ID   A0A1M5XM57_9BACT        Unreviewed;       976 AA.
AC   A0A1M5XM57;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dipeptidyl aminopeptidase/acylaminoacyl peptidase {ECO:0000313|EMBL:SHI00927.1};
GN   ORFNames=SAMN04488109_6737 {ECO:0000313|EMBL:SHI00927.1};
OS   Chryseolinea serpens.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC   Chryseolinea.
OX   NCBI_TaxID=947013 {ECO:0000313|EMBL:SHI00927.1, ECO:0000313|Proteomes:UP000184212};
RN   [1] {ECO:0000313|EMBL:SHI00927.1, ECO:0000313|Proteomes:UP000184212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24574 {ECO:0000313|EMBL:SHI00927.1,
RC   ECO:0000313|Proteomes:UP000184212};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQWQ01000006; SHI00927.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5XM57; -.
DR   STRING; 947013.SAMN04488109_6737; -.
DR   Proteomes; UP000184212; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:SHI00927.1};
KW   Hydrolase {ECO:0000313|EMBL:SHI00927.1};
KW   Protease {ECO:0000313|EMBL:SHI00927.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184212}.
FT   DOMAIN          776..950
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          182..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  110444 MW;  E75E2F9ECD5BFBA5 CRC64;
     MDVMHHGAVN THGSGSKKLS HMNKLFTAAL LLVACLPLSA QKKSVAQPKK ALTAEAFAIW
     KEIPYKAISP DGGVVAFTIN PQDGDGKVVF YHLKTNAQDS VRRAAEINLT ADSRYAVFKI
     KPPLQQVKEL RRQKKKKEDL PKDSLGVYSF ASRKTEKIAE VRSYKIPEKV GGWIAYQLEP
     KKDVKPKPED KKPDEKPKTL PDTLKKKEVK PKPVKKNNDT NGYTLKLKRL ADGKEFSFGF
     VKEYALAKYG QGLLLTTTGN DSSMKAGVYW FDLKEEKLTA LLEGKSKQKF KNLSINEDGT
     QVAFVVDLDT TKAPLRYPKL YSWKTGEPKA GILADETSAS LPAKWIVSEH STPYFSKDGT
     KLYLGVNPQP VVQDTTLLPE EIVSVEIWSA RDSVLYTQQN KQLEATRKQA FAAVVHLQDK
     KLVVLANKDI PTIAVADEGN ANIVLATSDI NYRWSDFYDP SGFSDAYVLN LSNGARQPVI
     SKVKGNPNLS AKAKYVYWFN LEDTTWYSYS VATQKTVALT KSLKTSFADE ENDTPDYSPA
     YGILGWTAND AALLVYDRYD IWSLDPENKI APVNITKLGR QQKLVFRYIR LDPEERFIDP
     AKELLLSAFN EDTKQSGYYK LSLKDNKLTK LLMSDHRYAV TTKAKNADKL IFTRENFREF
     PDVWTSDVNL TASSTKKLSD ANPQMKQYKW GTVEIVDWVS LDNVPLKGLL YKPDNFDASK
     KYPMIVYYYE KNSDGIHTYV APEPLRSSVN RSMYVSNDYI IFVPDIVYRI GYPGQSAYNC
     IMPGVTKLLS LGFVDEKNVG LQGHSWGGYQ TAYLVTRTNF FKAAEAGAVV SNMVSAYGGI
     RWETGLSRMF QYEHSQSRLG ATLWEKPLLY VENSPIFFAD KIETPLLLLH NDADGHVPWY
     QGIEMYMALR RLNKPAWMLN YNGEPHWPVK RENRIDFQIR MGQFFDHYLK GAPMPEWMRK
     GIPAVEKGIN KGYSTK
//