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P00782

- SUBT_BACAM

UniProt

P00782 - SUBT_BACAM

Protein

Subtilisin BPN'

Gene

apr

Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.1 Publication

    Catalytic activityi

    Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.

    Cofactori

    Binds 2 calcium ions per subunit.

    Enzyme regulationi

    Completely inhibited by phenylmethylsulfony fluoride (PMSF) and partially inhibited by benzamidine hydrochloride, leupeptin, and pepstatin A.1 Publication

    pH dependencei

    Optimum pH is 9.0.1 Publication

    Temperature dependencei

    Optimum temperature is 48 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi109 – 1091Calcium 1
    Active sitei139 – 1391Charge relay system1 Publication
    Metal bindingi148 – 1481Calcium 1
    Active sitei171 – 1711Charge relay system1 Publication
    Metal bindingi182 – 1821Calcium 1; via carbonyl oxygen
    Metal bindingi184 – 1841Calcium 1
    Metal bindingi186 – 1861Calcium 1; via carbonyl oxygen
    Metal bindingi188 – 1881Calcium 1; via carbonyl oxygen
    Metal bindingi276 – 2761Calcium 2; via carbonyl oxygen
    Metal bindingi278 – 2781Calcium 2; via carbonyl oxygen
    Metal bindingi281 – 2811Calcium 2; via carbonyl oxygen
    Active sitei328 – 3281Charge relay system1 Publication

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. fibrinolysis Source: UniProtKB
    2. proteolysis Source: UniProtKB
    3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Sporulation

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP00782.

    Protein family/group databases

    MEROPSiI09.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Subtilisin BPN' (EC:3.4.21.62)
    Alternative name(s):
    Alkaline protease
    Subtilisin DFE
    Subtilisin Novo
    Gene namesi
    Name:apr
    OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
    Taxonomic identifieri1390 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Biotechnological usei

    Used as a detergent protease. Sold under the name Alcalase by Novozymes.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030By similarityAdd
    BLAST
    Propeptidei31 – 107772 PublicationsPRO_0000027177Add
    BLAST
    Chaini108 – 382275Subtilisin BPN'PRO_0000027178Add
    BLAST

    Keywords - PTMi

    Zymogen

    Miscellaneous databases

    PMAP-CutDBP00782.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ica-2Q400598EBI-1033955,EBI-1040468From a different organism.

    Protein-protein interaction databases

    IntActiP00782. 2 interactions.
    MINTiMINT-242921.

    Structurei

    Secondary structure

    1
    382
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 446
    Turni46 – 494
    Helixi53 – 619
    Turni62 – 643
    Beta strandi66 – 705
    Beta strandi72 – 809
    Helixi83 – 908
    Beta strandi95 – 1006
    Beta strandi105 – 1084
    Helixi113 – 1175
    Helixi120 – 1267
    Beta strandi134 – 1407
    Beta strandi146 – 1483
    Beta strandi151 – 1566
    Beta strandi158 – 1603
    Beta strandi168 – 1703
    Helixi171 – 18010
    Beta strandi183 – 1886
    Beta strandi195 – 2017
    Beta strandi207 – 2093
    Helixi211 – 22313
    Beta strandi227 – 2315
    Beta strandi233 – 2364
    Helixi240 – 25112
    Beta strandi255 – 2595
    Turni275 – 2773
    Beta strandi281 – 2877
    Beta strandi289 – 2913
    Beta strandi305 – 3084
    Beta strandi310 – 3167
    Turni317 – 3193
    Beta strandi320 – 3245
    Helixi327 – 34418
    Helixi350 – 3589
    Beta strandi360 – 3623
    Helixi367 – 3704
    Helixi377 – 3804

