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Protein

Thermolysin

Gene

nprS

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Extracellular zinc metalloprotease.1 Publication

Catalytic activityi

Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+By similarityNote: Binds 4 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Temperature dependencei

Thermostable. Retains about 45% of its activity after treatment of 90 degrees Celsius for 30 minutes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi292Calcium 1By similarity1
Metal bindingi294Calcium 1By similarity1
Metal bindingi296Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi373Calcium 2By similarity1
Metal bindingi377Zinc; catalyticPROSITE-ProRule annotation1
Active sitei378PROSITE-ProRule annotation1
Metal bindingi381Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi401Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi412Calcium 2By similarity1
Metal bindingi412Calcium 3By similarity1
Metal bindingi418Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi420Calcium 2By similarity1
Metal bindingi420Calcium 3By similarity1
Metal bindingi422Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi425Calcium 2By similarity1
Metal bindingi425Calcium 3By similarity1
Metal bindingi429Calcium 4By similarity1
Metal bindingi432Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi435Calcium 4By similarity1
Active sitei466Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.28. 623.

Protein family/group databases

MEROPSiM04.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermolysin (EC:3.4.24.27)
Alternative name(s):
Neutral protease
Gene namesi
Name:nprS
Synonyms:nprM
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.
DB03255. Phenol.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
PropeptideiPRO_000002861232 – 235Activation peptide2 PublicationsAdd BLAST204
ChainiPRO_0000028613236 – 551ThermolysinAdd BLAST316

Keywords - PTMi

Zymogen

Expressioni

Inductioni

Is expressed in the stationary phase. Up-regulated by NprA.1 Publication

Structurei

Secondary structure

1551
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi238 – 246Combined sources9
Beta strandi252 – 264Combined sources13
Beta strandi274 – 278Combined sources5
Beta strandi291 – 297Combined sources7
Helixi300 – 302Combined sources3
Helixi303 – 321Combined sources19
Turni327 – 329Combined sources3
Beta strandi335 – 344Combined sources10
Beta strandi348 – 350Combined sources3
Beta strandi352 – 358Combined sources7
Beta strandi362 – 366Combined sources5
Helixi368 – 370Combined sources3
Helixi372 – 386Combined sources15
Helixi394 – 415Combined sources22
Beta strandi421 – 424Combined sources4
Turni425 – 427Combined sources3
Beta strandi437 – 441Combined sources5
Helixi443 – 445Combined sources3
Helixi452 – 454Combined sources3
Helixi461 – 464Combined sources4
Turni465 – 468Combined sources4
Helixi469 – 481Combined sources13
Beta strandi483 – 485Combined sources3
Beta strandi488 – 490Combined sources3
Helixi495 – 508Combined sources14
Helixi516 – 531Combined sources16
Helixi536 – 547Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DLHX-ray2.25A236-551[»]
ProteinModelPortaliP43133.
SMRiP43133.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd09597. M4_neutral_protease. 1 hit.
Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSiPR00730. THERMOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P43133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRKMKMKLV RFGLAAGLAA QVFFLPYNAL ASTEHVTWNQ QFQTPQFISG
60 70 80 90 100
DLLKVNGTSP EELVYQYVEK NENKFKFHEN AKDTLQLKEK KNDNLGFTFM
110 120 130 140 150
RFQQTYKGIP VFGAVVTAHV KDGTLTALSG TLIPNLDTKG SLKSGKKLSE
160 170 180 190 200
KQARDIAEKD LVANVTKEVP EYEQGKDTEF VVYVNGDEAS LAYVVNLNFL
210 220 230 240 250
TPEPGNWLYI IDAVDGKILN KFNQLDAAKP GDVKSITGTS TVGVGRGVLG
260 270 280 290 300
DQKNINTTYS TYYYLQDNTR GNGIFTYDAK YRTTLPGSLW ADADNQFFAS
310 320 330 340 350
YDAPAVDAHY YAGVTYDYYK NVHNRLSYDG NNAAIRSSVH YSQGYNNAFW
360 370 380 390 400
NGSQMVYGDG DGQTFIPLSG GIDVVAHELT HAVTDYTAGL IYQNESGAIN
410 420 430 440 450
EAISDIFGTL VEFYANKNPD WEIGEDVYTP GISGDSLRSM SDPAKYGDPD
460 470 480 490 500
HYSKRYTGTQ DNGGVHINSG IINKAAYLIS QGGTHYGVSV VGIGRDKLGK
510 520 530 540 550
IFYRALTQYL TPTSNFSQLR AAAVQSATDL YGSTSQEVAS VKQAFDAVGV

K
Length:551
Mass (Da):60,617
Last modified:November 1, 1995 - v1
Checksum:iFCF4B2B5A7870129
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10 – 14VRFGL → RSFGV AA sequence (PubMed:2203733).Curated5
Sequence conflicti24Missing in AAB02774 (PubMed:2203733).Curated1
Sequence conflicti29 – 33ALAST → RLASS AA sequence (PubMed:2203733).Curated5
Sequence conflicti114A → Q in AAB02774 (PubMed:2203733).Curated1
Sequence conflicti124T → S in AAB02774 (PubMed:2203733).Curated1
Sequence conflicti134P → PIP AA sequence (PubMed:2203733).Curated1
Sequence conflicti261T → S in AAB02774 (PubMed:2203733).Curated1
Sequence conflicti463G → A in AAB02774 (PubMed:2203733).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21663 Genomic DNA. Translation: AAB02774.1.
M34237 Genomic DNA. Translation: AAA22625.1.
PIRiA46564.
B36706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21663 Genomic DNA. Translation: AAB02774.1.
M34237 Genomic DNA. Translation: AAA22625.1.
PIRiA46564.
B36706.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5DLHX-ray2.25A236-551[»]
ProteinModelPortaliP43133.
SMRiP43133.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB02325. Isopropyl Alcohol.
DB03255. Phenol.

Protein family/group databases

MEROPSiM04.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.28. 623.

Family and domain databases

CDDicd09597. M4_neutral_protease. 1 hit.
Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSiPR00730. THERMOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHER_GEOSE
AccessioniPrimary (citable) accession number: P43133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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.