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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.Curated
Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi339 – 3391Calcium 1Sequence Analysis
Metal bindingi341 – 3411Calcium 1Sequence Analysis
Metal bindingi419 – 4191Calcium 2Sequence Analysis
Metal bindingi423 – 4231Zinc; catalyticPROSITE-ProRule annotation
Active sitei424 – 4241PROSITE-ProRule annotation
Metal bindingi427 – 4271Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi447 – 4471Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi466 – 4661Calcium 2Sequence Analysis
Metal bindingi466 – 4661Calcium 3Sequence Analysis
Metal bindingi469 – 4691Calcium 4; via carbonyl oxygenSequence Analysis
Metal bindingi470 – 4701Calcium 4Sequence Analysis
Metal bindingi473 – 4731Calcium 4; via carbonyl oxygenSequence Analysis
Metal bindingi476 – 4761Calcium 4Sequence Analysis
Active sitei507 – 5071Proton donorPROSITE-ProRule annotation

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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 286262Activation peptide1 PublicationPRO_0000028602Add
BLAST
Chaini287 – 590304BacillolysinPRO_0000028603Add
BLAST

Keywords - PTMi

Zymogen

Structurei

Secondary structure

1
590
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.
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.
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

        10         20         30         40         50
MKKVWFSLLG GAMLLGSVAS GASAESSVSG PAQLTPTFHT EQWKAPSSVS
60 70 80 90 100
GDDIVWSYLN RQKKSLLGVD SSSVREQFRI VDRTSDKSGV SHYRLKQYVN
110 120 130 140 150
GIPVYGAEQT IHVGKSGEVT SYLGAVINED QQEEATQGTT PKISASEAVY
160 170 180 190 200
TAYKEAAARI EALPTSDDTI SKDAEEPSSV SKDTYAEAAN NDKTLSVDKD
210 220 230 240 250
ELSLDKASVL KDSKIEAVEA EKSSIAKIAN LQPEVDPKAE LYYYPKGDDL
260 270 280 290 300
LLVYVTEVNV LEPAPLRTRY IIDANDGSIV FQYDIINEAT GKGVLGDSKS
310 320 330 340 350
FTTTASGSSY QLKDTTRGNG IVTYTASNRQ SIPGTLLTDA DNVWNDPAGV
360 370 380 390 400
DAHAYAAKTY DYYKSKFGRN SIDGRGLQLR STVHYGSRYN NAFWNGSQMT
410 420 430 440 450
YGDGDGDGST FIAFSGDPDV VGHELTHGVT EYTSNLEYYG ESGALNEAFS
460 470 480 490 500
DVIGNDIQRK NWLVGDDIYT PNICGDALRS MSNPTLYDQP HHYSNLYKGS
510 520 530 540 550
SDNGGVHTNS GIINKAYYLL AQGGTFHGVT VNGIGRDAAV QIYYSAFTNY
560 570 580 590
LTSSSDFSNA RAAVIQAAKD LYGANSAEAT AAAKSFDAVG
Length:590
Mass (Da):63,529
Last modified:December 1, 1992 - v1
Checksum:i4ED303761408F6F3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2893NEA → ATG AA sequence (PubMed:1834632)Curated

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: October 29, 2014
This is version 90 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