Reviewed, UniProtKB/Swiss-Prot Q79F14 (ESTB_BACSU)

Names and origin

Protein names

Recommended name:
    Extracellular esterase estB
    EC=3.1.1.3
Alternative name(s):
    Lipase B
    Triacylglycerol lipase

Gene names

Name:	estB
Synonyms:	lipB, yfiP
Ordered Locus Names:	BSU08350

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	An esterase which preferentially hydrolyzes triacylglyceride substrates with short chain fatty acids (less than C10) with the maximum activity towards tricaprylin (C8:0). Active against p-nitrophenylesters with fatty acid chain lengths from C6 to C18.
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Subcellular location	Secreted. Ref.3
Induction	Induced in rich but not minimal media. Ref.4
Sequence similarities	Belongs to the AB hydrolase superfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 11-12. Temperature dependence: Optimum temperature is 37 degrees Celsius. Stable up to 45 degrees Celsuis.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	triglyceride lipase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Ref.3
	Chain	29 – 210	182	Extracellular esterase estB		PRO_0000361687
Sites
	Active site	106	1	Nucleophile
	Active site	162	1	Charge relay system
	Active site	185	1	Charge relay system
Experimental info
	Mutagenesis	104	1	A → G: Enzyme activity changes to monoacylglycerol hydrolase. Marked decrease in temperature stability, decreased stability at pH 11 but increased stability at pH 5. Ref.3
	Mutagenesis	106	1	S → C: Complete loss of enzymatic activity. Ref.3
	Mutagenesis	162	1	D → N: Complete loss of enzymatic activity. Ref.3
	Mutagenesis	185	1	H → N: Complete loss of enzymatic activity. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q79F14-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 4358843F882C690A	FASTA	210	22,363
	10 20 30 40 50 60 MKKVLMAFII CLSLILSVLA APPSGAKAES VHNPVVLVHG ISGASYNFFA IKNYLISQGW 70 80 90 100 110 120 QSNKLYAIDF YDKTGNNLNN GPQLASYVDR VLKETGAKKV DIVAHSMGGA NTLYYIKYLG 130 140 150 160 170 180 GGNKIQNVVT LGGANGLVSS TALPGTDPNQ KILYTSIYSL NDQIVINSLS RLQGARNIQL 190 200 210 YGIGHIGLLS NSQVNGYIKE GLNGGGLNTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Bacillus subtilis chromosome region near 78 degrees contains the genes encoding a new two-component system, three ABC transporters and a lipase." Yamamoto H., Uchiyama S., Sekiguchi J. Gene 181:147-151(1996) [PubMed: 8973323] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / AC327.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"A novel extracellular esterase from Bacillus subtilis and its conversion to a monoacylglycerol hydrolase." Eggert T., Pencreac'h G., Douchet I., Verger R., Jaeger K.-E. Eur. J. Biochem. 267:6459-6469(2000) [PubMed: 11029590] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-38, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS OF ALA-104; SER-106; ASP-162 AND HIS-185. Strain: 168 / BCL 1050.
[4]	"Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in regulation of gene expression, biochemical properties, and three-dimensional structure." Eggert T., van Pouderoyen G., Dijkstra B.W., Jaeger K.-E. FEBS Lett. 502:89-92(2001) [PubMed: 11583117] [Abstract] Cited for: INDUCTION. Strain: 168 / BCL 1050.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D78508 Genomic DNA. Translation: BAA11406.1. AL009126 Genomic DNA. Translation: CAB12664.1.
RefSeq	NP_388716.1.
3D structure databases
SMR	Q79F14. Positions 32-210.
ModBase	Search...
Genome annotation databases
GeneID	939715.
GenomeReviews	Gene locus BSU08350 in contig AL009126_GR.
KEGG	bsu:BSU08350.
NMPDR	fig|224308.1.peg.835.
Organism-specific databases
SubtiList	BG11951. estB. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	Q79F14.
OMA	DESIRPR.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU0835-MON.
Family and domain databases
InterPro	IPR002918. Lipase_2. IPR008262. Lipase_Ser_AS. [Graphical view]
Pfam	PF01674. Lipase_2. 1 hit. [Graphical view]
PROSITE	PS00120. LIPASE_SER. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ESTB_BACSU

Accession

Primary (citable) accession number: Q79F14
Secondary accession number(s): Q796Z3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)