ID   A0A2A2EJ51_9BIFI        Unreviewed;       824 AA.
AC   A0A2A2EJ51;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Peptidase S9 {ECO:0000313|EMBL:PAU68955.1};
GN   ORFNames=B1526_0148 {ECO:0000313|EMBL:PAU68955.1};
OS   Bifidobacterium criceti.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1960969 {ECO:0000313|EMBL:PAU68955.1, ECO:0000313|Proteomes:UP000218399};
RN   [1] {ECO:0000313|EMBL:PAU68955.1, ECO:0000313|Proteomes:UP000218399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=71 {ECO:0000313|EMBL:PAU68955.1,
RC   ECO:0000313|Proteomes:UP000218399};
RX   PubMed=28837128; DOI=10.1038/ismej.2017.138;
RA   Milani C., Mangifesta M., Mancabelli L., Lugli G.A., James K., Duranti S.,
RA   Turroni F., Ferrario C., Ossiprandi M.C., van Sinderen D., Ventura M.;
RT   "Unveiling bifidobacterial biogeography across the mammalian branch of the
RT   tree of life.";
RL   ISME J. 11:2834-2847(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAU68955.1}.
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DR   EMBL; MVOH01000002; PAU68955.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2EJ51; -.
DR   Proteomes; UP000218399; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 2.
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;
FT   DOMAIN          30..305
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          579..811
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   824 AA;  92401 MW;  024859DF686A795A CRC64;
     MRAYNRRMTN EHNEQADMRP PHAACIASER RFHDDVFDDP YEWMRDKESP QLQRYVREEN
     DYTAARMAHL EPLRERLFEE FRSHVQETDM SVPTRMDGYW YYARTQEGKQ YAVQCRIPVT
     DEDDWNPPLI DAQQEPGTLD GEQIVLDANI EAQGHEFYRV GGMDISKDGR WMLLGVDTNG
     DERYDFTIRE IATGHELPER FEGIAAACFT PDARYVFYTV LDDAQRPWLI RRHKVGTDVS
     DDVDVYREED ERFWAGIGVS FDERHLVIGT GSKTTSEVLM LPVSDPEGEF TPFIPREEGV
     EYDVSFATFE GADEHGEDVP VAVVYHNATN PNFEIDVIDM RGVEPPFAPY AFGDGQMIAC
     GSPYGCELGD AVVEGAWSMP VGTPFDDPRN PALLRGARGL VIEGIALHRH FVALSYRADG
     LPRLAVMGKA AAAEDFLDGS PWRFEAVTPP ALEGDWKPED VPMPALDGFD GAAGRLYSIG
     TAGNPSYDAP RMRYMFTSYT RPGELHELDT RDGTDVLLKE ATVLGGYDAR EYAERRIWVE
     ARDGERIPVS LVWRRGAACA HMPMFIIGYG AYEISSDPGF SIARLSLLDR GVLYAVPHVR
     GGGEMGRAWY ENGRRMHKKH TFEDFVDVTA ALQDCGLADP ARTVANGGSA GGLLMGAVAN
     MAPERYAGIE ADVPFVDALT TMLDPSLPLT VTEWDEWGDP LHDVQAYRYM RDYSPYENAP
     MPEPAADGAV HAVWRDGEAV EHYPRIFVTT SMNDTRVLVV EPLKWVARLQ AAGLDALIKI
     EVEAGHGGGT GRYKQWRDVC YENAWCLEAM GAEVLIASRH GRWI
//