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Protein

Subtilisin E

Gene

aprE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: 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.

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+1 PublicationNote: Binds 2 calcium ions per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi108 – 1081Calcium 1
Active sitei138 – 1381Charge relay system
Metal bindingi147 – 1471Calcium 1
Active sitei170 – 1701Charge relay system
Metal bindingi181 – 1811Calcium 1; via carbonyl oxygen
Metal bindingi183 – 1831Calcium 1
Metal bindingi185 – 1851Calcium 1; via carbonyl oxygen
Metal bindingi187 – 1871Calcium 1; via carbonyl oxygen
Metal bindingi275 – 2751Calcium 2; via carbonyl oxygen
Metal bindingi277 – 2771Calcium 2; via carbonyl oxygen
Metal bindingi280 – 2801Calcium 2
Metal bindingi303 – 3031Calcium 2
Active sitei327 – 3271Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Sporulation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU10300-MONOMER.
SABIO-RKP04189.

Protein family/group databases

MEROPSiS08.036.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilisin E (EC:3.4.21.62)
Gene namesi
Name:aprE
Synonyms:apr, aprA, sprE
Ordered Locus Names:BSU10300
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381D → N: Prevents intramolecular processing to an active enzyme. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Propeptidei30 – 10677PRO_0000027187Add
BLAST
Chaini107 – 381275Subtilisin EPRO_0000027188Add
BLAST

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

PaxDbiP04189.
PRIDEiP04189.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005716.

Structurei

Secondary structure

1
381
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 437Combined sources
Beta strandi45 – 484Combined sources
Helixi52 – 609Combined sources
Turni61 – 633Combined sources
Beta strandi65 – 695Combined sources
Beta strandi71 – 8010Combined sources
Helixi82 – 898Combined sources
Beta strandi94 – 996Combined sources
Beta strandi102 – 1054Combined sources
Helixi112 – 1165Combined sources
Helixi119 – 1257Combined sources
Beta strandi133 – 1397Combined sources
Beta strandi150 – 1556Combined sources
Beta strandi167 – 1693Combined sources
Helixi170 – 17910Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi195 – 2006Combined sources
Beta strandi206 – 2094Combined sources
Helixi210 – 22213Combined sources
Beta strandi226 – 2305Combined sources
Beta strandi232 – 2354Combined sources
Helixi239 – 25012Combined sources
Beta strandi254 – 2585Combined sources
Turni274 – 2763Combined sources
Beta strandi280 – 2867Combined sources
Beta strandi304 – 3074Combined sources
Beta strandi309 – 3157Combined sources
Turni316 – 3183Combined sources
Beta strandi319 – 3235Combined sources
Helixi326 – 34318Combined sources
Helixi349 – 35810Combined sources
Helixi366 – 3694Combined sources
Helixi376 – 3794Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCJX-ray2.00A107-381[»]
B36-106[»]
3WHIX-ray2.40A/B30-381[»]
DisProtiDP00394.
ProteinModelPortaliP04189.
SMRiP04189. Positions 36-381.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04189.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 379247Peptidase S8Add
BLAST

Domaini

The propeptide functions as an intramolecular chaperone which is essential for the correct folding of the protease domain but is not required for enzymatic function of the folded protein. It is autoprocessed and degraded after completion of the folding process.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105RX7. Bacteria.
COG1404. LUCA.
HOGENOMiHOG000199176.
InParanoidiP04189.
KOiK01342.
OMAiQYSWIIN.
PhylomeDBiP04189.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. 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. Propept_inh.
IPR010259. S8pro/Inhibitor_I9.
[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.

