P37967 (PNBA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Para-nitrobenzyl esterase
EC=3.1.1.-

Alternative name(s):
Intracellular esterase B
PNB carboxy-esterase
Short name=PNBCE

Gene names

Name:	pnbA
Synonyms:	estB
Ordered Locus Names:	BSU34390

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	489 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes hydrolysis of several beta-lactam antibiotic PNB esters to the corresponding free acid and PNB alcohol.
Subunit structure	Monomer.
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Molecular function	Hydrolase Serine esterase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular_function	carboxylesterase activity Inferred from Biological aspect of Ancestor. Source: RefGenome cholinesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 489

489

Para-nitrobenzyl esterase

PRO_0000070296

Sites

Active site

189

1

Acyl-ester intermediate By similarity

Active site

310

1

Charge relay system By similarity

Active site

399

1

Charge relay system By similarity

Amino acid modifications

Modified residue

189

1

Phosphoserine Ref.7

Natural variations

Natural variant

59

1

S → P in strain: NRRL B8079.

Natural variant

95

1

K → Q in strain: NRRL B8079.

Natural variant

150

1

N → D in strain: NRRL B8079.

Natural variant

230

1

S → A in strain: NRRL B8079.

Natural variant

242

1

G → S in strain: NRRL B8079.

Natural variant

246

1

K → R in strain: NRRL B8079.

Natural variant

251

1

S → A in strain: NRRL B8079.

Natural variant

291

1

A → S in strain: NRRL B8079.

Natural variant

343

1

V → A in strain: NRRL B8079.

Natural variant

390

1

K → E in strain: NRRL B8079.

Natural variant

463

1

L → V in strain: NRRL B8079.

