P37957 (ESTA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipase EstA

Alternative name(s):
Lipase A
EC=3.1.1.3
Triacylglycerol lipase

Gene names

Name:	estA
Synonyms:	lip, lipA
Ordered Locus Names:	BSU02700

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	212 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	Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups. Ref.5
Catalytic activity	Triacylglycerol + H2O = diacylglycerol + a carboxylate.
Enzyme regulation	Strongly inhibited when incubated with the serine reagent phenylmethylsulfonyl fluoride. Activated by the addition of calcium to the reaction mixture. When calcium was incubated with the lipase but not added to the reaction mixture, its effect is lower but still observable. Magnesium, manganese and strontium are not able to replace calcium with full retention of activity. Ref.5
Subcellular location	Secreted.
Induction	Maximally expressed in late exponential growth phase. Expression decreases rapidly in the stationary phase. Expressed in both rich and minimal media. Ref.5 Ref.6
Sequence similarities	Belongs to the AB hydrolase superfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 10. The activity decreases strongly above pH 10.5 or below pH 6.5. The enzyme is remarkably stable at alkaline pH, showing maximum stability at pH 12 and retaining more than 65% of its activity after 24 hours at pH 13. Ref.5 Temperature dependence: Optimum temperature is 35 degrees Celsius. Stable for at least 30 minutes at 40 degrees Celsius. Virtually no activity remains after 30 minutes at 55 degrees Celsius.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
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	retinyl-palmitate esterase activity Inferred from electronic annotation. Source: EC 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 – 31

31

Chain

32 – 212

181

Lipase EstA

PRO_0000017819

Sites

Active site

108

1

Nucleophile

Active site

164

1

Charge relay system

Active site

187

1

Charge relay system

Experimental info

Sequence conflict

29

1

A → V in ABB54395. Ref.3

Sequence conflict

51

1

A → G in ABB54395. Ref.3

Sequence conflict

60

1

Q → H in ABB54395. Ref.3

Sequence conflict

133

1

L → V Ref.1

Sequence conflict

133

1

L → V Ref.3

Secondary structure

1

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212

Helix Strand Turn

Details...

Beta strand

37 – 40

4

Helix

47 – 50

4

Helix

51 – 59

9

Helix

64 – 66

3

Beta strand

67 – 69

3

Helix

79 – 97

19

Beta strand

102 – 107

6

Helix

110 – 120

11

Helix

123 – 125

3

Beta strand

127 – 134

8

Helix

137 – 139

3

Beta strand

155 – 161

7

Beta strand

165 – 167

3

Helix

169 – 172

4

Beta strand

177 – 184

8

Helix

188 – 192

5

Helix

194 – 204

11

Turn

205 – 207

3

Sequences

	Sequence		Length	Mass (Da)
	P37957 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: B8A70E027461188F	FASTA	212	22,791
	10 20 30 40 50 60 MKFVKRRIIA LVTILMLSVT SLFALQPSAK AAEHNPVVMV HGIGGASFNF AGIKSYLVSQ 70 80 90 100 110 120 GWSRDKLYAV DFWDKTGTNY NNGPVLSRFV QKVLDETGAK KVDIVAHSMG GANTLYYIKN 130 140 150 160 170 180 LDGGNKVANV VTLGGANRLT TGKALPGTDP NQKILYTSIY SSADMIVMNY LSRLDGARNV 190 200 210 QIHGVGHIGL LYSSQVNSLI KEGLNGGGQN TN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168." Dartois V., Baulard A., Schanck K., Colson C. Biochim. Biophys. Acta 1131:253-260(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"A 32 kb nucleotide sequence from the region of the lincomycin-resistance gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and identification of the site of the lin-2 mutation." Kumano M., Tamakoshi A., Yamane K. Microbiology 143:2775-2782(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"Molecular characterization of a lipase from a strain of Bacillus subtilis." Peerzada K., Johri S., Rasool S., Andrabi K. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[5]	"Purification and preliminary characterization of the extracellular lipase of Bacillus subtilis 168, an extremely basic pH-tolerant enzyme." Lesuisse E., Schanck K., Colson C. Eur. J. Biochem. 216:155-160(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, N-TERMINAL END. Strain: 168.
[6]	"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] [Europe PMC] [Abstract] Cited for: INDUCTION. Strain: 168 / BCL 1050.
[7]	"The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme." van Pouderoyen G., Eggert T., Jaeger K.-E., Dijkstra B.W. J. Mol. Biol. 309:215-226(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 32-212.
[8]	"Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution." Kawasaki K., Kondo H., Suzuki M., Ohgiya S., Tsuda S. Acta Crystallogr. D 58:1168-1174(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 32-212.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M74010 Genomic DNA. Translation: AAA22574.1.
AB000617 Genomic DNA. Translation: BAA22231.1.
DQ250714 Genomic DNA. Translation: ABB54395.1.
AL009126 Genomic DNA. Translation: CAB12064.1.

PIR

S23934.

RefSeq

NP_388152.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I6W	X-ray	1.50	A/B	32-212	[»]
1ISP	X-ray	1.30	A	32-212	[»]
1R4Z	X-ray	1.80	A/B	32-212	[»]
1R50	X-ray	1.45	A/B	32-212	[»]
1T2N	X-ray	1.80	A	32-212	[»]
1T4M	X-ray	2.00	A	32-212	[»]
2QXT	X-ray	2.00	A/B	34-212	[»]
2QXU	X-ray	1.90	A/B/C/D/E/F/G/H	34-212	[»]
3D2A	X-ray	1.73	A	32-212	[»]
3D2B	X-ray	1.95	A/B	32-212	[»]
3D2C	X-ray	2.18	A/B/C/D/E/F/G/H/I/J/K/L	32-212	[»]
3QMM	X-ray	1.89	A/B	32-212	[»]
3QZU	X-ray	1.85	A/B	32-212	[»]

ProteinModelPortal

P37957.

SMR

P37957. Positions 33-211.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU02700.

Proteomic databases

PaxDb

P37957.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB12064; CAB12064; BSU02700.

GeneID

938389.

KEGG

bsu:BSU02700.

PATRIC

18972099. VBIBacSub10457_0278.

Organism-specific databases

GenoList

BSU02700. [Micado]

Phylogenomic databases

eggNOG

COG1075.

HOGENOM

HOG000008725.

KO

K01046.

OMA

QIHGVGH.

ProtClustDB

CLSK886633.

Enzyme and pathway databases

BioCyc

BSUB:BSU02700-MONOMER.

Family and domain databases

InterPro

IPR002918. Lipase_EstA/Esterase_EstB.
[Graphical view]

Pfam

PF01674. Lipase_2. 1 hit.
[Graphical view]

PROSITE

PS00120. LIPASE_SER. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P37957.

Entry information

Entry name

ESTA_BACSU

Accession

Primary (citable) accession number: P37957
Secondary accession number(s): O34644, Q2XU59

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	May 30, 2000
Last modified:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program