[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 16-31. STRAIN=ATCC 12872 / QMRDC B1551; PubMed=1840582 [NCBI, ExPASy, EBI, Israel, Japan] Sussman M.D., Setlow P.; "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis gpr gene, which codes for the protease that initiates degradation of small, acid-soluble proteins during spore germination."; J. Bacteriol. 173:291-300(1991).
[2]	CHARACTERIZATION. PubMed=9748439 [NCBI, ExPASy, EBI, Israel, Japan] Nessi C., Jedrzejas M.J., Setlow P.; "Structure and mechanism of action of the protease that degrades small, acid-soluble spore proteins during germination of spores of Bacillus species."; J. Bacteriol. 180:5077-5084(1998).
[3]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF ZYMOGEN P46. DOI=10.1006/jmbi.2000.3849; PubMed=10864493 [NCBI, ExPASy, EBI, Israel, Japan] Ponnuraj K., Rowland S., Nessi C., Setlow P., Jedrzejas M.J.; "Crystal structure of a novel germination protease from spores of Bacillus megaterium: structural arrangement and zymogen activation."; J. Mol. Biol. 300:1-10(2000).

Comments

FUNCTION: Initiates the rapid degradation of small, acid-soluble proteins during spore germination.
CATALYTIC ACTIVITY: Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala.
SUBUNIT: Homotetramer.
DEVELOPMENTAL STAGE: GPR transcription occurs during sporulation in forespore first by sigma-F and then by sigma-G.
PTM: Autoproteolytically processed. The inactive tetrameric zymogen termed p46 autoprocesses to a smaller form termed p41, which is active only during spore germination.
SIMILARITY: Belongs to the peptidase A25 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M55262; AAA22499.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A39198; A39198.

3D structure databases

PDB

1C8B; X-ray; 3.00 A; A/B=1-371.

[ExPASy / RCSB / EBI]

PDBsum

1C8B; -.

ModBase

P22321.

Protein family/group databases

MEROPS

A25.001; -.

Ontologies

GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from HAMAP).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from HAMAP).
GO:0009847;	Biological process: spore germination (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00626; -; 1.
PBIL [Tree]

InterPro

IPR005080; Peptidase_A25.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.10100; Peptidase_A25; 1.

Pfam

PF03418; Peptidase_A25; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF019549; Peptidase_A25; 1.

ProDom

PD041835; Peptidase_A25; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR01441; GPR; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Hydrolase; Protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 15`	`15`		`PRO_0000026868`
`CHAIN`	`16 371`	`356`	`Germination protease.`	`PRO_0000026869`
`HELIX`	`19 27`	`9`
`STRAND`	`43 51`	`9`
`STRAND`	`54 61`	`8`
`HELIX`	`63 66`	`4`
`TURN`	`67 70`	`4`
`STRAND`	`74 80`	`7`
`STRAND`	`84 89`	`6`
`HELIX`	`90 106`	`17`
`STRAND`	`115 119`	`5`
`STRAND`	`123 125`	`3`
`HELIX`	`126 128`	`3`
`HELIX`	`130 136`	`7`
`HELIX`	`142 147`	`6`
`STRAND`	`159 162`	`4`
`HELIX`	`165 167`	`3`
`HELIX`	`174 185`	`12`
`STRAND`	`188 196`	`9`
`HELIX`	`201 203`	`3`
`STRAND`	`204 211`	`8`
`STRAND`	`219 222`	`4`
`STRAND`	`227 230`	`4`
`STRAND`	`246 252`	`7`
`STRAND`	`255 257`	`3`
`HELIX`	`261 264`	`4`
`TURN`	`265 269`	`5`
`HELIX`	`316 323`	`8`
`STRAND`	`331 335`	`5`
`HELIX`	`338 353`	`16`
`HELIX`	`354 357`	`4`

Sequence information

Length: 371 AA [This is the length of the unprocessed precursor]

Molecular weight: 40626 Da [This is the MW of the unprocessed precursor]

CRC64: 40ABE62ECA2F835D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKELDLSQY SVRTDLAVEA KDIALENQPK PNNQSEIKGV IVKEKEEQGV KISMVEITEE 

        70         80         90        100        110        120 
GAEAIGKKKG RYVTLESVGI REQDTEKQEE AMEEVFAKEL NFFIKSLNIP DDASCLVVGL 

       130        140        150        160        170        180 
GNLSVTPDAL GPKAVDNLLI TRHLFELQPE SVQDGFRPVS AIVPGVMGMT GIETSDIIFG 

       190        200        210        220        230        240 
VVKKVNPDFI IAIDALAARS IERVNATIQI SDSGIHPGSG VGNKRKEISY ETLGIPVIAI 

       250        260        270        280        290        300 
GIPTVVDAVS ITSDTIDFIL KHFGREMKEQ GKPSKSLLPS GMTFGEKKKL TEDDLPNEEQ 

       310        320        330        340        350        360 
RQTYLGMIGT LPDEEKRRLI HEVLAPLGHN LMVTPKEVDM FIEDMANVVA GGLNAALHHE 

       370 
VDQENFGAYT H

P22321 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools