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P05806

- NPRE_BACCE

UniProt

P05806 - NPRE_BACCE

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Protein

Bacillolysin

Gene

npr

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Extracellular zinc metalloprotease.

Catalytic activityi

Similar, but not identical, to that of thermolysin.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 4 Ca(2+) ions per subunit.
  • Zn2+Note: 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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 2608Combined sources
Beta strandi266 – 2749Combined sources
Beta strandi277 – 2826Combined sources
Beta strandi284 – 2874Combined sources
Beta strandi289 – 29810Combined sources
Beta strandi306 – 3127Combined sources
Helixi315 – 3173Combined sources
Helixi318 – 33821Combined sources
Turni342 – 3454Combined sources
Beta strandi350 – 35910Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi367 – 3726Combined sources
Beta strandi377 – 3804Combined sources
Helixi383 – 3853Combined sources
Helixi387 – 40014Combined sources
Turni401 – 4033Combined sources
Helixi409 – 42921Combined sources
Beta strandi436 – 4394Combined sources
Turni440 – 4423Combined sources
Beta strandi445 – 4473Combined sources
Beta strandi452 – 4565Combined sources
Helixi458 – 4614Combined sources
Helixi467 – 4693Combined sources
Helixi475 – 49622Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi503 – 5053Combined sources
Helixi510 – 52314Combined sources
Helixi531 – 54616Combined sources
Helixi551 – 56212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MKKKSLALVL ATGMAVTTFG GTGSAFADSK NVLSTKKYNE TVQSPEFISG
60 70 80 90 100
DLTEATGKKA ESVVFDYLNA AKGDYKLGEK SAQDSFKVKQ VKKDAVTDST
110 120 130 140 150
VVRMQQVYEG VPVWGSTQVA HVSKDGSLKV LSGTVAPDLD KKEKLKNKNK
160 170 180 190 200
IEGAKAIEIA QQDLGVTPKY EVEPKADLYV YQNGEETTYA YVVNLNFLDP
210 220 230 240 250
SPGNYYYFIE ADSGKVLNKF NTIDHVTNDD KSPVKQEAPK QDAKAVVKPV
260 270 280 290 300
TGTNKVGTGK GVLGDTKSLN TTLSGSSYYL QDNTRGATIF TYDAKNRSTL
310 320 330 340 350
PGTLWADADN VFNAAYDAAA VDAHYYAGKT YDYYKATFNR NSINDAGAPL
360 370 380 390 400
KSTVHYGSNY NNAFWNGSQM VYGDGDGVTF TSLSGGIDVI GHELTHAVTE
410 420 430 440 450
NSSNLIYQNE SGALNEAISD IFGTLVEFYD NRNPDWEIGE DIYTPGKAGD
460 470 480 490 500
ALRSMSDPTK YGDPDHYSKR YTGSSDNGGV HTNSGIINKQ AYLLANGGTH
510 520 530 540 550
YGVTVTGIGK DKLGAIYYRA NTQYFTQSTT FSQARAGAVQ AAADLYGANS
560
AEVAAVKQSF SAVGVN
Length:566
Mass (Da):60,919
Last modified:October 1, 1996 - v2
Checksum:iE18B4572C2C4E1D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83910 Genomic DNA. Translation: AAA22620.1.
PIRiS22690. HYBSU.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83910 Genomic DNA. Translation: AAA22620.1 .
PIRi S22690. HYBSU.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 113 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