Kumamolisin - Bacillus sp. MN-32

Preferred order of sections

Names and origin

Protein names

Submitted name:
Kumamolisin EMBL BAB85637.2

Gene names

Name:

kscp EMBL BAB85637.2

Organism

Bacillus sp. MN-32 EMBL BAB85637.2

Taxonomic identifier

198803 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG Metal-binding PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG
Technical term	3D-structure PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular_function	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

Chain

189 – 552

364

kumamolisin EMBL BAB85637.2

PRO_5000049828

Sites

Metal binding

504

1

Calcium PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG

Metal binding

505

1

Calcium; via carbonyl oxygen PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG

Metal binding

522

1

Calcium; via carbonyl oxygen PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG

Metal binding

524

1

Calcium; via carbonyl oxygen PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG

Metal binding

526

1

Calcium PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG

Sequences

Sequence

Length

Mass (Da)

Tools

Q8RR56 [UniParc].

Last modified June 1, 2003. Version 2.
Checksum: 7EA9586DD366835C
Show »

FASTA

552

57,743

        10         20         30         40         50         60 
MSDMEKPWKE EEKREVLAGH ARRQAPQAVD KGPVTGDQRI SVTVVLRRQR GDELEAHVER 

        70         80         90        100        110        120 
QAALAPHARV HLEREAFAAS HGASLDDFAE IRKFAEAHGL TLDRAHVAAG TAVLSGPVDA 

       130        140        150        160        170        180 
VNQAFGVELR HFDHPDGSYR SYVGDVRVPA SIAPLIEAVF GLDTRPVARP HFRLRRRAEG 

       190        200        210        220        230        240 
EFEARSQSAA PTAYTPLDVA QAYQFPEGLD GQGQCIAIIE LGGGYDETSL AQYFASLGVS 

       250        260        270        280        290        300 
APQVVSVSVD GATNQPTGDP NGPDGEVELD IEVAGALAPG AKIAVYFAPN TDAGFLNAIT 

       310        320        330        340        350        360 
TAVHDPTHKP SIVSISWGGP EDSWAPASIA AMNRAFLDAA ALGVTVLAAA GDSGSTDGEQ 

       370        380        390        400        410        420 
DGLYHVDFPA ASPYVLACGG TRLVASAGRI ERETVWNDGP DGGSTGGGVS RIFPLPSWQE 

       430        440        450        460        470        480 
RANVPPSANP GAGSGRGVPD VAGNADPATG YEVVIDGETT VIGGTSAVAP LFAALVARIN 

       490        500        510        520        530        540 
QKLGKPVGYL NPTLYQLPPE VFHDITEGNN DIANRARIYQ AGPGWDPCTG LGSPIGIRLL 

       550 
QALLPSASQA QP

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References

[1]	"A CLN2-related and thermostable serine-carboxyl proteinase, kumamolysin: cloning, expression, and identification of catalytic serine residue." Oyama H., Hamada T., Ogasawara S., Uchida K., Murao S., Beyer B.B., Dunn M.B., Oda K. J. Biochem. 131:757-765(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: MN-32 EMBL BAB85637.2.
[2]	"The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase." Comellas-Bigler M., Fuentes-Prior P., Maskos K., Huber R., Oyama H., Uchida K., Dunn B.M., Oda K., Bode W. Structure 10:865-876(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 189-545 IN COMPLEX WITH CALCIUM.
[3]	"1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase." Comellas-Bigler M., Maskos K., Huber R., Oyama H., Oda K., Bode W. Structure 12:1313-1323(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB070740 Genomic DNA. Translation: BAB85637.2.

PIR

JC7833.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GT9	X-ray	1.38	1/2	189-545	[»]
1GTG	X-ray	2.30	1	189-545	[»]
1GTJ	X-ray	1.75	1/2	189-545	[»]
1GTL	X-ray	2.80	1/2	189-545	[»]
1T1E	X-ray	1.18	A	1-552	[»]
1T1G	X-ray	1.18	A	189-552	[»]
1T1I	X-ray	1.28	A	189-552	[»]

ProteinModelPortal

Q8RR56.

SMR

Q8RR56. Positions 12-545.

ModBase

Search...

Protein family/group databases

MEROPS

S53.004.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.4.21.B48. 275055.

Family and domain databases

Gene3D

3.40.50.200. 1 hit.

InterPro

IPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
[Graphical view]

Pfam

PF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]

SMART

SM00944. Pro-kuma_activ. 1 hit.
[Graphical view]

SUPFAM

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

ProtoNet

Search...

Other

EvolutionaryTrace

Q8RR56.

Entry information

Entry name

Q8RR56_9BACI

Accession

Primary (citable) accession number: Q8RR56

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2002
Last sequence update:	June 1, 2003
Last modified:	April 3, 2013
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)