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:11491291,
FT ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:11491291,
FT ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437"
FT ACT_SITE 187
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:11491291,
FT ECO:0000305|PubMed:11583117, ECO:0000305|PubMed:12077437"
FT CONFLICT 29
FT /note="A -> V (in Ref. 3; ABB54395)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="A -> G (in Ref. 3; ABB54395)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="Q -> H (in Ref. 3; ABB54395)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="L -> V (in Ref. 1; AAA22574 and 3; ABB54395)"
FT /evidence="ECO:0000305"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:5CTA"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 79..97
FT /evidence="ECO:0007829|PDB:5CTA"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5CTA"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5CTA"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:5CTA"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:5CTA"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:5CTA"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:5CTA"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:5CTA"
SQ SEQUENCE 212 AA; 22791 MW; B8A70E027461188F CRC64;
MKFVKRRIIA LVTILMLSVT SLFALQPSAK AAEHNPVVMV HGIGGASFNF AGIKSYLVSQ
GWSRDKLYAV DFWDKTGTNY NNGPVLSRFV QKVLDETGAK KVDIVAHSMG GANTLYYIKN
LDGGNKVANV VTLGGANRLT TGKALPGTDP NQKILYTSIY SSADMIVMNY LSRLDGARNV
QIHGVGHIGL LYSSQVNSLI KEGLNGGGQN TN
