P29148 (NPRE_PAEPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bacillolysin
EC=3.4.24.28

Alternative name(s):
Neutral protease

Gene names

Name:

npr

Organism

Paenibacillus polymyxa (Bacillus polymyxa)

Taxonomic identifier

1406 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	590 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the generation of beta- and alpha-amylases from the large amylase precursor.
Catalytic activity	Similar, but not identical, to that of thermolysin.
Cofactor	Binds 4 calcium ions per subunit Potential. Binds 1 zinc ion per subunit Potential.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase M4 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Propeptide

25 – 286

262

Activation peptide

PRO_0000028602

Chain

287 – 590

304

Bacillolysin

PRO_0000028603

Sites

Active site

424

1

By similarity

Active site

507

1

Proton donor By similarity

Metal binding

339

1

Calcium 1 Potential

Metal binding

341

1

Calcium 1 Potential

Metal binding

419

1

Calcium 2 Potential

Metal binding

423

1

Zinc; catalytic By similarity

Metal binding

427

1

Zinc; catalytic By similarity

Metal binding

447

1

Zinc; catalytic By similarity

Metal binding

466

1

Calcium 2 Potential

Metal binding

466

1

Calcium 3 Potential

Metal binding

469

1

Calcium 4; via carbonyl oxygen Potential

Metal binding

470

1

Calcium 4 Potential

Metal binding

473

1

Calcium 4; via carbonyl oxygen Potential

Metal binding

476

1

Calcium 4 Potential

Experimental info

Sequence conflict

287 – 289

3

NEA → ATG AA sequence Ref.1

Secondary structure

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590

Helix Strand Turn

Details...

Beta strand

290 – 292

3

Beta strand

298 – 302

5

Beta strand

304 – 306

3

Beta strand

309 – 314

6

Beta strand

321 – 325

5

Beta strand

338 – 344

7

Helix

347 – 367

21

Turn

371 – 373

3

Beta strand

379 – 388

10

Beta strand

392 – 394

3

Beta strand

399 – 401

3

Beta strand

408 – 411

4

Helix

414 – 416

3

Helix

418 – 431

14

Turn

432 – 434

3

Helix

440 – 458

19

Beta strand

460 – 465

6

Helix

466 – 468

3

Beta strand

478 – 482

5

Helix

484 – 487

4

Helix

493 – 495

3

Helix

501 – 522

22

Beta strand

524 – 526

3

Beta strand

529 – 531

3

Helix

536 – 549

14

Helix

557 – 572

16

Helix

577 – 589

13

Sequences

	Sequence		Length	Mass (Da)
	P29148 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 4ED303761408F6F3	FASTA	590	63,529
	10 20 30 40 50 60 MKKVWFSLLG GAMLLGSVAS GASAESSVSG PAQLTPTFHT EQWKAPSSVS GDDIVWSYLN 70 80 90 100 110 120 RQKKSLLGVD SSSVREQFRI VDRTSDKSGV SHYRLKQYVN GIPVYGAEQT IHVGKSGEVT 130 140 150 160 170 180 SYLGAVINED QQEEATQGTT PKISASEAVY TAYKEAAARI EALPTSDDTI SKDAEEPSSV 190 200 210 220 230 240 SKDTYAEAAN NDKTLSVDKD ELSLDKASVL KDSKIEAVEA EKSSIAKIAN LQPEVDPKAE 250 260 270 280 290 300 LYYYPKGDDL LLVYVTEVNV LEPAPLRTRY IIDANDGSIV FQYDIINEAT GKGVLGDSKS 310 320 330 340 350 360 FTTTASGSSY QLKDTTRGNG IVTYTASNRQ SIPGTLLTDA DNVWNDPAGV DAHAYAAKTY 370 380 390 400 410 420 DYYKSKFGRN SIDGRGLQLR STVHYGSRYN NAFWNGSQMT YGDGDGDGST FIAFSGDPDV 430 440 450 460 470 480 VGHELTHGVT EYTSNLEYYG ESGALNEAFS DVIGNDIQRK NWLVGDDIYT PNICGDALRS 490 500 510 520 530 540 MSNPTLYDQP HHYSNLYKGS SDNGGVHTNS GIINKAYYLL AQGGTFHGVT VNGIGRDAAV 550 560 570 580 590 QIYYSAFTNY LTSSSDFSNA RAAVIQAAKD LYGANSAEAT AAAKSFDAVG

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D00861 Genomic DNA. Translation: BAA00734.1.

PIR

A41335.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4GER	X-ray	1.59	A/B	290-590	[»]

ProteinModelPortal

P29148.

SMR

P29148. Positions 289-590.

ModBase

Search...

Protein family/group databases

MEROPS

M04.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.10.170.10. 1 hit.

InterPro

IPR011096. FTP_domain.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]

Pfam

PF07504. FTP. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]

PRINTS

PR00730. THERMOLYSIN.

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

NPRE_PAEPO

Accession

Primary (citable) accession number: P29148

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program