Reviewed, UniProtKB/Swiss-Prot Q59536 (PTRB_MORLA)

Names and origin

Protein names

Recommended name:
    Protease 2
    EC=3.4.21.83
Alternative name(s):
    Protease II
    Oligopeptidase B

Gene names

Name:

ptrB

Organism

Moraxella lacunata

Taxonomic identifier

477 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Moraxella

Protein attributes

Sequence length	690 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.

Ontologies

Keywords
Molecular function	Hydrolase Protease Serine protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	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	1 – 690	690	Protease 2		PRO_0000122405
Sites
	Active site	534	1	Charge relay system By similarity
	Active site	619	1	Charge relay system By similarity
	Active site	654	1	Charge relay system By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q59536-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5F2B7065EF44B4B8	FASTA	690	79,507
	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

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: 7629037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D38405 Genomic DNA. Translation: BAA07460.1.
PIR	JC4185.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	S09.010.
Enzyme and pathway databases
BRENDA	3.4.21.83. 290675.
Family and domain databases
InterPro	IPR002471. Pept_S9_AS. IPR001375. Peptidase_S9. IPR002470. Peptidase_S9A. IPR004106. Peptidase_S9A_N. [Graphical view]
PANTHER	PTHR11757. Peptidase_S9A. 1 hit.
Pfam	PF00326. Peptidase_S9. 1 hit. PF02897. Peptidase_S9_N. 1 hit. [Graphical view]
PRINTS	PR00862. PROLIGOPTASE.
PROSITE	PS00708. PRO_ENDOPEP_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PTRB_MORLA

Accession

Primary (citable) accession number: Q59536

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 20, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)