EST_BACSU
ID EST_BACSU Reviewed; 246 AA.
AC O32232;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Carboxylesterase;
DE EC=3.1.1.1;
GN Name=est; Synonyms=yvaK; OrderedLocusNames=BSU33620;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17369301; DOI=10.1128/jb.00062-07;
RA Shin J.H., Price C.W.;
RT "The SsrA-SmpB ribosome rescue system is important for growth of Bacillus
RT subtilis at low and high temperatures.";
RL J. Bacteriol. 189:3729-3737(2007).
CC -!- FUNCTION: Involved in the detoxification of xenobiotics. Shows maximal
CC activity with C6 substrates, with gradually decreasing activity from C8
CC to C12 substrates. No activity for higher chain length substrates acids
CC rather than long-chain ones (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INDUCTION: Constitutively expressed, part of a 5 gene operon with
CC multiple promoters. Not ethanol-stress induced.
CC {ECO:0000269|PubMed:17369301}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17369301}.
CC -!- SIMILARITY: Belongs to the lipase/esterase LIP3/BchO family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB15367.2; -; Genomic_DNA.
DR PIR; H70027; H70027.
DR RefSeq; NP_391242.1; NC_000964.3.
DR RefSeq; WP_003242610.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32232; -.
DR SMR; O32232; -.
DR STRING; 224308.BSU33620; -.
DR ESTHER; bacsu-YVAK; CarbLipBact_1.
DR MEROPS; S09.946; -.
DR jPOST; O32232; -.
DR PaxDb; O32232; -.
DR PRIDE; O32232; -.
DR EnsemblBacteria; CAB15367; CAB15367; BSU_33620.
DR GeneID; 938643; -.
DR KEGG; bsu:BSU33620; -.
DR PATRIC; fig|224308.179.peg.3647; -.
DR eggNOG; COG1647; Bacteria.
DR InParanoid; O32232; -.
DR OMA; DWYAEVD; -.
DR BioCyc; BSUB:BSU33620-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012354; Esterase_lipase.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PIRSF; PIRSF017388; Esterase_lipase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..246
FT /note="Carboxylesterase"
FT /id="PRO_0000360656"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 246 AA; 28193 MW; 786A980DDD4F17EC CRC64;
MKVVTPKPFT FKGGDKAVLL LHGFTGNTAD VRMLGRYLNE RGYTCHAPQY EGHGVPPEEL
VHTGPEDWWK NVMDGYEYLK SEGYESIAAC GLSLGGVFSL KLGYTVPIKG IVPMCAPMHI
KSEEVMYQGV LSYARNYKKF EGKSPEQIEE EMKEFEKTPM NTLKALQDLI ADVRNNVDMI
YSPTFVVQAR HDHMINTESA NIIYNEVETD DKQLKWYEES GHVITLDKER DLVHQDVYEF
LEKLDW
