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Q43880

- THER_ALIAC

UniProt

Q43880 - THER_ALIAC

Protein

Thermolysin

Gene
N/A
Organism
Alicyclobacillus acidocaldarius (Bacillus acidocaldarius)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (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 bindingi407 – 4071Calcium 2By similarity
    Metal bindingi407 – 4071Calcium 3By similarity
    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
    OrganismiAlicyclobacillus acidocaldarius (Bacillus acidocaldarius)
    Taxonomic identifieri1388 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesAlicyclobacillaceaeAlicyclobacillus

    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_0000028584Add
    BLAST
    Chaini229 – 546318ThermolysinPRO_0000028585Add
    BLAST

    Keywords - PTMi

    Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliQ43880.
    SMRiQ43880. 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.

    Q43880-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKRAMLGAI 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):59,770
    Last modified:November 1, 1996 - v1
    Checksum:i3AC33A611BD2B071
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07824 Genomic DNA. Translation: AAC43402.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07824 Genomic DNA. Translation: AAC43402.1 .

    3D structure databases

    ProteinModelPortali Q43880.
    SMRi Q43880. 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. "Cloning and sequencing of the neutral protease-encoding gene from a thermophilic strain of Bacillus sp."
      Vecerek B., Kyslik P.
      Gene 158:147-148(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: BT1.

    Entry informationi

    Entry nameiTHER_ALIAC
    AccessioniPrimary (citable) accession number: Q43880
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 72 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