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Protein

Extracellular esterase EstB

Gene

estB

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

Functioni

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 activityi

Triacylglycerol + H2O = diacylglycerol + a carboxylate.

pH dependencei

Optimum pH is 11-12.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius. Stable up to 45 degrees Celsuis.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei106Nucleophile1
Active sitei162Charge relay system1
Active sitei185Charge relay system1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU08350-MONOMER.
SABIO-RKiQ79F14.

Protein family/group databases

ESTHERibacsu-LIPB. Lipase_2.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular esterase EstB (EC:3.1.1.3)
Alternative name(s):
Lipase B
Triacylglycerol lipase
Gene namesi
Name:estB
Synonyms:lipB, yfiP
Ordered Locus Names:BSU08350
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi104A → G: Enzyme activity changes to monoacylglycerol hydrolase. Marked decrease in temperature stability, decreased stability at pH 11 but increased stability at pH 5. 1 Publication1
Mutagenesisi106S → C: Complete loss of enzymatic activity. 1 Publication1
Mutagenesisi162D → N: Complete loss of enzymatic activity. 1 Publication1
Mutagenesisi185H → N: Complete loss of enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000036168729 – 210Extracellular esterase EstBAdd BLAST182

Proteomic databases

PaxDbiQ79F14.
PRIDEiQ79F14.

Expressioni

Inductioni

Induced in rich but not minimal media.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100004633.

Structurei

3D structure databases

ProteinModelPortaliQ79F14.
SMRiQ79F14.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108KTS. Bacteria.
ENOG41104NC. LUCA.
HOGENOMiHOG000008725.
InParanoidiQ79F14.
KOiK01046.
OMAiQGARNIQ.
PhylomeDBiQ79F14.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiView protein in InterPro
IPR029058. AB_hydrolase.
IPR002918. Lipase_EstA/Esterase_EstB.
PANTHERiPTHR32015. PTHR32015. 2 hits.
PfamiView protein in Pfam
PF01674. Lipase_2. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q79F14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVLMAFII CLSLILSVLA APPSGAKAES VHNPVVLVHG ISGASYNFFA
60 70 80 90 100
IKNYLISQGW QSNKLYAIDF YDKTGNNLNN GPQLASYVDR VLKETGAKKV
110 120 130 140 150
DIVAHSMGGA NTLYYIKYLG GGNKIQNVVT LGGANGLVSS TALPGTDPNQ
160 170 180 190 200
KILYTSIYSL NDQIVINSLS RLQGARNIQL YGIGHIGLLS NSQVNGYIKE
210
GLNGGGLNTN
Length:210
Mass (Da):22,363
Last modified:July 5, 2004 - v1
Checksum:i4358843F882C690A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78508 Genomic DNA. Translation: BAA11406.1.
AL009126 Genomic DNA. Translation: CAB12664.1.
RefSeqiNP_388716.1. NC_000964.3.
WP_003243184.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12664; CAB12664; BSU08350.
GeneIDi939715.
KEGGibsu:BSU08350.
PATRICifig|224308.179.peg.903.

Similar proteinsi

Entry informationi

Entry nameiESTB_BACSU
AccessioniPrimary (citable) accession number: Q79F14
Secondary accession number(s): Q796Z3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 5, 2004
Last modified: November 22, 2017
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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