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Protein

Bacillolysin

Gene

npr

Organism
Bacillus cereus
Status
Reviewed-Annotation score: 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 Ca2+ ions per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Temperature dependencei

Thermolabile.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi307Calcium 11 Publication1
Metal bindingi309Calcium 11 Publication1
Metal bindingi311Calcium 1; via carbonyl oxygen1
Metal bindingi388Calcium 21 Publication1
Metal bindingi392Zinc; catalyticPROSITE-ProRule annotation1 Publication1
Active sitei3931
Metal bindingi396Zinc; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi416Zinc; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi427Calcium 21 Publication1
Metal bindingi427Calcium 31 Publication1
Metal bindingi433Calcium 3; via carbonyl oxygen1
Metal bindingi435Calcium 21 Publication1
Metal bindingi435Calcium 31 Publication1
Metal bindingi437Calcium 2; via carbonyl oxygen1
Metal bindingi440Calcium 21 Publication1
Metal bindingi440Calcium 31 Publication1
Metal bindingi443Calcium 4; via carbonyl oxygen1
Metal bindingi444Calcium 41 Publication1
Metal bindingi447Calcium 4; via carbonyl oxygen1
Metal bindingi450Calcium 41 Publication1
Active sitei481Proton donor1

GO - Molecular functioni

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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
PropeptideiPRO_000002859828 – 249Activation peptide1 PublicationAdd BLAST222
ChainiPRO_0000028599250 – 566BacillolysinAdd BLAST317

Interactioni

Protein-protein interaction databases

STRINGi226900.BC0602.

Structurei

Secondary structure

1566
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi253 – 260Combined sources8
Beta strandi266 – 274Combined sources9
Beta strandi277 – 282Combined sources6
Beta strandi284 – 287Combined sources4
Beta strandi289 – 298Combined sources10
Beta strandi306 – 312Combined sources7
Helixi315 – 317Combined sources3
Helixi318 – 338Combined sources21
Turni342 – 345Combined sources4
Beta strandi350 – 359Combined sources10
Beta strandi363 – 365Combined sources3
Beta strandi367 – 372Combined sources6
Beta strandi377 – 380Combined sources4
Helixi383 – 385Combined sources3
Helixi387 – 400Combined sources14
Turni401 – 403Combined sources3
Helixi409 – 429Combined sources21
Beta strandi436 – 439Combined sources4
Turni440 – 442Combined sources3
Beta strandi445 – 447Combined sources3
Beta strandi452 – 456Combined sources5
Helixi458 – 461Combined sources4
Helixi467 – 469Combined sources3
Helixi475 – 496Combined sources22
Beta strandi498 – 500Combined sources3
Beta strandi503 – 505Combined sources3
Helixi510 – 523Combined sources14
Helixi531 – 546Combined sources16
Helixi551 – 562Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ESPX-ray2.80A250-566[»]
1NPCX-ray2.00A250-566[»]
ProteinModelPortaliP05806.
SMRiP05806.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05806.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3227. LUCA.

Family and domain databases

CDDicd09597. M4_neutral_protease. 1 hit.
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.
RefSeqiWP_000730369.1. NZ_MCAX01000007.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M83910 Genomic DNA. Translation: AAA22620.1.
PIRiS22690. HYBSU.
RefSeqiWP_000730369.1. NZ_MCAX01000007.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ESPX-ray2.80A250-566[»]
1NPCX-ray2.00A250-566[»]
ProteinModelPortaliP05806.
SMRiP05806.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC0602.

Protein family/group databases

MEROPSiM04.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG3227. LUCA.

Miscellaneous databases

EvolutionaryTraceiP05806.

Family and domain databases

CDDicd09597. M4_neutral_protease. 1 hit.
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]
ProtoNetiSearch...

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 30, 2016
This is version 126 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

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.