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A2QX-ray1.80A108-382[»]
    1AK9X-ray1.80A108-382[»]
    1AQNX-ray1.80A108-382[»]
    1AU9X-ray1.80A108-382[»]
    1DUIX-ray2.00A108-382[»]
    1GNSX-ray1.80A112-382[»]
    1GNVX-ray1.90A108-382[»]
    1LW6X-ray1.50E108-382[»]
    1S01X-ray1.70A108-382[»]
    1S02X-ray1.90A108-382[»]
    1SBHX-ray1.80A108-382[»]
    1SBIX-ray2.20A108-382[»]
    1SBNX-ray2.10E108-382[»]
    1SBTX-ray2.50A108-382[»]
    1SIBX-ray2.40E108-382[»]
    1SPBX-ray2.00P37-107[»]
    S108-382[»]
    1ST2X-ray2.00A108-382[»]
    1SUAX-ray2.10A108-382[»]
    1SUBX-ray1.75A108-382[»]
    1SUCX-ray1.80A108-382[»]
    1SUDX-ray1.90A108-382[»]
    1SUEX-ray1.80A108-382[»]
    1SUPX-ray1.60A108-382[»]
    1TM1X-ray1.70E108-382[»]
    1TM3X-ray1.57E108-382[»]
    1TM4X-ray1.70E108-382[»]
    1TM5X-ray1.45E108-382[»]
    1TM7X-ray1.59E108-382[»]
    1TMGX-ray1.67E108-382[»]
    1TO1X-ray1.68E108-382[»]
    1TO2X-ray1.30E108-382[»]
    1UBNX-ray2.40A108-382[»]
    1V5IX-ray1.50A108-382[»]
    1Y1KX-ray1.56E108-382[»]
    1Y33X-ray1.80E108-382[»]
    1Y34X-ray1.55E108-382[»]
    1Y3BX-ray1.80E108-382[»]
    1Y3CX-ray1.69E108-382[»]
    1Y3DX-ray1.80E108-382[»]
    1Y3FX-ray1.72E108-382[»]
    1Y48X-ray1.84E108-382[»]
    1Y4AX-ray1.60E108-382[»]
    1Y4DX-ray2.00E108-382[»]
    1YJAX-ray1.80A108-382[»]
    1YJBX-ray1.80A108-382[»]
    1YJCX-ray1.80A108-382[»]
    2SBTX-ray2.80A108-382[»]
    2SICX-ray1.80E108-382[»]
    2SNIX-ray2.10E108-382[»]
    2ST1X-ray1.80A108-382[»]
    3BGOX-ray1.80S108-382[»]
    3CNQX-ray1.71P32-111[»]
    S108-382[»]
    3CO0X-ray1.93P32-111[»]
    S108-382[»]
    3F49X-ray1.70S108-382[»]
    3SICX-ray1.80E108-382[»]
    5SICX-ray2.20E108-382[»]
    ProteinModelPortaliP00782.
    SMRiP00782. Positions 37-382.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00782.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini134 – 380247Peptidase S8Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S8 family.Curated
    Contains 1 peptidase S8 domain.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.200. 1 hit.
    InterProiIPR010259. Inhibitor_I9.
    IPR000209. Peptidase_S8/S53_dom.
    IPR023827. Peptidase_S8_Asp-AS.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR009020. Prot_inh_propept.
    [Graphical view]
    PANTHERiPTHR10795. PTHR10795. 1 hit.
    PfamiPF05922. Inhibitor_I9. 1 hit.
    PF00082. Peptidase_S8. 1 hit.
    [Graphical view]
    PRINTSiPR00723. SUBTILISIN.
    SUPFAMiSSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
    PS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00782-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST    50
    MSAAKKKDVI SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE 100
    DHVAHAYAQS VPYGVSQIKA PALHSQGYTG SNVKVAVIDS GIDSSHPDLK 150
    VAGGASMVPS ETNPFQDNNS HGTHVAGTVA ALNNSIGVLG VAPSASLYAV 200
    KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA ALKAAVDKAV 250
    ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG 300
    PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN 350
    TQVRSSLENT TTKLGDSFYY GKGLINVQAA AQ 382
    Length:382
    Mass (Da):39,181
    Last modified:July 21, 1986 - v1
    Checksum:iED987DAFA37B8335
    GO