P04189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSKKLWISL LFALTLIFTM AFSNMSAQAA GKSSTEKKYI VGFKQTMSAM
60 70 80 90 100
SSAKKKDVIS EKGGKVQKQF KYVNAAAATL DEKAVKELKK DPSVAYVEED
110 120 130 140 150
HIAHEYAQSV PYGISQIKAP ALHSQGYTGS NVKVAVIDSG IDSSHPDLNV
160 170 180 190 200
RGGASFVPSE TNPYQDGSSH GTHVAGTIAA LNNSIGVLGV APSASLYAVK
210 220 230 240 250
VLDSTGSGQY SWIINGIEWA ISNNMDVINM SLGGPTGSTA LKTVVDKAVS
260 270 280 290 300
SGIVVAAAAG NEGSSGSTST VGYPAKYPST IAVGAVNSSN QRASFSSAGS
310 320 330 340 350
ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA
360 370 380
QVRDRLESTA TYLGNSFYYG KGLINVQAAA Q
Length:381
Mass (Da):39,479
Last modified:June 16, 2009 - v3
Checksum:i5C8A4B0E42FCE83D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271A → V in CAA74536 (PubMed:9579061).Curated
Sequence conflicti191 – 1911A → S in AAA22742 (PubMed:6427178).Curated
Sequence conflicti191 – 1911A → S in CAA74536 (PubMed:9579061).Curated
Sequence conflicti191 – 1911A → S (PubMed:7589571).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01988 Genomic DNA. Translation: AAA22742.1.
Y14083 Genomic DNA. Translation: CAA74536.1.
AL009126 Genomic DNA. Translation: CAB12870.2.
K01443 Genomic DNA. Translation: AAA22814.1.
M16639 Genomic DNA. Translation: AAA22744.1.
M31060 Genomic DNA. Translation: AAA22246.1.
M19125 Genomic DNA. Translation: AAA22245.1.
PIRiA00972. SUBSI.
RefSeqiNP_388911.2. NC_000964.3.
WP_003233171.1. NZ_JNCM01000035.1.
WP_009966941.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB12870; CAB12870; BSU10300.
GeneIDi939313.
KEGGibsu:BSU10300.
PATRICi18973758. VBIBacSub10457_1073.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01988 Genomic DNA. Translation: AAA22742.1.
Y14083 Genomic DNA. Translation: CAA74536.1.
AL009126 Genomic DNA. Translation: CAB12870.2.
K01443 Genomic DNA. Translation: AAA22814.1.
M16639 Genomic DNA. Translation: AAA22744.1.
M31060 Genomic DNA. Translation: AAA22246.1.
M19125 Genomic DNA. Translation: AAA22245.1.
PIRiA00972. SUBSI.
RefSeqiNP_388911.2. NC_000964.3.
WP_003233171.1. NZ_JNCM01000035.1.
WP_009966941.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SCJX-ray2.00A107-381[»]
B36-106[»]
3WHIX-ray2.40A/B30-381[»]
DisProtiDP00394.
ProteinModelPortaliP04189.
SMRiP04189. Positions 36-381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005716.

Protein family/group databases

MEROPSiS08.036.

Proteomic databases

PaxDbiP04189.
PRIDEiP04189.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12870; CAB12870; BSU10300.
GeneIDi939313.
KEGGibsu:BSU10300.
PATRICi18973758. VBIBacSub10457_1073.

Phylogenomic databases

eggNOGiENOG4105RX7. Bacteria.
COG1404. LUCA.
HOGENOMiHOG000199176.
InParanoidiP04189.
KOiK01342.
OMAiQYSWIIN.
PhylomeDBiP04189.

Enzyme and pathway databases

BioCyciBSUB:BSU10300-MONOMER.
SABIO-RKP04189.

Miscellaneous databases

EvolutionaryTraceiP04189.

Family and domain databases

Gene3Di3.30.70.80. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR000209. 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. Propept_inh.
IPR010259. S8pro/Inhibitor_I9.
[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]
ProtoNetiSearch...

Entry informationi

Entry nameiSUBT_BACSU
AccessioniPrimary (citable) accession number: P04189
Secondary accession number(s): O07613, P70989
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: June 16, 2009
Last modified: September 7, 2016
This is version 148 of the entry and version 3 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, 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. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.