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P00782

- SUBT_BACAM

UniProt

P00782 - SUBT_BACAM

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Protein

Subtilisin BPN'

Gene

apr

Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Ca2+Note: 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. 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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 446Combined sources
Turni46 – 494Combined sources
Helixi53 – 619Combined sources
Turni62 – 643Combined sources
Beta strandi66 – 705Combined sources
Beta strandi72 – 809Combined sources
Helixi83 – 908Combined sources
Beta strandi95 – 1006Combined sources
Beta strandi105 – 1084Combined sources
Helixi113 – 1175Combined sources
Helixi120 – 1267Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi168 – 1703Combined sources
Helixi171 – 18010Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi195 – 2017Combined sources
Beta strandi207 – 2093Combined sources
Helixi211 – 22313Combined sources
Beta strandi227 – 2315Combined sources
Beta strandi233 – 2364Combined sources
Helixi240 – 25112Combined sources
Beta strandi255 – 2595Combined sources
Turni275 – 2773Combined sources
Beta strandi281 – 2877Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi305 – 3084Combined sources
Beta strandi310 – 3167Combined sources
Turni317 – 3193Combined sources
Beta strandi320 – 3245Combined sources
Helixi327 – 34418Combined sources
Helixi350 – 3589Combined sources
Beta strandi360 – 3623Combined sources
Helixi367 – 3704Combined sources
Helixi377 – 3804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST
60 70 80 90 100
MSAAKKKDVI SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE
110 120 130 140 150
DHVAHAYAQS VPYGVSQIKA PALHSQGYTG SNVKVAVIDS GIDSSHPDLK
160 170 180 190 200
VAGGASMVPS ETNPFQDNNS HGTHVAGTVA ALNNSIGVLG VAPSASLYAV
210 220 230 240 250
KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA ALKAAVDKAV
260 270 280 290 300
ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG
310 320 330 340 350
PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN
360 370 380
TQVRSSLENT TTKLGDSFYY GKGLINVQAA AQ
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. Curated

Natural variant

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 130 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