pnbA
168

para-nitrobenzyl esterase

Locus

BSU_34390

Molecular weight

53.82 kDa

Isoelectric point

4.78

Protein length

489 aaSequenceBlast

Gene length

1470 bpSequenceBlast

Function

lipid degradation

Product

para-nitrobenzyl esterase

Essential

E.C.

3.1.1.3

Synonyms

pnbA, estB

Outlinks

BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

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Categories containing this gene/protein

List of homologs in different organisms, belongs to COG2272 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene

Coordinates

3,530,635 3,532,104

The protein

Protein family

type-B carboxylesterase/lipase family (single member, according to UniProt)

Structure

1C7J (PDB)\tPubMed

P37967 (AlphaFold)

Modification

phosphorylation on Ser-189 PubMed

Expression and Regulation

Operons

Genes

pnbA

Description

PubMed

Regulation

repressed during logarithmic growth (AbrB) PubMed

Regulatory mechanism

AbrB: repression, PubMed, in abrB regulon

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Genes

slrR-pnbA

Description

PubMed

Regulatory mechanism

Abh: activation, PubMed, in abh regulon

SinR: repression, PubMed, in sinR regulon

AbrB: repression, PubMed, in abrB regulon

Additional information

induction by sequestration of SinR by SinI, SlrA PubMed or by SlrR itself PubMed

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Biological materials

Mutant

GP951 (pnbA::cat), available in Jörg Stülke's lab

GP955 (''slrR-pnbA::cat''), available in Jörg Stülke's lab

BKE34390 (pnbA::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATTGTGTTCTCTCCCTTTT, downstream forward: _UP4_TAAATATGGGGAAAACAGGA

BKK34390 (pnbA::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATTGTGTTCTCTCCCTTTT, downstream forward: _UP4_TAAATATGGGGAAAACAGGA

References

Zhou J, Sang Y, Wang Z, Feng J, Zhu L, Chen XEnhancing the Enantioselectivity and Catalytic Efficiency of Esterase from Bacillus subtilis for Kinetic Resolution of l-Menthol through Semirational Design.Journal of agricultural and food chemistry. 2024 Jan 18; . PMID: 38235660

Qiao J, Yang D, Feng Y, Wei W, Liu X, Zhang Y, Zheng J, Ying XEngineering a Bacillus subtilis esterase for selective hydrolysis of d, l-menthyl acetate in an organic solvent-free system.RSC advances. 2023 Apr 3; 13(16):10468-10475. PMID: 37021103

Legler PM, Boisvert SM, Compton JR, Millard CB Development of organophosphate hydrolase activity in a bacterial homolog of human cholinesterase. Frontiers in chemistry. 2014; 2:46. doi:10.3389/fchem.2014.00046. PMID:25077141

Yu X, Sigler SC, Hossain D, Wierdl M, Gwaltney SR, Potter PM, Wadkins RM Global and local molecular dynamics of a bacterial carboxylesterase provide insight into its catalytic mechanism. Journal of molecular modeling. 2012 Jun; 18(6):2869-83. doi:10.1007/s00894-011-1308-9. PMID:22127613

Ribitsch D, Heumann S, Trotscha E, Herrero Acero E, Greimel K, Leber R, Birner-Gruenberger R, Deller S, Eiteljoerg I, Remler P, Weber T, Siegert P, Maurer KH, Donelli I, Freddi G, Schwab H, Guebitz GM Hydrolysis of polyethyleneterephthalate by p-nitrobenzylesterase from Bacillus subtilis. Biotechnology progress. 2011 Jul; 27(4):951-60. doi:10.1002/btpr.610. PMID:21574267

Macek B, Mijakovic I, Olsen JV, Gnad F, Kumar C, Jensen PR, Mann M The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Molecular & cellular proteomics : MCP. 2007 Apr; 6(4):697-707. . PMID:17218307

Spiller B, Gershenson A, Arnold FH, Stevens RC A structural view of evolutionary divergence. Proceedings of the National Academy of Sciences of the United States of America. 1999 Oct 26; 96(22):12305-10. . PMID:10535917

Zock J, Cantwell C, Swartling J, Hodges R, Pohl T, Sutton K, Rosteck P, McGilvray D, Queener S The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase: cloning, sequence and high-level expression in Escherichia coli. Gene. 1994 Dec 30; 151(1-2):37-43. . PMID:7828905

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Time of last update: 2025-04-04 08:50:27

Author of last update: Jstuelk

pnbA 168

pnbA
168