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P05806

- NPRE_BACCE

UniProt

P05806 - NPRE_BACCE

Protein

Bacillolysin

Gene

npr

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      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.
    Binds 1 zinc ion per subunit.

    Temperature dependencei

    Thermolabile.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi307 – 3071Calcium 11 Publication
    Metal bindingi309 – 3091Calcium 11 Publication
    Metal bindingi311 – 3111Calcium 1; via carbonyl oxygen
    Metal bindingi388 – 3881Calcium 21 Publication
    Metal bindingi392 – 3921Zinc; catalytic1 PublicationPROSITE-ProRule annotation
    Active sitei393 – 3931
    Metal bindingi396 – 3961Zinc; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi416 – 4161Zinc; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi427 – 4271Calcium 21 Publication
    Metal bindingi427 – 4271Calcium 31 Publication
    Metal bindingi433 – 4331Calcium 3; via carbonyl oxygen
    Metal bindingi435 – 4351Calcium 21 Publication
    Metal bindingi435 – 4351Calcium 31 Publication
    Metal bindingi437 – 4371Calcium 2; via carbonyl oxygen
    Metal bindingi440 – 4401Calcium 21 Publication
    Metal bindingi440 – 4401Calcium 31 Publication
    Metal bindingi443 – 4431Calcium 4; via carbonyl oxygen
    Metal bindingi444 – 4441Calcium 41 Publication
    Metal bindingi447 – 4471Calcium 4; via carbonyl oxygen
    Metal bindingi450 – 4501Calcium 41 Publication
    Active sitei481 – 4811Proton donor

    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
    Synonyms:nprC
    OrganismiBacillus cereus
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus 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 – 2727Sequence AnalysisAdd
    BLAST
    Propeptidei28 – 249222Activation peptide1 PublicationPRO_0000028598Add
    BLAST
    Chaini250 – 566317BacillolysinPRO_0000028599Add
    BLAST

    Structurei

    Secondary structure

    1
    566
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi253 – 2608
    Beta strandi266 – 2749
    Beta strandi277 – 2826
    Beta strandi284 – 2874
    Beta strandi289 – 29810
    Beta strandi306 – 3127
    Helixi315 – 3173
    Helixi318 – 33821
    Turni342 – 3454
    Beta strandi350 – 35910
    Beta strandi363 – 3653
    Beta strandi367 – 3726
    Beta strandi377 – 3804
    Helixi383 – 3853
    Helixi387 – 40014
    Turni401 – 4033
    Helixi409 – 42921
    Beta strandi436 – 4394
    Turni440 – 4423
    Beta strandi445 – 4473
    Beta strandi452 – 4565
    Helixi458 – 4614
    Helixi467 – 4693
    Helixi475 – 49622
    Beta strandi498 – 5003
    Beta strandi503 – 5053
    Helixi510 – 52314
    Helixi531 – 54616
    Helixi551 – 56212

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ESPX-ray2.80A250-566[»]
    1NPCX-ray2.00A250-566[»]
    ProteinModelPortaliP05806.
    SMRiP05806. Positions 250-566.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05806.

    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.

    P05806-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKKSLALVL ATGMAVTTFG GTGSAFADSK NVLSTKKYNE TVQSPEFISG    50
    DLTEATGKKA ESVVFDYLNA AKGDYKLGEK SAQDSFKVKQ VKKDAVTDST 100
    VVRMQQVYEG VPVWGSTQVA HVSKDGSLKV LSGTVAPDLD KKEKLKNKNK 150
    IEGAKAIEIA QQDLGVTPKY EVEPKADLYV YQNGEETTYA YVVNLNFLDP 200
    SPGNYYYFIE ADSGKVLNKF NTIDHVTNDD KSPVKQEAPK QDAKAVVKPV 250
    TGTNKVGTGK GVLGDTKSLN TTLSGSSYYL QDNTRGATIF TYDAKNRSTL 300
    PGTLWADADN VFNAAYDAAA VDAHYYAGKT YDYYKATFNR NSINDAGAPL 350
    KSTVHYGSNY NNAFWNGSQM VYGDGDGVTF TSLSGGIDVI GHELTHAVTE 400
    NSSNLIYQNE SGALNEAISD IFGTLVEFYD NRNPDWEIGE DIYTPGKAGD 450
    ALRSMSDPTK YGDPDHYSKR YTGSSDNGGV HTNSGIINKQ AYLLANGGTH 500
    YGVTVTGIGK DKLGAIYYRA NTQYFTQSTT FSQARAGAVQ AAADLYGANS 550
    AEVAAVKQSF SAVGVN 566
    Length:566
    Mass (Da):60,919
    Last modified:October 1, 1996 - v2
    Checksum:iE18B4572C2C4E1D3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83910 Genomic DNA. Translation: AAA22620.1.
    PIRiS22690. HYBSU.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M83910 Genomic DNA. Translation: AAA22620.1 .
    PIRi S22690. HYBSU.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ESP X-ray 2.80 A 250-566 [» ]
    1NPC X-ray 2.00 A 250-566 [» ]
    ProteinModelPortali P05806.
    SMRi P05806. Positions 250-566.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M04.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P05806.

    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. "The role of the pro-sequence in the processing and secretion of the thermolysin-like neutral protease from Bacillus cereus."
      Wetmore D.R., Wong S.L., Roche R.S.
      Mol. Microbiol. 6:1593-1604(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase."
      Sidler W., Niederer E., Suter F., Zuber H.
      Biol. Chem. Hoppe-Seyler 367:643-657(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 250-566.
      Strain: DSM 3101.
    3. "Crystal structure of neutral protease from Bacillus cereus refined at 3.0-A resolution and comparison with the homologous but more thermostable enzyme thermolysin."
      Pauptit R.A., Karlsson R., Picot D., Jenkins J.A., Niklaus-Reimer A.-S., Jansonius J.N.
      J. Mol. Biol. 199:525-537(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    4. "The structure of neutral protease from Bacillus cereus at 0.2-nm resolution."
      Stark W., Pauptit R.A., Wilson K.S., Jansonius J.N.
      Eur. J. Biochem. 207:781-791(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    5. "E144S active-site mutant of the Bacillus cereus thermolysin-like neutral protease at 2.8-A resolution."
      Lister S.A., Wetmore D.R., Roche R.S., Codding P.W.
      Acta Crystallogr. D 52:543-550(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT SER-393.

    Entry informationi

    Entry nameiNPRE_BACCE
    AccessioniPrimary (citable) accession number: P05806
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3