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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...

GO - Biological processi

    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...

    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

    Similar proteinsi