M-protease precursor - Bacillus clausii (strain KSM-K16)

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Q99405 (PRTM_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
M-protease
EC=3.4.21.-

Gene names

Name:	aprE
Ordered Locus Names:	ABC0761

Organism

Bacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]

Taxonomic identifier

66692 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	380 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)

Cofactor	Binds 2 calcium ions per subunit.
Subunit structure	Monomer.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase S8 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Serine protease
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of catalytic activity Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	identical protein binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase 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 – 27

Potential

Propeptide

28 – 111

PRO_0000027142

Chain

112 – 380

269

M-protease

PRO_0000027143

Sites

Active site

143

Charge relay system

Active site

173

Charge relay system

Active site

326

Charge relay system

Metal binding

113

Calcium 1

Metal binding

151

Calcium 1

Metal binding

184

Calcium 1; via carbonyl oxygen

Metal binding

186

Calcium 1

Metal binding

188

Calcium 1; via carbonyl oxygen

Metal binding

190

Calcium 1; via carbonyl oxygen

Metal binding

274

Calcium 2; via carbonyl oxygen

Metal binding

276

Calcium 2; via carbonyl oxygen

Metal binding

279

Calcium 2; via carbonyl oxygen

Secondary structure

380

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q99405 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 9A916CFACD8E43E9
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FASTA

380

38,881

        10         20         30         40         50         60 
MKKPLGKIVA STALLISVAF SSSIASAAEE AKEKYLIGFN EQEAVSEFVE QIEANDDVAI 

        70         80         90        100        110        120 
LSEEEEVEIE LLHEFETIPV LSVELSPEDV DALELDPTIS YIEEDAEVTT MAQSVPWGIS 

       130        140        150        160        170        180 
RVQAPAAHNR GLTGSGVKVA VLDTGISTHP DLNIRGGASF VPGEPSTQDG NGHGTHVAGT 

       190        200        210        220        230        240 
IAALNNSIGV LGVAPSAELY AVKVLGASGS GSVSSIAQGL EWAGNNGMHV ANLSLGSPSP 

       250        260        270        280        290        300 
SATLEQAVNS ATSRGVLVVA ASGNSGAGSI SYPARYANAM AVGATDQNNN RASFSQYGAG 

       310        320        330        340        350        360 
LDIVAPGVNV QSTYPGSTYA SLNGTSMATP HVAGVAALVK QKNPSWSNVQ IRNHLKNTAT 

       370        380 
GLGNTNLYGS GLVNAEAATR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16." Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KSM-K16.
[2]	"Purification and properties of an alkaline protease from alkalophilic Bacillus sp. KSM-K16." Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K., Kawai S., Ito S. Appl. Microbiol. Biotechnol. 43:473-481(1995) [PubMed: 7632397] [Abstract] Cited for: PROTEIN SEQUENCE OF 112-134, CHARACTERIZATION.
[3]	"Structure of a new alkaline serine protease (M-protease) from Bacillus sp. KSM-K16." Yamane T., Kani T., Hatanaka T., Suzuki A., Ashida T., Kobayashi T., Ito S., Yamashita O. Acta Crystallogr. D 51:199-206(1995) [PubMed: 15299321] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 112-380.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AP006627 Genomic DNA. Translation: BAD63300.1.

RefSeq

YP_174261.1. NC_006582.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MPT	X-ray	2.40	A	112-380	[»]
1WSD	X-ray	1.50	A	112-380	[»]

ProteinModelPortal

Q99405.

SMR

Q99405. Positions 112-380.

ModBase

Search...

Protein family/group databases

MEROPS

S08.010.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000048168; EBBACP00000046929; EBBACG00000048159.

GeneID

3201703.

GenomeReviews

Gene locus ABC0761 in contig AP006627_GR.

KEGG

bcl:ABC0761.

NMPDR

fig|66692.3.peg.1095.

PATRIC

18920804. VBIBacCla58185_0807.

Organism-specific databases

CMR

Search...

Phylogenomic databases

eggNOG

COG1404.

GeneTree

EBGT00050000000194.

HOGENOM

HBG752219.

OMA

TSMATSH.

ProtClustDB

CLSK2484250.

Enzyme and pathway databases

BioCyc

BCLA66692:ABC0761-MONOMER.

Family and domain databases

InterPro

IPR000209. Peptidase_S8/S53.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR009020. Prot_inh_propept.
IPR010259. Prot_inh_S8A.
[Graphical view]

Gene3D

G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.

K01342.

PANTHER

PTHR10795. SubtilSerProt. 1 hit.

Pfam

PF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]

PRINTS

PR00723. SUBTILISIN.

SUPFAM

SSF52743. Pept_S8_S53. 1 hit.
SSF54897. Prot_inh_propept. 1 hit.

PROSITE

PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRTM_BACSK

Accession

Primary (citable) accession number: Q99405
Secondary accession number(s): Q5WK05

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 4, 2005
Last modified:	January 25, 2012
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents