Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P23384

- NPRE_BACCL

UniProt

P23384 - NPRE_BACCL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bacillolysin

Gene

npr

Organism
Bacillus caldolyticus
Status
Reviewed - Annotation score: 3 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+By similarityNote: Binds 4 Ca(2+) ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Temperature dependencei

Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi285 – 2851Calcium 1By similarity
Metal bindingi287 – 2871Calcium 1By similarity
Metal bindingi289 – 2891Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi366 – 3661Calcium 2By similarity
Metal bindingi370 – 3701Zinc; catalyticPROSITE-ProRule annotation
Active sitei371 – 3711PROSITE-ProRule annotation
Metal bindingi374 – 3741Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi394 – 3941Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi405 – 4051Calcium 2By similarity
Metal bindingi405 – 4051Calcium 3By similarity
Metal bindingi411 – 4111Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi413 – 4131Calcium 2By similarity
Metal bindingi413 – 4131Calcium 3By similarity
Metal bindingi415 – 4151Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi418 – 4181Calcium 2By similarity
Metal bindingi418 – 4181Calcium 3By similarity
Metal bindingi421 – 4211Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi422 – 4221Calcium 4By similarity
Metal bindingi425 – 4251Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi428 – 4281Calcium 4By similarity
Active sitei459 – 4591Proton 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

Names & Taxonomyi

Protein namesi
Recommended name:
Bacillolysin (EC:3.4.24.28)
Alternative name(s):
Thermostable neutral protease
Gene namesi
Name:npr
OrganismiBacillus caldolyticus
Taxonomic identifieri1394 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillusGeobacillus thermoleovorans 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 – 2525Add
BLAST
Propeptidei26 – 225200Activation peptidePRO_0000028600Add
BLAST
Chaini226 – 544319BacillolysinPRO_0000028601Add
BLAST

Keywords - PTMi

Zymogen

Structurei

3D structure databases

ProteinModelPortaliP23384.
SMRiP23384. Positions 226-543.
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.

P23384-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNKRAMLGAI GLAFGLMAWP FGASAKGKSM VWNEQWKTPS FVSGSLLGRC
60 70 80 90 100
SQELVYRYLD QEKNTFQLGG QARERLSLIG NKLDELGHTV MRFEQAIAAS
110 120 130 140 150
LCMGAVLVAH VNDGELSSLS GTLIPNLDKR TLKTEAAISI QQAEMIAKQD
160 170 180 190 200
VADRVTKERP AAEEGKPTRL VIYPDEETPR LAYEVNVRFL TPVPGNWIYM
210 220 230 240 250
IDAADGKVLN KWNQMDEAKP GGAQPVAGTS TVGVGRGVLG DQKYINTTYS
260 270 280 290 300
SYYGYYYLQD NTRGSGIFTY DGRNRTVLPG SLWADGDNQF FASYDAAAVD
310 320 330 340 350
AHYYAGVVYD YYKNVHGRLS YDGSNAAIRS TVHYGRGYNN AFWNGSQMVY
360 370 380 390 400
GDGDGQTFLP FSGGIDVVGH ELTHAVTDYT AGLVYQNESG AINEAMSDIF
410 420 430 440 450
GTLVEFYANR NPDWEIGEDI YTPGVAGDAL RSMSDPAKYG DPDHYSKRYT
460 470 480 490 500
GTQDNGGVHT NSGIINKAAY LLSQGGVHYG VSVTGIGRDK MGKIFYRALV
510 520 530 540
YYLTPTSNFS QLRAACVQAA ADLYGSTSQE VNSVKQAFNA VGVY
Length:544
Mass (Da):59,413
Last modified:November 1, 1991 - v1
Checksum:iC551E67ACCA356FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63575 Genomic DNA. Translation: AAA22623.1.
PIRiA42464.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63575 Genomic DNA. Translation: AAA22623.1 .
PIRi A42464.

3D structure databases

ProteinModelPortali P23384.
SMRi P23384. Positions 226-543.
ModBasei Search...
MobiDBi Search...

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. "A highly thermostable neutral protease from Bacillus caldolyticus: cloning and expression of the gene in Bacillus subtilis and characterization of the gene product."
    van den Burg B., Enequist H.G., van de Haar M.E., Eijsink V.G.H., Stulp B.K., Venema G.
    J. Bacteriol. 173:4107-4115(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiNPRE_BACCL
AccessioniPrimary (citable) accession number: P23384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 26, 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

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