Experimental info

Sequence conflict

17

1

T → Q AA sequence Ref.1

Secondary structure

1

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489

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Beta strand

11 – 14

4

Beta strand

16 – 18

3

Beta strand

21 – 28

8

Helix

35 – 37

3

Beta strand

49 – 53

5

Turn

65 – 67

3

Helix

68 – 71

4

Beta strand

84 – 90

7

Beta strand

96 – 103

8

Turn

107 – 109

3

Helix

116 – 118

3

Helix

121 – 127

7

Beta strand

130 – 134

5

Helix

139 – 142

4

Turn

147 – 149

3

Helix

157 – 172

16

Helix

173 – 176

4

Beta strand

178 – 188

11

Helix

190 – 198

9

Helix

202 – 204

3

Beta strand

209 – 215

7

Helix

223 – 237

15

Helix

244 – 248

5

Helix

252 – 263

12

Beta strand

274 – 276

3

Turn

281 – 283

3

Helix

288 – 293

6

Turn

294 – 299

6

Beta strand

302 – 307

6

Helix

310 – 313

4

Helix

324 – 335

12

Helix

337 – 343

7

Helix

344 – 346

3

Helix

351 – 362

12

Helix

364 – 374

11

Turn

375 – 377

3

Beta strand

380 – 385

6

Turn

399 – 402

4

Helix

403 – 407

5

Helix

412 – 417

6

Helix

423 – 442

20

Turn

457 – 459

3

Beta strand

461 – 468

8

Beta strand

470 – 474

5

Helix

477 – 483

7

Sequences

	Sequence		Length	Mass (Da)
	P37967 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: 95D1EF12F613C400	FASTA	489	53,986
	10 20 30 40 50 60 MTHQIVTTQY GKVKGTTENG VHKWKGIPYA KPPVGQWRFK APEPPEVWED VLDATAYGSI 70 80 90 100 110 120 CPQPSDLLSL SYTELPRQSE DCLYVNVFAP DTPSKNLPVM VWIHGGAFYL GAGSEPLYDG 130 140 150 160 170 180 SKLAAQGEVI VVTLNYRLGP FGFLHLSSFN EAYSDNLGLL DQAAALKWVR ENISAFGGDP 190 200 210 220 230 240 DNVTVFGESA GGMSIAALLA MPAAKGLFQK AIMESGASRT MTKEQAASTS AAFLQVLGIN 250 260 270 280 290 300 EGQLDKLHTV SAEDLLKAAD QLRIAEKENI FQLFFQPALD PKTLPEEPEK AIAEGAASGI 310 320 330 340 350 360 PLLIGTTRDE GYLFFTPDSD VHSQETLDAA LEYLLGKPLA EKVADLYPRS LESQIHMMTD 370 380 390 400 410 420 LLFWRPAVAY ASAQSHYAPV WMYRFDWHPK KPPYNKAFHA LELPFVFGNL DGLERMAKAE 430 440 450 460 470 480 ITDEVKQLSH TIQSAWITFA KTGNPSTEAV NWPAYHEETR ETLILDSEIT IENDPESEKR QKLFPSKGE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase: cloning, sequence and high-level expression in Escherichia coli." Zock J., Cantwell C., Swartling J., Hodges R., Pohl T., Sutton K., Rosteck P. Jr., McGilvray D., Queener S. Gene 151:37-43(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22 AND 211-223. Strain: NRRL B8079.
[2]	"Identification of a SinR-homolog involved in initiation of competence development and sporulation in Bacillus subtilis." Dartois V.A., Ferrari E., Hoch J.A. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"Integrated mapping and sequencing of a 115 kb DNA fragment from Bacillus subtilis: sequence analysis of a 21 kb segment containing the sigL locus." Fabret C., Quentin Y., Chapal N., Guiseppi A., Haiech J., Denizot F. Microbiology 142:3089-3096(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[4]	Denizot F. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[5]	"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.
[6]	"Purification and properties of p-nitrobenzyl esterase from Bacillus subtilis." Chen Y.-R., Usui S., Yu C.-A. FASEB J. 6:A332-A332(1991) Cited for: PROTEIN SEQUENCE OF 1-22 AND 211-223, CHARACTERIZATION.
[7]	"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, MASS SPECTROMETRY. Strain: 168.
[8]	"A structural view of evolutionary divergence." Spiller B., Gershenson A., Arnold F.H., Stevens R.C. Proc. Natl. Acad. Sci. U.S.A. 96:12305-12310(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U06089 Genomic DNA. Translation: AAA81915.1.
U46134 Genomic DNA. Translation: AAB39889.1.
Z71928 Genomic DNA. Translation: CAA96487.1.
Z94043 Genomic DNA. Translation: CAB08021.1.
AL009126 Genomic DNA. Translation: CAB15444.1.

PIR

B69680.

RefSeq

NP_391319.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C7I	X-ray	2.00	A	1-489	[»]
1C7J	X-ray	1.60	A	1-489	[»]
1QE3	X-ray	1.50	A	1-489	[»]

ProteinModelPortal

P37967.

SMR

P37967. Positions 2-486.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU34390.

Protein family/group databases

MEROPS

S09.948.

PTM databases

PhosSite

P0802231.

Proteomic databases

PaxDb

P37967.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB15444; CAB15444; BSU34390.

GeneID

938580.

KEGG

bsu:BSU34390.

PATRIC

18978878. VBIBacSub10457_3602.

Organism-specific databases

GenoList

BSU34390. [Micado]

Phylogenomic databases

eggNOG

COG2272.

HOGENOM

HOG000091866.

KO

K03929.

OMA

MYRFDWH.

ProtClustDB

CLSK887919.

Enzyme and pathway databases

BioCyc

BSUB:BSU34390-MONOMER.

Family and domain databases

InterPro

IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]

Pfam

PF00135. COesterase. 1 hit.
[Graphical view]

PRINTS

PR00878. CHOLNESTRASE.

PROSITE

PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P37967.

Entry information

Entry name

PNBA_BACSU

Accession

Primary (citable) accession number: P37967
Secondary accession number(s): O08167 , O08472, P71048, Q795H9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 5, 2005
Last modified:	May 1, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program