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P37967

- PNBA_BACSU

UniProt

P37967 - PNBA_BACSU

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Protein
Para-nitrobenzyl esterase
Gene
pnbA, estB, BSU34390
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes hydrolysis of several beta-lactam antibiotic PNB esters to the corresponding free acid and PNB alcohol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei189 – 1891Acyl-ester intermediate By similarity
Active sitei310 – 3101Charge relay system By similarity
Active sitei399 – 3991Charge relay system By similarity

GO - Molecular functioni

  1. cholinesterase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciBSUB:BSU34390-MONOMER.

Protein family/group databases

MEROPSiS09.948.

Names & Taxonomyi

Protein namesi
Recommended name:
Para-nitrobenzyl esterase (EC:3.1.1.-)
Alternative name(s):
Intracellular esterase B
PNB carboxy-esterase
Short name:
PNBCE
Gene namesi
Name:pnbA
Synonyms:estB
Ordered Locus Names:BSU34390
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU34390. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489Para-nitrobenzyl esterase
PRO_0000070296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP37967.

PTM databases

PhosSiteiP0802231.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi224308.BSU34390.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84
Beta strandi11 – 144
Beta strandi16 – 183
Beta strandi21 – 288
Helixi35 – 373
Beta strandi49 – 535
Turni65 – 673
Helixi68 – 714
Beta strandi84 – 907
Beta strandi96 – 1038
Turni107 – 1093
Helixi116 – 1183
Helixi121 – 1277
Beta strandi130 – 1345
Helixi139 – 1424
Turni147 – 1493
Helixi157 – 17216
Helixi173 – 1764
Beta strandi178 – 18811
Helixi190 – 1989
Helixi202 – 2043
Beta strandi209 – 2157
Helixi223 – 23715
Helixi244 – 2485
Helixi252 – 26312
Beta strandi274 – 2763
Turni281 – 2833
Helixi288 – 2936
Turni294 – 2996
Beta strandi302 – 3076
Helixi310 – 3134
Helixi324 – 33512
Helixi337 – 3437
Helixi344 – 3463
Helixi351 – 36212
Helixi364 – 37411
Turni375 – 3773
Beta strandi380 – 3856
Turni399 – 4024
Helixi403 – 4075
Helixi412 – 4176
Helixi423 – 44220
Turni457 – 4593
Beta strandi461 – 4688
Beta strandi470 – 4745
Helixi477 – 4837

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7IX-ray2.00A1-489[»]
1C7JX-ray1.60A1-489[»]
1QE3X-ray1.50A1-489[»]
ProteinModelPortaliP37967.
SMRiP37967. Positions 2-486.

Miscellaneous databases

EvolutionaryTraceiP37967.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2272.
HOGENOMiHOG000091866.
KOiK03929.
OMAiESAGACI.
OrthoDBiEOG6X10Z4.
PhylomeDBiP37967.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37967-1 [UniParc]FASTAAdd to Basket

« Hide

MTHQIVTTQY GKVKGTTENG VHKWKGIPYA KPPVGQWRFK APEPPEVWED    50
VLDATAYGSI CPQPSDLLSL SYTELPRQSE DCLYVNVFAP DTPSKNLPVM 100
VWIHGGAFYL GAGSEPLYDG SKLAAQGEVI VVTLNYRLGP FGFLHLSSFN 150
EAYSDNLGLL DQAAALKWVR ENISAFGGDP DNVTVFGESA GGMSIAALLA 200
MPAAKGLFQK AIMESGASRT MTKEQAASTS AAFLQVLGIN EGQLDKLHTV 250
SAEDLLKAAD QLRIAEKENI FQLFFQPALD PKTLPEEPEK AIAEGAASGI 300
PLLIGTTRDE GYLFFTPDSD VHSQETLDAA LEYLLGKPLA EKVADLYPRS 350
LESQIHMMTD LLFWRPAVAY ASAQSHYAPV WMYRFDWHPK KPPYNKAFHA 400
LELPFVFGNL DGLERMAKAE ITDEVKQLSH TIQSAWITFA KTGNPSTEAV 450
NWPAYHEETR ETLILDSEIT IENDPESEKR QKLFPSKGE 489
Length:489
Mass (Da):53,986
Last modified:July 5, 2005 - v2
Checksum:i95D1EF12F613C400
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591S → P in strain: NRRL B8079.
Natural varianti95 – 951K → Q in strain: NRRL B8079.
Natural varianti150 – 1501N → D in strain: NRRL B8079.
Natural varianti230 – 2301S → A in strain: NRRL B8079.
Natural varianti242 – 2421G → S in strain: NRRL B8079.
Natural varianti246 – 2461K → R in strain: NRRL B8079.
Natural varianti251 – 2511S → A in strain: NRRL B8079.
Natural varianti291 – 2911A → S in strain: NRRL B8079.
Natural varianti343 – 3431V → A in strain: NRRL B8079.
Natural varianti390 – 3901K → E in strain: NRRL B8079.
Natural varianti463 – 4631L → V in strain: NRRL B8079.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171T → Q AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiB69680.
RefSeqiNP_391319.1. NC_000964.3.
WP_003243926.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB15444; CAB15444; BSU34390.
GeneIDi938580.
KEGGibsu:BSU34390.
PATRICi18978878. VBIBacSub10457_3602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi B69680.
RefSeqi NP_391319.1. NC_000964.3.
WP_003243926.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P37967.
SMRi P37967. Positions 2-486.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU34390.

Protein family/group databases

MEROPSi S09.948.

PTM databases

PhosSitei P0802231.

Proteomic databases

PaxDbi P37967.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15444 ; CAB15444 ; BSU34390 .
GeneIDi 938580.
KEGGi bsu:BSU34390.
PATRICi 18978878. VBIBacSub10457_3602.

Organism-specific databases

GenoListi BSU34390. [Micado ]

Phylogenomic databases

eggNOGi COG2272.
HOGENOMi HOG000091866.
KOi K03929.
OMAi ESAGACI.
OrthoDBi EOG6X10Z4.
PhylomeDBi P37967.

Enzyme and pathway databases

BioCyci BSUB:BSU34390-MONOMER.

Miscellaneous databases

EvolutionaryTracei P37967.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR00878. CHOLNESTRASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Entry informationi

Entry nameiPNBA_BACSU
AccessioniPrimary (citable) accession number: P37967
Secondary accession number(s): O08167
, O08472, P71048, Q795H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 5, 2005
Last modified: September 3, 2014
This is version 102 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, Direct protein sequencing, 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

External Data

Dasty 3

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