Skip Header

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

Bacillolysin

Gene

npr

Organism
Bacillus caldolyticus
Status
Reviewed-Annotation score: 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 Ca2+ ions per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Temperature dependencei

Thermostable.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi285Calcium 1By similarity1
Metal bindingi287Calcium 1By similarity1
Metal bindingi289Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi366Calcium 2By similarity1
Metal bindingi370Zinc; catalyticPROSITE-ProRule annotation1
Active sitei371PROSITE-ProRule annotation1
Metal bindingi374Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi394Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi405Calcium 2By similarity1
Metal bindingi405Calcium 3By similarity1
Metal bindingi411Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi413Calcium 2By similarity1
Metal bindingi413Calcium 3By similarity1
Metal bindingi415Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi418Calcium 2By similarity1
Metal bindingi418Calcium 3By similarity1
Metal bindingi421Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi422Calcium 4By similarity1
Metal bindingi425Calcium 4; via carbonyl oxygenBy similarity1
Metal bindingi428Calcium 4By similarity1
Active sitei459Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Add BLAST25
PropeptideiPRO_000002860026 – 225Activation peptideAdd BLAST200
ChainiPRO_0000028601226 – 544BacillolysinAdd BLAST319

Keywords - PTMi

Zymogen

Structurei

3D structure databases

ProteinModelPortaliP23384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.Curated

Keywords - Domaini

Signal

Family and domain databases

CDDicd09597. M4_neutral_protease. 1 hit.
Gene3Di3.10.170.10. 1 hit.
InterProiIPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF03413. 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.
PIRiA42464.

3D structure databases

ProteinModelPortaliP23384.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd09597. M4_neutral_protease. 1 hit.
Gene3Di3.10.170.10. 1 hit.
InterProiIPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF03413. 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]
ProtoNetiSearch...

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 30, 2016
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.