    Sequence cautioni

    The sequence CAA24990.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281Y → F in strain: DC-4. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02496 Genomic DNA. Translation: AAB05345.1.
    X00165 Genomic DNA. Translation: CAA24990.1. Different initiation.
    PIRiB25415. SUBSN.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02496 Genomic DNA. Translation: AAB05345.1 .
    X00165 Genomic DNA. Translation: CAA24990.1 . Different initiation.
    PIRi B25415. SUBSN.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A2Q X-ray 1.80 A 108-382 [» ]
    1AK9 X-ray 1.80 A 108-382 [» ]
    1AQN X-ray 1.80 A 108-382 [» ]
    1AU9 X-ray 1.80 A 108-382 [» ]
    1DUI X-ray 2.00 A 108-382 [» ]
    1GNS X-ray 1.80 A 112-382 [» ]
    1GNV X-ray 1.90 A 108-382 [» ]
    1LW6 X-ray 1.50 E 108-382 [» ]
    1S01 X-ray 1.70 A 108-382 [» ]
    1S02 X-ray 1.90 A 108-382 [» ]
    1SBH X-ray 1.80 A 108-382 [» ]
    1SBI X-ray 2.20 A 108-382 [» ]
    1SBN X-ray 2.10 E 108-382 [» ]
    1SBT X-ray 2.50 A 108-382 [» ]
    1SIB X-ray 2.40 E 108-382 [» ]
    1SPB X-ray 2.00 P 37-107 [» ]
    S 108-382 [» ]
    1ST2 X-ray 2.00 A 108-382 [» ]
    1SUA X-ray 2.10 A 108-382 [» ]
    1SUB X-ray 1.75 A 108-382 [» ]
    1SUC X-ray 1.80 A 108-382 [» ]
    1SUD X-ray 1.90 A 108-382 [» ]
    1SUE X-ray 1.80 A 108-382 [» ]
    1SUP X-ray 1.60 A 108-382 [» ]
    1TM1 X-ray 1.70 E 108-382 [» ]
    1TM3 X-ray 1.57 E 108-382 [» ]
    1TM4 X-ray 1.70 E 108-382 [» ]
    1TM5 X-ray 1.45 E 108-382 [» ]
    1TM7 X-ray 1.59 E 108-382 [» ]
    1TMG X-ray 1.67 E 108-382 [» ]
    1TO1 X-ray 1.68 E 108-382 [» ]
    1TO2 X-ray 1.30 E 108-382 [» ]
    1UBN X-ray 2.40 A 108-382 [» ]
    1V5I X-ray 1.50 A 108-382 [» ]
    1Y1K X-ray 1.56 E 108-382 [» ]
    1Y33 X-ray 1.80 E 108-382 [» ]
    1Y34 X-ray 1.55 E 108-382 [» ]
    1Y3B X-ray 1.80 E 108-382 [» ]
    1Y3C X-ray 1.69 E 108-382 [» ]
    1Y3D X-ray 1.80 E 108-382 [» ]
    1Y3F X-ray 1.72 E 108-382 [» ]
    1Y48 X-ray 1.84 E 108-382 [» ]
    1Y4A X-ray 1.60 E 108-382 [» ]
    1Y4D X-ray 2.00 E 108-382 [» ]
    1YJA X-ray 1.80 A 108-382 [» ]
    1YJB X-ray 1.80 A 108-382 [» ]
    1YJC X-ray 1.80 A 108-382 [» ]
    2SBT X-ray 2.80 A 108-382 [» ]
    2SIC X-ray 1.80 E 108-382 [» ]
    2SNI X-ray 2.10 E 108-382 [» ]
    2ST1 X-ray 1.80 A 108-382 [» ]
    3BGO X-ray 1.80 S 108-382 [» ]
    3CNQ X-ray 1.71 P 32-111 [» ]
    S 108-382 [» ]
    3CO0 X-ray 1.93 P 32-111 [» ]
    S 108-382 [» ]
    3F49 X-ray 1.70 S 108-382 [» ]
    3SIC X-ray 1.80 E 108-382 [» ]
    5SIC X-ray 2.20 E 108-382 [» ]
    ProteinModelPortali P00782.
    SMRi P00782. Positions 37-382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00782. 2 interactions.
    MINTi MINT-242921.

