Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q59536 (PTRB_MORLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protease 2

EC=3.4.21.83
Alternative name(s):
Oligopeptidase B
Protease II
Gene names
Name:ptrB
OrganismMoraxella lacunata
Taxonomic identifier477 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeMoraxella

Protein attributes

Sequence length690 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues.

Catalytic activity

Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in oligopeptides, even when P1' residue is proline.

Sequence similarities

Belongs to the peptidase S9A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 690690Protease 2
PRO_0000122405

Sites

Active site5341Charge relay system By similarity
Active site6191Charge relay system By similarity
Active site6541Charge relay system By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59536 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5F2B7065EF44B4B8

FASTA69079,507
        10         20         30         40         50         60 
MKLPIAKRIP HPHELHGDVR EDDYYWLKDR DNTEVIQYLE EENRYYHEIM RPLQEQTEQI 

        70         80         90        100        110        120 
YESMVDRVPD SEMKVPVQHG QFFYYSRLDK NKQYPIYARK QAASRALLQD ATEEVVLDLN 

       130        140        150        160        170        180 
ELAEEDDYLS VTVQRMTTDH SRLAYLENRD GTDRYTIYIK DLNTGELLSD RVPNVYIYGS 

       190        200        210        220        230        240 
MEWCRCGDYI FYTTVDEHQR PCQLWRHRLG SDVESDELIF EEKDDTFTLF ISKSQSGKFI 

       250        260        270        280        290        300 
FVYSSSKTTS EIHMIDTDSP LSPLQLVDER RDGILYDVEH WEDDLLILTN EGALNFQLLR 

       310        320        330        340        350        360 
CPLNDLSSKV NVVEYNEERY LQEMYPFRDK LLIAGRENGL TQIWVVHDGE LQQISWDEPL 

       370        380        390        400        410        420 
YTVAVLSEQS YDTNEVLIQY ESLLTPKTTF GLNLQTGEKQ CLQVAPVSGE YDRSQFRQEQ 

       430        440        450        460        470        480 
LWATGRSGVK VPMTAVYLEG ALDNGPAPLI LYGYGSYGSN SDPRFDPYRL PLLEKGIVFV 

       490        500        510        520        530        540 
TAQVRGGSEM GRGWYEDGKM QNKRNTFTDF IAAAKHLIDQ NYTSPTKMAA RGGSAGGLLV 

       550        560        570        580        590        600 
GAVANMAGEL FKVIVPAVPF VDVVTTMLDT SIPLTTLEWD EWGDPRKQED YFYMKSYSPY 

       610        620        630        640        650        660 
DNVEAKDYPH MYITTGINDP RVGYFEPAKW VARLRAVKTD NNTLVMKTNM GAGHFGKSGR 

       670        680        690 
FNHLKEAAES YAFILDKLGV EAEEKVLNHR 

« Hide

References

[1]"Protease II from Moraxella lacunata: cloning, sequencing, and expression of the enzyme gene, and crystallization of the expressed enzyme."
Yoshimoto T., Tabira J., Kabashima T., Inoue S., Ito K.
J. Biochem. 117:654-660(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38405 Genomic DNA. Translation: BAA07460.1.
PIRJC4185.

3D structure databases

ProteinModelPortalQ59536.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS09.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.130.10.120. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR023302. Pept_S9A_N.
IPR001375. Peptidase_S9.
IPR002470. Peptidase_S9A.
[Graphical view]
PANTHERPTHR11757. PTHR11757. 1 hit.
PfamPF00326. Peptidase_S9. 1 hit.
PF02897. Peptidase_S9_N. 1 hit.
[Graphical view]
PRINTSPR00862. PROLIGOPTASE.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTRB_MORLA
AccessionPrimary (citable) accession number: Q59536
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries