ID   PTRB_MORLA              Reviewed;         690 AA.
AC   Q59536;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protease 2;
DE            EC=3.4.21.83;
DE   AltName: Full=Oligopeptidase B;
DE   AltName: Full=Protease II;
GN   Name=ptrB;
OS   Moraxella lacunata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7629037; DOI=10.1093/oxfordjournals.jbchem.a124759;
RA   Yoshimoto T., Tabira J., Kabashima T., Inoue S., Ito K.;
RT   "Protease II from Moraxella lacunata: cloning, sequencing, and expression
RT   of the enzyme gene, and crystallization of the expressed enzyme.";
RL   J. Biochem. 117:654-660(1995).
CC   -!- FUNCTION: Cleaves peptide bonds on the C-terminal side of lysyl and
CC       argininyl residues.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in
CC         oligopeptides, even when P1' residue is proline.; EC=3.4.21.83;
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; D38405; BAA07460.1; -; Genomic_DNA.
DR   PIR; JC4185; JC4185.
DR   AlphaFoldDB; Q59536; -.
DR   SMR; Q59536; -.
DR   ESTHER; morla-ptrb; S9N_PREPL_Peptidase_S9.
DR   MEROPS; S09.010; -.
DR   BRENDA; 3.4.21.83; 9781.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Serine protease.
FT   CHAIN           1..690
FT                   /note="Protease 2"
FT                   /id="PRO_0000122405"
FT   ACT_SITE        534
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        619
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        654
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
SQ   SEQUENCE   690 AA;  79507 MW;  5F2B7065EF44B4B8 CRC64;
     MKLPIAKRIP HPHELHGDVR EDDYYWLKDR DNTEVIQYLE EENRYYHEIM RPLQEQTEQI
     YESMVDRVPD SEMKVPVQHG QFFYYSRLDK NKQYPIYARK QAASRALLQD ATEEVVLDLN
     ELAEEDDYLS VTVQRMTTDH SRLAYLENRD GTDRYTIYIK DLNTGELLSD RVPNVYIYGS
     MEWCRCGDYI FYTTVDEHQR PCQLWRHRLG SDVESDELIF EEKDDTFTLF ISKSQSGKFI
     FVYSSSKTTS EIHMIDTDSP LSPLQLVDER RDGILYDVEH WEDDLLILTN EGALNFQLLR
     CPLNDLSSKV NVVEYNEERY LQEMYPFRDK LLIAGRENGL TQIWVVHDGE LQQISWDEPL
     YTVAVLSEQS YDTNEVLIQY ESLLTPKTTF GLNLQTGEKQ CLQVAPVSGE YDRSQFRQEQ
     LWATGRSGVK VPMTAVYLEG ALDNGPAPLI LYGYGSYGSN SDPRFDPYRL PLLEKGIVFV
     TAQVRGGSEM GRGWYEDGKM QNKRNTFTDF IAAAKHLIDQ NYTSPTKMAA RGGSAGGLLV
     GAVANMAGEL FKVIVPAVPF VDVVTTMLDT SIPLTTLEWD EWGDPRKQED YFYMKSYSPY
     DNVEAKDYPH MYITTGINDP RVGYFEPAKW VARLRAVKTD NNTLVMKTNM GAGHFGKSGR
     FNHLKEAAES YAFILDKLGV EAEEKVLNHR