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P43133

- THER_GEOSE

UniProt

P43133 - THER_GEOSE

Protein

Thermolysin

Gene

nprS

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Extracellular zinc metalloprotease.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 4 calcium ions per subunit.By similarity
    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

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    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

    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

    MKRKMKMKLV RFGLAAGLAA QVFFLPYNAL ASTEHVTWNQ QFQTPQFISG    50
    DLLKVNGTSP EELVYQYVEK NENKFKFHEN AKDTLQLKEK KNDNLGFTFM 100
    RFQQTYKGIP VFGAVVTAHV KDGTLTALSG TLIPNLDTKG SLKSGKKLSE 150
    KQARDIAEKD LVANVTKEVP EYEQGKDTEF VVYVNGDEAS LAYVVNLNFL 200
    TPEPGNWLYI IDAVDGKILN KFNQLDAAKP GDVKSITGTS TVGVGRGVLG 250
    DQKNINTTYS TYYYLQDNTR GNGIFTYDAK YRTTLPGSLW ADADNQFFAS 300
    YDAPAVDAHY YAGVTYDYYK NVHNRLSYDG NNAAIRSSVH YSQGYNNAFW 350
    NGSQMVYGDG DGQTFIPLSG GIDVVAHELT HAVTDYTAGL IYQNESGAIN 400
    EAISDIFGTL VEFYANKNPD WEIGEDVYTP GISGDSLRSM SDPAKYGDPD 450
    HYSKRYTGTQ DNGGVHINSG IINKAAYLIS QGGTHYGVSV VGIGRDKLGK 500
    IFYRALTQYL TPTSNFSQLR AAAVQSATDL YGSTSQEVAS VKQAFDAVGV 550
    K 551
    Length:551
    Mass (Da):60,617
    Last modified:November 1, 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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21663 Genomic DNA. Translation: AAB02774.1.
    M34237 Genomic DNA. Translation: AAA22625.1.
    PIRiA46564.
    B36706.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M21663 Genomic DNA. Translation: AAB02774.1 .
    M34237 Genomic DNA. Translation: AAA22625.1 .
    PIRi A46564.
    B36706.

    3D structure databases

    ProteinModelPortali P43133.
    SMRi P43133. Positions 236-551.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    DrugBanki DB01093. Dimethyl sulfoxide.

    Protein family/group databases

    MEROPSi M04.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.10.170.10. 1 hit.
    InterProi IPR011096. FTP_domain.
    IPR025711. PepSY.
    IPR023612. Peptidase_M4.
    IPR001570. Peptidase_M4_C_domain.
    IPR013856. Peptidase_M4_domain.
    [Graphical view ]
    Pfami PF07504. FTP. 1 hit.
    PF03413. PepSY. 1 hit.
    PF01447. Peptidase_M4. 1 hit.
    PF02868. Peptidase_M4_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00730. THERMOLYSIN.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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(1988) [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(1990) [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: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 92 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