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Q8RR56 (Q8RR56_9BACI) Unreviewed, UniProtKB/TrEMBL

Last modified October 16, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
Gene names
Name:kscp EMBL BAB85637.2
OrganismBacillus sp. MN-32 EMBL BAB85637.2
Taxonomic identifier198803 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain189 – 552364kumamolisin EMBL BAB85637.2
PRO_5000049828

Regions

Region386 – 3894Sulfate 2 binding PDB 1T1G PDB 1GT9
Region386 – 3894Sulfate 3 binding PDB 1GT9

Sites

Metal binding5041Calcium PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG
Metal binding5051Calcium; via carbonyl oxygen PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG
Metal binding5221Calcium; via carbonyl oxygen PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG
Metal binding5241Calcium; via carbonyl oxygen PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG
Metal binding5261Calcium PDB 1GTJ PDB 1GTL PDB 1T1G PDB 1T1I PDB 1GT9 PDB 1T1E PDB 1GTG
Binding site3871Sulfate 4 (covalent) PDB 1T1I
Binding site4171Sulfate 3 PDB 1GT9

Sequences

Sequence LengthMass (Da)Tools
Q8RR56 [UniParc].

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

FASTA55257,743
        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 

« Hide

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 AND SULFATE.
[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.
PIRJC7833.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ8RR56.
SMRQ8RR56. Positions 12-545.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS53.004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.21.B48. 275055.

Family and domain databases

Gene3D3.40.50.200. 1 hit.
InterProIPR015366. Peptidase_S53_propep.
IPR000209. Peptidase_S8/S53_dom.
IPR009020. Prot_inh_propept.
[Graphical view]
PfamPF00082. Peptidase_S8. 1 hit.
PF09286. Pro-kuma_activ. 1 hit.
[Graphical view]
SMARTSM00944. Pro-kuma_activ. 1 hit.
[Graphical view]
SUPFAMSSF52743. SSF52743. 1 hit.
SSF54897. SSF54897. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ8RR56.

Entry information

Entry nameQ8RR56_9BACI
AccessionPrimary (citable) accession number: Q8RR56
Entry history
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2003
Last modified: October 16, 2013
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)