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P43263

- NPRE_BREBE

UniProt

P43263 - NPRE_BREBE

Protein

Bacillolysin

Gene

npr

Organism
Brevibacillus brevis (Bacillus brevis)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Extracellular zinc metalloprotease.

    Catalytic activityi

    Similar, but not identical, to that of thermolysin.

    Cofactori

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

    Temperature dependencei

    Thermolabile.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi276 – 2761Calcium 1Sequence Analysis
    Metal bindingi278 – 2781Calcium 1Sequence Analysis
    Metal bindingi354 – 3541Calcium 2Sequence Analysis
    Metal bindingi358 – 3581Zinc; catalyticPROSITE-ProRule annotation
    Active sitei359 – 3591PROSITE-ProRule annotation
    Metal bindingi362 – 3621Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi382 – 3821Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi393 – 3931Calcium 2Sequence Analysis
    Metal bindingi393 – 3931Calcium 3Sequence Analysis
    Metal bindingi394 – 3941Calcium 3; via carbonyl oxygenSequence Analysis
    Metal bindingi396 – 3961Calcium 2Sequence Analysis
    Metal bindingi396 – 3961Calcium 3Sequence Analysis
    Metal bindingi401 – 4011Calcium 2Sequence Analysis
    Metal bindingi401 – 4011Calcium 3Sequence Analysis
    Metal bindingi404 – 4041Calcium 4; via carbonyl oxygenSequence Analysis
    Metal bindingi405 – 4051Calcium 4Sequence Analysis
    Metal bindingi411 – 4111Calcium 4Sequence Analysis
    Active sitei442 – 4421Proton 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:
    Bacillolysin (EC:3.4.24.28)
    Alternative name(s):
    Neutral protease
    Gene namesi
    Name:npr
    OrganismiBrevibacillus brevis (Bacillus brevis)
    Taxonomic identifieri1393 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaeBrevibacillus

    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 – 2828Sequence AnalysisAdd
    BLAST
    Propeptidei29 – 223195Activation peptide1 PublicationPRO_0000028596Add
    BLAST
    Chaini224 – 527304BacillolysinPRO_0000028597Add
    BLAST

    Keywords - PTMi

    Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliP43263.
    SMRiP43263. Positions 226-527.
    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.

    P43263-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKSYLATSL TLSIAVGVSG FTSVPAFAKT KIDYHKQWDT PQYIGEVWEP    50
    EGAKGDDVVW SYLEKYKDEF RIQGNVEDHF EIVNEARNKE TDTKHYRLQE 100
    VYNGIPIYGF QQTVHIDADG NVTSFLGQFI PDLDSNKQLK KKPKLNEQKA 150
    VKQAIKDVEG EVGEKPDFIQ DPEAKLYIYV HEDESYLAYA VELNFLDPEP 200
    GRWMYFIDAH SGDVINKYNM LDHVTATGKG VLGDTKQFET TKQGSTYMLK 250
    DTTRGKGIET YTANNRTSLP GTLMTDSDNY WTDGAAVDAH AHAQKTYDYF 300
    RNVHNRNSYD GNGAVIRSTV HYSTRYNNAF WNGSQMVYGD GDGTTFLPLS 350
    GGLDVVAHEL THAVTERTAG LVYQNESGAL NESMSDIFGA MVDNDDWLMG 400
    EDIYTPGRSG DALRSLQDPA AYGDPDHYSK RYTGSQDNGG VHTNSGINNK 450
    AAYLLAEGGT HYGVRVNGIG RTDTAKIYYH ALTHYLTPYS NFSAMRRAAV 500
    LSATDLFGAN SRQVQAVNAA YDAVGVK 527
    Length:527
    Mass (Da):58,646
    Last modified:November 1, 1995 - v1
    Checksum:i8D3704C3C9D8D756
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61286 Genomic DNA. Translation: CAA43589.1.
    PIRiPN0114.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61286 Genomic DNA. Translation: CAA43589.1 .
    PIRi PN0114.

    3D structure databases

    ProteinModelPortali P43263.
    SMRi P43263. Positions 226-527.
    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. "Structure of the Bacillus brevis metalloprotease gene."
      Avakov A.S., Bolotin A.P., Sorokin A.V.
      Mol. Biol. (Mosk.) 24:1363-1372(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 7882.
    2. "Analysis of the structure of Bacillus brevis neutral proteinase and its biosynthesis in Bacillus subtilis cells."
      Kaidalova N.V., Akimkina T.V., Khodova O.D., Kostrov S.V., Strongin A.Y.
      Mol. Biol. (Mosk.) 24:1381-1392(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 224-228, CHARACTERIZATION.

    Entry informationi

    Entry nameiNPRE_BREBE
    AccessioniPrimary (citable) accession number: P43263
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 87 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