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Protein

Lipase EstA

Gene

estA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Active toward p-nitrophenyl esters and triacylglycerides with a marked preference for esters with C8 acyl groups.1 Publication

Catalytic activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

Enzyme regulationi

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.1 Publication

pH dependencei

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 13.1 Publication

Temperature dependencei

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei108Nucleophile1
Active sitei164Charge relay system1
Active sitei187Charge relay system1

GO - Molecular functioni

  • triglyceride lipase activity Source: CACAO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU02700-MONOMER.
SABIO-RKP37957.

Protein family/group databases

ESTHERibacsu-lip. Lipase_2.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipase EstA
Alternative name(s):
Lipase A (EC:3.1.1.3)
Triacylglycerol lipase
Gene namesi
Name:estA
Synonyms:lip, lipA
Ordered Locus Names:BSU02700
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000001781932 – 212Lipase EstAAdd BLAST181

Proteomic databases

PaxDbiP37957.

Expressioni

Inductioni

Maximally expressed in late exponential growth phase. Expression decreases rapidly in the stationary phase. Expressed in both rich and minimal media.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001498.

Structurei

Secondary structure

1212
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 40Combined sources4
Helixi47 – 50Combined sources4
Helixi51 – 59Combined sources9
Helixi64 – 66Combined sources3
Beta strandi67 – 69Combined sources3
Helixi79 – 97Combined sources19
Beta strandi102 – 107Combined sources6
Helixi110 – 120Combined sources11
Helixi123 – 125Combined sources3
Beta strandi127 – 134Combined sources8
Helixi137 – 139Combined sources3
Beta strandi155 – 161Combined sources7
Beta strandi165 – 167Combined sources3
Helixi169 – 172Combined sources4
Beta strandi177 – 184Combined sources8
Helixi189 – 191Combined sources3
Helixi194 – 204Combined sources11
Turni205 – 207Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I6WX-ray1.50A/B32-212[»]
1ISPX-ray1.30A32-212[»]
1R4ZX-ray1.80A/B32-212[»]
1R50X-ray1.45A/B32-212[»]
1T2NX-ray1.80A32-212[»]
1T4MX-ray2.00A32-212[»]
2QXTX-ray2.00A/B34-212[»]
2QXUX-ray1.90A/B/C/D/E/F/G/H34-212[»]
3D2AX-ray1.73A32-212[»]
3D2BX-ray1.95A/B32-212[»]
3D2CX-ray2.18A/B/C/D/E/F/G/H/I/J/K/L32-212[»]
3QMMX-ray1.89A/B32-212[»]
3QZUX-ray1.85A/B32-212[»]
5CRIX-ray1.63A/B32-212[»]
5CT4X-ray1.49A/B33-212[»]
5CT5X-ray1.75A/B33-212[»]
5CT6X-ray1.90A/B33-212[»]
5CT8X-ray1.29A33-212[»]
5CT9X-ray1.40A33-212[»]
5CTAX-ray1.24A33-212[»]
5CURX-ray1.30A33-212[»]
ProteinModelPortaliP37957.
SMRiP37957.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37957.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108KTS. Bacteria.
ENOG41104NC. LUCA.
HOGENOMiHOG000008725.
InParanoidiP37957.
KOiK01046.
OMAiFAGIKSY.
PhylomeDBiP37957.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002918. Lipase_EstA/Esterase_EstB.
[Graphical view]
PfamiPF01674. Lipase_2. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37957-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFVKRRIIA LVTILMLSVT SLFALQPSAK AAEHNPVVMV HGIGGASFNF
60 70 80 90 100
AGIKSYLVSQ GWSRDKLYAV DFWDKTGTNY NNGPVLSRFV QKVLDETGAK
110 120 130 140 150
KVDIVAHSMG GANTLYYIKN LDGGNKVANV VTLGGANRLT TGKALPGTDP
160 170 180 190 200
NQKILYTSIY SSADMIVMNY LSRLDGARNV QIHGVGHIGL LYSSQVNSLI
210
KEGLNGGGQN TN
Length:212
Mass (Da):22,791
Last modified:May 30, 2000 - v2
Checksum:iB8A70E027461188F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29A → V in ABB54395 (Ref. 3) Curated1
Sequence conflicti51A → G in ABB54395 (Ref. 3) Curated1
Sequence conflicti60Q → H in ABB54395 (Ref. 3) Curated1
Sequence conflicti133L → V (PubMed:1320940).Curated1
Sequence conflicti133L → V (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74010 Genomic DNA. Translation: AAA22574.1.
AB000617 Genomic DNA. Translation: BAA22231.1.
DQ250714 Genomic DNA. Translation: ABB54395.1.
AL009126 Genomic DNA. Translation: CAB12064.1.
PIRiS23934.
RefSeqiNP_388152.1. NC_000964.3.
WP_003246250.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB12064; CAB12064; BSU02700.
GeneIDi938389.
KEGGibsu:BSU02700.
PATRICi18972099. VBIBacSub10457_0278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74010 Genomic DNA. Translation: AAA22574.1.
AB000617 Genomic DNA. Translation: BAA22231.1.
DQ250714 Genomic DNA. Translation: ABB54395.1.
AL009126 Genomic DNA. Translation: CAB12064.1.
PIRiS23934.
RefSeqiNP_388152.1. NC_000964.3.
WP_003246250.1. NZ_JNCM01000030.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I6WX-ray1.50A/B32-212[»]
1ISPX-ray1.30A32-212[»]
1R4ZX-ray1.80A/B32-212[»]
1R50X-ray1.45A/B32-212[»]
1T2NX-ray1.80A32-212[»]
1T4MX-ray2.00A32-212[»]
2QXTX-ray2.00A/B34-212[»]
2QXUX-ray1.90A/B/C/D/E/F/G/H34-212[»]
3D2AX-ray1.73A32-212[»]
3D2BX-ray1.95A/B32-212[»]
3D2CX-ray2.18A/B/C/D/E/F/G/H/I/J/K/L32-212[»]
3QMMX-ray1.89A/B32-212[»]
3QZUX-ray1.85A/B32-212[»]
5CRIX-ray1.63A/B32-212[»]
5CT4X-ray1.49A/B33-212[»]
5CT5X-ray1.75A/B33-212[»]
5CT6X-ray1.90A/B33-212[»]
5CT8X-ray1.29A33-212[»]
5CT9X-ray1.40A33-212[»]
5CTAX-ray1.24A33-212[»]
5CURX-ray1.30A33-212[»]
ProteinModelPortaliP37957.
SMRiP37957.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001498.

Protein family/group databases

ESTHERibacsu-lip. Lipase_2.

Proteomic databases

PaxDbiP37957.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12064; CAB12064; BSU02700.
GeneIDi938389.
KEGGibsu:BSU02700.
PATRICi18972099. VBIBacSub10457_0278.

Phylogenomic databases

eggNOGiENOG4108KTS. Bacteria.
ENOG41104NC. LUCA.
HOGENOMiHOG000008725.
InParanoidiP37957.
KOiK01046.
OMAiFAGIKSY.
PhylomeDBiP37957.

Enzyme and pathway databases

BioCyciBSUB:BSU02700-MONOMER.
SABIO-RKP37957.

Miscellaneous databases

EvolutionaryTraceiP37957.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002918. Lipase_EstA/Esterase_EstB.
[Graphical view]
PfamiPF01674. Lipase_2. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiESTA_BACSU
AccessioniPrimary (citable) accession number: P37957
Secondary accession number(s): O34644, Q2XU59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.