Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Kumamolisin

Gene

kscp

Organism
Bacillus sp. MN-32
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi504 – 5041CalciumCombined sources
Metal bindingi505 – 5051Calcium; via carbonyl oxygenCombined sources
Metal bindingi522 – 5221Calcium; via carbonyl oxygenCombined sources
Metal bindingi524 – 5241Calcium; via carbonyl oxygenCombined sources
Metal bindingi526 – 5261CalciumCombined sources

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BRENDAi3.4.21.B48. 275055.

Protein family/group databases

MEROPSiS53.004.

Names & Taxonomyi

Protein namesi
Submitted name:
KumamolisinImported
Gene namesi
Name:kscpImported
OrganismiBacillus sp. MN-32Imported
Taxonomic identifieri198803 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini189 – 552364kumamolisinImportedPRO_5000049828Add
BLAST

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GT9X-ray1.381/2189-545[»]
1GTGX-ray2.301189-545[»]
1GTJX-ray1.751/2189-545[»]
1GTLX-ray2.801/2189-545[»]
1T1EX-ray1.18A1-552[»]
1T1GX-ray1.18A189-552[»]
1T1IX-ray1.28A189-552[»]
ProteinModelPortaliQ8RR56.
SMRiQ8RR56. Positions 12-545.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8RR56.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
IPR030400. Sedolisin_dom.
[Graphical view]
PfamiPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTiSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS51695. SEDOLISIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8RR56-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDMEKPWKE EEKREVLAGH ARRQAPQAVD KGPVTGDQRI SVTVVLRRQR
60 70 80 90 100
GDELEAHVER QAALAPHARV HLEREAFAAS HGASLDDFAE IRKFAEAHGL
110 120 130 140 150
TLDRAHVAAG TAVLSGPVDA VNQAFGVELR HFDHPDGSYR SYVGDVRVPA
160 170 180 190 200
SIAPLIEAVF GLDTRPVARP HFRLRRRAEG EFEARSQSAA PTAYTPLDVA
210 220 230 240 250
QAYQFPEGLD GQGQCIAIIE LGGGYDETSL AQYFASLGVS APQVVSVSVD
260 270 280 290 300
GATNQPTGDP NGPDGEVELD IEVAGALAPG AKIAVYFAPN TDAGFLNAIT
310 320 330 340 350
TAVHDPTHKP SIVSISWGGP EDSWAPASIA AMNRAFLDAA ALGVTVLAAA
360 370 380 390 400
GDSGSTDGEQ DGLYHVDFPA ASPYVLACGG TRLVASAGRI ERETVWNDGP
410 420 430 440 450
DGGSTGGGVS RIFPLPSWQE RANVPPSANP GAGSGRGVPD VAGNADPATG
460 470 480 490 500
YEVVIDGETT VIGGTSAVAP LFAALVARIN QKLGKPVGYL NPTLYQLPPE
510 520 530 540 550
VFHDITEGNN DIANRARIYQ AGPGWDPCTG LGSPIGIRLL QALLPSASQA

QP
Length:552
Mass (Da):57,743
Last modified:June 1, 2003 - v2
Checksum:i7EA9586DD366835C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070740 Genomic DNA. Translation: BAB85637.2.
PIRiJC7833.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070740 Genomic DNA. Translation: BAB85637.2.
PIRiJC7833.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GT9X-ray1.381/2189-545[»]
1GTGX-ray2.301189-545[»]
1GTJX-ray1.751/2189-545[»]
1GTLX-ray2.801/2189-545[»]
1T1EX-ray1.18A1-552[»]
1T1GX-ray1.18A189-552[»]
1T1IX-ray1.28A189-552[»]
ProteinModelPortaliQ8RR56.
SMRiQ8RR56. Positions 12-545.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS53.004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.B48. 275055.

Miscellaneous databases

EvolutionaryTraceiQ8RR56.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
IPR030400. Sedolisin_dom.
[Graphical view]
PfamiPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTiSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMiSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
PROSITEiPS51695. SEDOLISIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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-32Imported.
  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).

Entry informationi

Entry nameiQ8RR56_9BACI
AccessioniPrimary (citable) accession number: Q8RR56
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2003
Last modified: January 7, 2015
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.