    Protein family/group databases

    MEROPSi I09.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P00782.

    Miscellaneous databases

    EvolutionaryTracei P00782.
    PMAP-CutDB P00782.

    Family and domain databases

    Gene3Di 3.40.50.200. 1 hit.
    InterProi IPR010259. Inhibitor_I9.
    IPR000209. Peptidase_S8/S53_dom.
    IPR023827. Peptidase_S8_Asp-AS.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR009020. Prot_inh_propept.
    [Graphical view ]
    PANTHERi PTHR10795. PTHR10795. 1 hit.
    Pfami PF05922. Inhibitor_I9. 1 hit.
    PF00082. Peptidase_S8. 1 hit.
    [Graphical view ]
    PRINTSi PR00723. SUBTILISIN.
    SUPFAMi SSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    PROSITEi PS00136. SUBTILASE_ASP. 1 hit.
    PS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genes for alkaline protease and neutral protease from Bacillus amyloliquefaciens contain a large open reading frame between the regions coding for signal sequence and mature protein."
      Vasantha N., Thompson L.D., Rhodes C., Banner C., Nagle J., Filpula D.
      J. Bacteriol. 159:811-819(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 23844 / P.
    2. "Cloning, sequencing, and secretion of Bacillus amyloliquefaciens subtilisin in Bacillus subtilis."
      Wells J.A., Ferrari E., Henner D.J., Estell D.A., Chen E.Y.
      Nucleic Acids Res. 11:7911-7925(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-382.
    3. "Subtilisin BPN. VII. Isolation of cyanogen bromide peptides and the complete amino acid sequence."
      Markland F.S., Smith E.L.
      J. Biol. Chem. 242:5198-5211(1967) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 108-382.
    4. "Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food."
      Peng Y., Huang Q., Zhang R.-H., Zhang Y.-Z.
      Comp. Biochem. Physiol. 134B:45-52(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 108-131, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, VARIANT PHE-128.
      Strain: DC-4.
    5. "A hydrogen-bond network at the active site of subtilisin BPN'."
      Alden R.A., Wright C.S., Kraut J.
      Philos. Trans. R. Soc. Lond., B, Biol. Sci. 257:119-124(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    6. "Crystal structure at 2.6-A resolution of the complex of subtilisin BPN' with streptomyces subtilisin inhibitor."
      Hirono S., Akagawa H., Mitsui Y., Iitaka Y.
      J. Mol. Biol. 178:389-413(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
    7. "Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding."
      Pantoliano M.W., Whitlow M., Wood J.F., Dodd S.W., Hardman K.D., Rollence M.L., Bryan P.N.
      Biochemistry 28:7205-7213(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT.
    8. "Subtilisin BPN' at 1.6-A resolution: analysis for discrete disorder and comparison of crystal forms."
      Gallagher T., Oliver J., Bott R., Betzel C., Gilliland G.L.
      Acta Crystallogr. D 52:1125-1135(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    9. "Identification of histidine 64 in the active site of subtilisin."
      Markland F.S., Shaw E., Smith E.L.
      Proc. Natl. Acad. Sci. U.S.A. 61:1440-1447(1968) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE.

    Entry informationi

    Entry nameiSUBT_BACAM
    AccessioniPrimary (citable) accession number: P00782
    Secondary accession number(s): P83945, Q44684
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3