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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi292 – 2921Calcium 1By similarity
Metal bindingi294 – 2941Calcium 1By similarity
Metal bindingi296 – 2961Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi373 – 3731Calcium 2By similarity
Metal bindingi377 – 3771Zinc; catalyticPROSITE-ProRule annotation
Active sitei378 – 3781PROSITE-ProRule annotation
Metal bindingi381 – 3811Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi401 – 4011Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi412 – 4121Calcium 2By similarity
Metal bindingi412 – 4121Calcium 3By similarity
Metal bindingi418 – 4181Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi420 – 4201Calcium 2By similarity
Metal bindingi420 – 4201Calcium 3By similarity
Metal bindingi422 – 4221Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi425 – 4251Calcium 2By similarity
Metal bindingi425 – 4251Calcium 3By similarity
Metal bindingi429 – 4291Calcium 4By similarity
Metal bindingi432 – 4321Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi435 – 4351Calcium 4By similarity
Active sitei466 – 4661Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
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

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Propeptidei32 – 235204Activation peptide2 PublicationsPRO_0000028612Add
BLAST
Chaini236 – 551316ThermolysinPRO_0000028613Add
BLAST

Keywords - PTMi

Zymogen

Expressioni

Inductioni

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

Structurei

3D structure databases

ProteinModelPortaliP43133.
SMRiP43133. Positions 236-551.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.Curated

Keywords - Domaini

Signal

Family and domain databases

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:October 31, 1995 - v1
Checksum:iFCF4B2B5A7870129
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 145VRFGL → RSFGV AA sequence (PubMed:2203733).Curated
Sequence conflicti24 – 241Missing in AAB02774 (PubMed:2203733).Curated
Sequence conflicti29 – 335ALAST → RLASS AA sequence (PubMed:2203733).Curated
Sequence conflicti114 – 1141A → Q in AAB02774 (PubMed:2203733).Curated
Sequence conflicti124 – 1241T → S in AAB02774 (PubMed:2203733).Curated
Sequence conflicti134 – 1341P → PIP AA sequence (PubMed:2203733).Curated
Sequence conflicti261 – 2611T → S in AAB02774 (PubMed:2203733).Curated
Sequence conflicti463 – 4631G → A in AAB02774 (PubMed:2203733).Curated

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

ProteinModelPortaliP43133.
SMRiP43133. Positions 236-551.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB03255. 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

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...

Publicationsi

  1. "Cloning and nucleotide sequence of the highly thermostable neutral protease gene from Bacillus stearothermophilus."
    Kubo M., Imanaka T.
    J. Gen. Microbiol. 134:1883-1892(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 236-240, FUNCTION AS A PROTEASE, TEMPERATURE DEPENDENCE, SUBCELLULAR LOCATION.
    Strain: MK232.
  2. "Cloning and nucleotide sequences of the Bacillus stearothermophilus neutral protease gene and its transcriptional activator gene."
    Nishiya Y., Imanaka T.
    J. Bacteriol. 172:4861-4869(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 236-239, INDUCTION.
    Strain: TELNE.

Entry informationi

Entry nameiTHER_GEOSE
AccessioniPrimary (citable) accession number: P43133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1995
Last sequence update: October 31, 1995
Last modified: March 31, 2015
This is version 96 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

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.