Reviewed, UniProtKB/Swiss-Prot P22321 (GPR_BACME)

Names and origin

Protein names

Recommended name:
    Germination protease
    EC=3.4.24.78
Alternative name(s):
    Spore protease
    GPR endopeptidase
    Germination proteinase

Gene names

Name:

gpr

Organism

Bacillus megaterium

Taxonomic identifier

1404 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	371 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	Initiates the rapid degradation of small, acid-soluble proteins during spore germination. HAMAP MF_00626
Catalytic activity	Endopeptidase action with P4 Glu or Asp, P1 preferably Glu > Asp, P1' hydrophobic and P2' Ala. HAMAP MF_00626
Subunit structure	Homotetramer. HAMAP MF_00626
Developmental stage	GPR transcription occurs during sporulation in forespore first by sigma-F and then by sigma-G. HAMAP MF_00626
Post-translational modification	Autoproteolytically processed. The inactive tetrameric zymogen termed p46 autoprocesses to a smaller form termed p41, which is active only during spore germination. HAMAP MF_00626
Sequence similarities	Belongs to the peptidase A25 family.

Ontologies

Keywords
Molecular function	Hydrolase Protease
PTM	Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: HAMAP spore germination Inferred from electronic annotation. Source: HAMAP
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 15

15

Ref.1

PRO_0000026868

Chain

16 – 371

356

Germination protease HAMAP MF_00626

PRO_0000026869

Secondary structure

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371

Helix Strand Turn

Details...

Helix

19 – 27

9

Beta strand

43 – 51

9

Beta strand

54 – 61

8

Helix

63 – 66

4

Turn

67 – 70

4

Beta strand

74 – 80

7

Beta strand

84 – 89

6

Helix

90 – 106

17

Beta strand

115 – 119

5

Beta strand

123 – 125

3

Helix

126 – 128

3

Helix

130 – 136

7

Helix

142 – 147

6

Beta strand

159 – 162

4

Helix

165 – 167

3

Helix

174 – 185

12

Beta strand

188 – 196

9

Helix

201 – 203

3

Beta strand

204 – 211

8

Beta strand

219 – 222

4

Beta strand

227 – 230

4

Beta strand

246 – 252

7

Beta strand

255 – 257

3

Helix

261 – 264

4

Turn

265 – 269

5

Helix

316 – 323

8

Beta strand

331 – 335

5

Helix

338 – 353

16

Helix

354 – 357

4

Sequences

	Sequence		Length	Mass (Da)
	P22321-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 40ABE62ECA2F835D	FASTA	371	40,626
	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

References

[1]	"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." Sussman M.D., Setlow P. J. Bacteriol. 173:291-300(1991) [PubMed: 1840582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 16-31. Strain: ATCC 12872 / QMRDC B1551.
[2]	"Structure and mechanism of action of the protease that degrades small, acid-soluble spore proteins during germination of spores of Bacillus species." Nessi C., Jedrzejas M.J., Setlow P. J. Bacteriol. 180:5077-5084(1998) [PubMed: 9748439] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Crystal structure of a novel germination protease from spores of Bacillus megaterium: structural arrangement and zymogen activation." Ponnuraj K., Rowland S., Nessi C., Setlow P., Jedrzejas M.J. J. Mol. Biol. 300:1-10(2000) [PubMed: 10864493] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF ZYMOGEN P46.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M55262 Genomic DNA. Translation: AAA22499.1.

PIR

A39198.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C8B	X-ray	3.00	A/B	1-371	[»]

ModBase

Search...

Protein family/group databases

MEROPS

A25.001.

Enzyme and pathway databases

BRENDA

3.4.24.78. 325.

Family and domain databases

HAMAP

MF_00626.
[Tree]

InterPro

IPR005080. Peptidase_A25.
[Graphical view]

Gene3D

G3DSA:3.40.50.10100. Peptidase_A25. 1 hit.

Pfam

PF03418. Peptidase_A25. 1 hit.
[Graphical view]

PIRSF

PIRSF019549. Peptidase_A25. 1 hit.

ProDom

PD041835. Peptidase_A25. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01441. GPR. 1 hit.

ProtoNet

Search...

Entry information

Entry name

GPR_BACME

Accession

Primary (citable) accession number: P22321

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	January 20, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)