ID   Q8D097_YERPE            Unreviewed;       683 AA.
AC   Q8D097;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   SubName: Full=Protease II {ECO:0000313|EMBL:AAM86083.1};
GN   Name=ptrB {ECO:0000313|EMBL:AAM86083.1};
GN   OrderedLocusNames=y2527 {ECO:0000313|EMBL:AAM86083.1};
OS   Yersinia pestis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632 {ECO:0000313|EMBL:AAM86083.1, ECO:0000313|Proteomes:UP000002490};
RN   [1] {ECO:0000313|EMBL:AAM86083.1, ECO:0000313|Proteomes:UP000002490}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis
RC   {ECO:0000313|Proteomes:UP000002490};
RX   PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G.III., Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plana G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
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DR   EMBL; AE009952; AAM86083.1; -; Genomic_DNA.
DR   RefSeq; WP_002231190.1; NZ_VEZW01000009.1.
DR   AlphaFoldDB; Q8D097; -.
DR   IntAct; Q8D097; 4.
DR   ESTHER; yerpe-PTRB; S9N_PREPL_Peptidase_S9.
DR   MEROPS; S09.010; -.
DR   DNASU; 1147474; -.
DR   KEGG; ypk:y2527; -.
DR   PATRIC; fig|632.152.peg.3055; -.
DR   HOGENOM; CLU_011290_0_1_6; -.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR   PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AAM86083.1};
KW   Protease {ECO:0000313|EMBL:AAM86083.1}.
FT   DOMAIN          5..411
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          470..681
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   683 AA;  78516 MW;  9F6835015240636C CRC64;
     MMTPPKADKR PYPMTRHGDT RVDDYYWLRD DERTDADVLN YLQSENAFTA AVLKPQQQLR
     ETLYQEMVGR IPPQEESVPY VRNGYRYQTR FEPGNEYAIY VRQPVSTDSD WETLLDGNQR
     AEGHEFYTLG GLDVSPDNQL LAVAEDYLSR RQYDIRIKNL SSGGWHDEVI SNTSGGFEWA
     NDSKTLYYVR KHEKTLLPYQ VYRHVVGTDP EQDKLIYQES DDTFYVSLEK TTSERFILIH
     LSSTTTSEIL LLDADLPEPV PQVFAPRRKD HEYGVDHYKQ HFYIRSNKEG KNFGLYKIED
     SQGCSDFADE SQWALLIAPR TDVMLEGFSL FRDWLVVEER SEGLTHLRQI HWSTGEEKSI
     TFDDPTYVTW LAYNPEPETA LLRYGYSSMT TPSSMFEINM DSGERQLLKQ QEVKDFTPEK
     YRSERIWVTA SDGVKIPVSL VYHRDYFVSG SNPLLVYAYG SYGSSMDPVF SSSRLSLLDR
     GFVFALAHIR GGGELGQQWY EDGKLLNKLN TFSDFTDVTK ALVNEGYGDA QRVFAMGGSA
     GGLLMGVIVN QAPELYKAVV AQVPFVDVVT TMLDESIPLT TGEYDEWGNP NDKVYYDYIK
     QYSPYDQVKA QDYPHMLVTT GLHDSQVQYW EPAKWVAKLR EMKTDDHQLL LYTDMDSGHG
     GKSGRFKAYE DIALEYAFIL SLI
//