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P29148

- NPRE_PAEPO

UniProt

P29148 - NPRE_PAEPO

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Protein
Bacillolysin
Gene
npr
Organism
Paenibacillus polymyxa (Bacillus polymyxa)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the generation of beta- and alpha-amylases from the large amylase precursor.

Catalytic activityi

Similar, but not identical, to that of thermolysin.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi339 – 3391Calcium 1 Reviewed prediction
Metal bindingi341 – 3411Calcium 1 Reviewed prediction
Metal bindingi419 – 4191Calcium 2 Reviewed prediction
Metal bindingi423 – 4231Zinc; catalytic By similarity
Active sitei424 – 4241 By similarity
Metal bindingi427 – 4271Zinc; catalytic By similarity
Metal bindingi447 – 4471Zinc; catalytic By similarity
Metal bindingi466 – 4661Calcium 2 Reviewed prediction
Metal bindingi466 – 4661Calcium 3 Reviewed prediction
Metal bindingi469 – 4691Calcium 4; via carbonyl oxygen Reviewed prediction
Metal bindingi470 – 4701Calcium 4 Reviewed prediction
Metal bindingi473 – 4731Calcium 4; via carbonyl oxygen Reviewed prediction
Metal bindingi476 – 4761Calcium 4 Reviewed prediction
Active sitei507 – 5071Proton donor By similarity

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
OrganismiPaenibacillus polymyxa (Bacillus polymyxa)
Taxonomic identifieri1406 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed prediction
Add
BLAST
Propeptidei25 – 286262Activation peptide
PRO_0000028602Add
BLAST
Chaini287 – 590304Bacillolysin
PRO_0000028603Add
BLAST

Keywords - PTMi

Zymogen

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi290 – 2923
Beta strandi298 – 3025
Beta strandi304 – 3063
Beta strandi309 – 3146
Beta strandi321 – 3255
Beta strandi338 – 3447
Helixi347 – 36721
Turni371 – 3733
Beta strandi379 – 38810
Beta strandi392 – 3943
Beta strandi399 – 4024
Beta strandi408 – 4114
Helixi414 – 4163
Helixi418 – 43114
Turni432 – 4343
Helixi440 – 45819
Beta strandi460 – 4656
Helixi466 – 4683
Beta strandi478 – 4825
Helixi484 – 4874
Helixi493 – 4953
Helixi501 – 52222
Beta strandi524 – 5263
Beta strandi529 – 5313
Helixi536 – 54914
Helixi557 – 57216
Helixi577 – 58913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GERX-ray1.59A/B290-590[»]
ProteinModelPortaliP29148.
SMRiP29148. Positions 289-590.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 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.

P29148-1 [UniParc]FASTAAdd to Basket

« Hide

MKKVWFSLLG GAMLLGSVAS GASAESSVSG PAQLTPTFHT EQWKAPSSVS    50
GDDIVWSYLN RQKKSLLGVD SSSVREQFRI VDRTSDKSGV SHYRLKQYVN 100
GIPVYGAEQT IHVGKSGEVT SYLGAVINED QQEEATQGTT PKISASEAVY 150
TAYKEAAARI EALPTSDDTI SKDAEEPSSV SKDTYAEAAN NDKTLSVDKD 200
ELSLDKASVL KDSKIEAVEA EKSSIAKIAN LQPEVDPKAE LYYYPKGDDL 250
LLVYVTEVNV LEPAPLRTRY IIDANDGSIV FQYDIINEAT GKGVLGDSKS 300
FTTTASGSSY QLKDTTRGNG IVTYTASNRQ SIPGTLLTDA DNVWNDPAGV 350
DAHAYAAKTY DYYKSKFGRN SIDGRGLQLR STVHYGSRYN NAFWNGSQMT 400
YGDGDGDGST FIAFSGDPDV VGHELTHGVT EYTSNLEYYG ESGALNEAFS 450
DVIGNDIQRK NWLVGDDIYT PNICGDALRS MSNPTLYDQP HHYSNLYKGS 500
SDNGGVHTNS GIINKAYYLL AQGGTFHGVT VNGIGRDAAV QIYYSAFTNY 550
LTSSSDFSNA RAAVIQAAKD LYGANSAEAT AAAKSFDAVG 590
Length:590
Mass (Da):63,529
Last modified:December 1, 1992 - v1
Checksum:i4ED303761408F6F3
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2893NEA → ATG AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00861 Genomic DNA. Translation: BAA00734.1.
PIRiA41335.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00861 Genomic DNA. Translation: BAA00734.1 .
PIRi A41335.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4GER X-ray 1.59 A/B 290-590 [» ]
ProteinModelPortali P29148.
SMRi P29148. Positions 289-590.
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.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view ]
Pfami PF07504. FTP. 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. "Proteases involved in generation of beta- and alpha-amylases from a large amylase precursor in Bacillus polymyxa."
    Takekawa S., Uozumi N., Tsukagoshi N., Udaka S.
    J. Bacteriol. 173:6820-6825(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 287-301.
    Strain: 72.

Entry informationi

Entry nameiNPRE_PAEPO
AccessioniPrimary (citable) accession number: P29148
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 14, 2014
This is version 88 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

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

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