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Q59193

- THER_BACCL

UniProt

Q59193 - THER_BACCL

Protein

Thermolysin

Gene

npr

Organism
Bacillus caldolyticus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Extracellular zinc metalloprotease.

    Catalytic activityi

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

    Cofactori

    Binds 4 calcium ions per subunit.
    Binds 1 zinc ion per subunit.

    Temperature dependencei

    Thermostable.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi287 – 2871Calcium 1By similarity
    Metal bindingi289 – 2891Calcium 1By similarity
    Metal bindingi291 – 2911Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi368 – 3681Calcium 2By similarity
    Metal bindingi372 – 3721Zinc; catalyticPROSITE-ProRule annotation
    Active sitei373 – 3731PROSITE-ProRule annotation
    Metal bindingi376 – 3761Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi396 – 3961Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi413 – 4131Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi415 – 4151Calcium 2By similarity
    Metal bindingi415 – 4151Calcium 3By similarity
    Metal bindingi417 – 4171Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi420 – 4201Calcium 2By similarity
    Metal bindingi420 – 4201Calcium 3By similarity
    Metal bindingi423 – 4231Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi424 – 4241Calcium 4By similarity
    Metal bindingi427 – 4271Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi430 – 4301Calcium 4By similarity
    Active sitei461 – 4611Proton 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):
    Thermostable neutral proteinase
    Gene namesi
    Name:npr
    OrganismiBacillus caldolyticus
    Taxonomic identifieri1394 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillusGeobacillus thermoleovorans group

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Propeptidei26 – 228203Activation peptidePRO_0000028586Add
    BLAST
    Chaini229 – 546318ThermolysinPRO_0000028587Add
    BLAST

    Keywords - PTMi

    Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliQ59193.
    SMRiQ59193. Positions 228-545.
    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.

    Q59193-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKRAMLGAI GLAFGLMAWP FGASAKEKSM VWNEQWKTPS FVSGSLLKGE    50
    DAPEELVYRY LDQEKNTFQL GGQARERLSL IGKQTDELGH TVMRFEQRYR 100
    GIPVYGAVLV AHVNDGELSS LSGTLIPNLD KRTLKTEAAI SIQQAEMIAK 150
    QDVADAVTKE RPAAEEGKPT RLVIYPDGET PRLAYEVNVR FLTPVPGNWI 200
    YMIDAADGKV LNKWNQMDEA KPGGGQPVAG TSTVGVGRGV LGDQKYINTT 250
    YSSYYGYYYL QDNTRGSGIF TYDGRNRTVL PGSLWADGDN QFFASYDAAA 300
    VDAHYYAGVV YDYYKNVHGR LSYDGSNAAI RSTVHYGRGY NNAFWNGSQM 350
    VYGDGDGQTF LPFSGGIDVV GHELTHAVTD YTAGLVYQNE SGAINEAMSD 400
    IFGTLVEFYA NRNPDWEIGE DIYTPGIAGD ALRSMSDPAK YGDPDHYSKR 450
    YTGTQDNGGV HTNSGIINKA AYLLSQGGVH YGVSVTGIGR DKMGKIFYRA 500
    LVYYLTPTSN FSQLRAACVQ AAADLYGSTS QEVNSVKQAF NAVGVY 546
    Length:546
    Mass (Da):59,771
    Last modified:November 1, 1996 - v1
    Checksum:i38019807FF32B071
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25629 Genomic DNA. Translation: AAB18652.1.
    PIRiS72176.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U25629 Genomic DNA. Translation: AAB18652.1 .
    PIRi S72176.

    3D structure databases

    ProteinModelPortali Q59193.
    SMRi Q59193. Positions 228-545.
    ModBasei Search...
    MobiDBi Search...

    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. "Sequence of the gene encoding a highly thermostable neutral proteinase from Bacillus sp. strain EA1: expression in Escherichia coli and characterisation."
      Saul D.J., Williams L.C., Toogood H.S., Daniel R.M., Bergquist P.L.
      Biochim. Biophys. Acta 1308:74-80(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: DSM 405 / NBRC 15313 / YP-T.

    Entry informationi

    Entry nameiTHER_BACCL
    AccessioniPrimary (citable) accession number: Q59193
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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