P00782

EV
Gene name
apr
Protein name
Subtilisin BPN'
Names
Alkaline protease, Subtilisin DFE, Subtilisin Novo
Species
Bacillus amyloliquefaciens (Bacillus velezensis)
KEGG Pathway
EC number
3.4.21.62: Serine endopeptidases
Protein Class
PEPTIDASE S8 (PTHR43806)

Descriptions

Serine protease subtilisin BPN (SBT) is secreted by the soil bacterium for the apparent biological function of digesting environmental proteins for bacterial absorption. The N-terminal prosegment domain forms a compact domain that binds SBT through an extensive interface involving the two parallel surface helices of enzyme, and binds the active site of SBT in a product-like manner, with Tyr77 in P1 binding pocket. This N-terminal 77 residues must be removed for the activation of this enzyme.

Autoinhibitory domains (AIDs)

1-77 (N-terminal prosegment domain) EV

Target domain

132-360 (Subtilisin Carlsberg-like catalytic domain)

Relief mechanism

Cleavage

Assay

Mutagenesis experiment, Structural analysis

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

64 structures for P00782

Entry ID Method Resolution Chain Position Source
1A2Q X-ray 180 A A 108-382 PDB
1AK9 X-ray 180 A A 108-382 PDB
1AQN X-ray 180 A A 108-382 PDB
1AU9 X-ray 180 A A 108-382 PDB
1DUI X-ray 200 A A 108-382 PDB
1GNS X-ray 180 A A 112-382 PDB
1GNV X-ray 190 A A 108-382 PDB
1LW6 X-ray 150 A E 108-382 PDB
1S01 X-ray 170 A A 108-382 PDB
1S02 X-ray 190 A A 108-382 PDB
1SBH X-ray 180 A A 108-382 PDB
1SBI X-ray 220 A A 108-382 PDB
1SBN X-ray 210 A E 108-382 PDB
1SBT X-ray 250 A A 108-382 PDB
1SIB X-ray 240 A E 108-382 PDB
1SPB X-ray 200 A PDB
1ST2 X-ray 200 A A 108-382 PDB
1SUA X-ray 210 A A 108-382 PDB
1SUB X-ray 175 A A 108-382 PDB
1SUC X-ray 180 A A 108-382 PDB
1SUD X-ray 190 A A 108-382 PDB
1SUE X-ray 180 A A 108-382 PDB
1SUP X-ray 160 A A 108-382 PDB
1TM1 X-ray 170 A E 108-382 PDB
1TM3 X-ray 157 A E 108-382 PDB
1TM4 X-ray 170 A E 108-382 PDB
1TM5 X-ray 145 A E 108-382 PDB
1TM7 X-ray 159 A E 108-382 PDB
1TMG X-ray 167 A E 108-382 PDB
1TO1 X-ray 168 A E 108-382 PDB
1TO2 X-ray 130 A E 108-382 PDB
1UBN X-ray 240 A A 108-382 PDB
1V5I X-ray 150 A A 108-382 PDB
1Y1K X-ray 156 A E 108-382 PDB
1Y33 X-ray 180 A E 108-382 PDB
1Y34 X-ray 155 A E 108-382 PDB
1Y3B X-ray 180 A E 108-382 PDB
1Y3C X-ray 169 A E 108-382 PDB
1Y3D X-ray 180 A E 108-382 PDB
1Y3F X-ray 172 A E 108-382 PDB
1Y48 X-ray 184 A E 108-382 PDB
1Y4A X-ray 160 A E 108-382 PDB
1Y4D X-ray 200 A E 108-382 PDB
1YJA X-ray 180 A A 108-382 PDB
1YJB X-ray 180 A A 108-382 PDB
1YJC X-ray 180 A A 108-382 PDB
2SBT X-ray 280 A A 108-382 PDB
2SIC X-ray 180 A E 108-382 PDB
2SNI X-ray 210 A E 108-382 PDB
2ST1 X-ray 180 A A 108-382 PDB
3BGO X-ray 180 A PDB
3CNQ X-ray 171 A PDB
3CO0 X-ray 193 A PDB
3F49 X-ray 170 A S 108-382 PDB
3SIC X-ray 180 A E 108-382 PDB
5OX2 X-ray 224 A A 108-382 PDB
5SIC X-ray 220 A E 108-382 PDB
7AM3 X-ray 161 A A 108-382 PDB
7AM4 X-ray 181 A A 108-382 PDB
7AM5 X-ray 230 A A 108-382 PDB
7AM6 X-ray 270 A A/B/C 108-382 PDB
7AM7 X-ray 261 A A/B/C 108-382 PDB
7AM8 X-ray 204 A A 108-382 PDB
AF-P00782-F1 Predicted AlphaFoldDB

1 variants for P00782

Variant ID(s) Position Change Description Diseaes Association Provenance
128 Y>F strain: DC-4 [UniProt] No

No associated diseases with P00782

6 regional properties for P00782

Type Name Position InterPro Accession
domain Peptidase S8/S53 domain 130 - 366 IPR000209
domain Peptidase S8 propeptide/proteinase inhibitor I9 39 - 105 IPR010259
active_site Peptidase S8, subtilisin, His-active site 171 - 181 IPR022398
active_site Peptidase S8, subtilisin, Asp-active site 135 - 146 IPR023827
active_site Peptidase S8, subtilisin, Ser-active site 326 - 336 IPR023828
domain Subtilisin Carlsberg-like catalytic domain 132 - 360 IPR034202

Functions

Description
EC Number 3.4.21.62 Serine endopeptidases
Subcellular Localization
  • Secreted
PANTHER Family PTHR43806 PEPTIDASE S8
PANTHER Subfamily PTHR43806:SF59 CEREVISIN-RELATED
PANTHER Protein Class serine protease
protease
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

3 GO annotations of biological process

Name Definition
fibrinolysis A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
sporulation resulting in formation of a cellular spore The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRGKKVWISL LFALALIFTM AFGSTSSAQA AGKSNGEKKY IVGFKQTMST MSAAKKKDVI
70 80 90 100 110 120
SEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE DHVAHAYAQS VPYGVSQIKA
130 140 150 160 170 180
PALHSQGYTG SNVKVAVIDS GIDSSHPDLK VAGGASMVPS ETNPFQDNNS HGTHVAGTVA
190 200 210 220 230 240
ALNNSIGVLG VAPSASLYAV KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA
250 260 270 280 290 300
ALKAAVDKAV ASGVVVVAAA GNEGTSGSSS TVGYPGKYPS VIAVGAVDSS NQRASFSSVG
310 320 330 340 350 360
PELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN TQVRSSLENT
370 380
TTKLGDSFYY GKGLINVQAA AQ