ID   A0A1I2JCX7_9BACT        Unreviewed;       954 AA.
AC   A0A1I2JCX7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dipeptidyl aminopeptidase/acylaminoacyl peptidase {ECO:0000313|EMBL:SFF51027.1};
GN   ORFNames=SAMN04488541_104422 {ECO:0000313|EMBL:SFF51027.1};
OS   Thermoflexibacter ruber.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Thermoflexibacteraceae;
OC   Thermoflexibacter.
OX   NCBI_TaxID=1003 {ECO:0000313|EMBL:SFF51027.1, ECO:0000313|Proteomes:UP000199513};
RN   [1] {ECO:0000313|EMBL:SFF51027.1, ECO:0000313|Proteomes:UP000199513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GEY, DSM 9560 {ECO:0000313|Proteomes:UP000199513};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FONY01000044; SFF51027.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2JCX7; -.
DR   STRING; 1003.SAMN04488541_104422; -.
DR   OrthoDB; 9812921at2; -.
DR   Proteomes; UP000199513; 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:SFF51027.1};
KW   Hydrolase {ECO:0000313|EMBL:SFF51027.1};
KW   Protease {ECO:0000313|EMBL:SFF51027.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199513};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..954
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011492718"
FT   DOMAIN          754..924
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          169..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   954 AA;  110136 MW;  E598879E3DF736D6 CRC64;
     MKKLLFILLL LYCFAASAQQ KGGKQTALVS TKKPLTHSVY DSWKEIGFRA VSNDGSWAVY
     TVNPQEGDGK VIFYNLKTNQ IDSVQRASQV EISQDNQFVV FKIAPPLKIM KDLRRQKKKK
     EDLPRDTLGI YNLQTKQLAK VANLKSFKLP EKAGAWLAYQ IEQIEKKETP KKDTAKEVKK
     EEAKKPAKPK KKESEENGYR LVMRKLANAK ETTFDFVKEY KFDKFGKNLI FSTTGNDSTL
     LAGVYVYDLQ SEKLKPLFRA KKGNFKNLAF DESGSQVAFV ADLDTTKTQV RYFKLYHWKN
     GQDSALAIAD TTNITKGLLV SEHYVPNFSQ NGAKLFFGMA NKPVVQDTTL LPEEIVNLDI
     WHWQDDYIQP QQGRRLEQDK KRSYLSVYHV DSKRIVQLAT NEVPSISLAN EGNANLALAS
     SDVPYRRLTN WDISGFEDLY LLDLQTGNKK LIQQKIKGDA AISPQGNYVY WFSLPDTAWF
     TYSVKSGQIF KLNQGLKEKF ADEEDDHPDY PLEYGFAGWT ENDQTFLVYD RYDIWAFDPE
     NRKAPVNLTQ TGRKEKLVFR NIRLDQEEKF FKADQTLLLS VFDETTKQSG YYSLNLKDNS
     KQKLLMDNYR FSTFQTRKAK DASVLLFTRE SFKDYPDLYA TDLTFKNIKK ISEANPQQKD
     YAWGSVEMYS WLSLDGIPLQ GLLYKPENFD PKKQYPMMVY YYEKNSDNIH NHIVPAPIRS
     AINYTYFVSN GYLVFVPDVV YRIGYPGESA YNCIMPAVTS LIEKGFVNKE RIGIQGHSWG
     GYQNAYLITK TNLFRAAEAG APVSNMVSAY GGIRWESGYS RMFQYEKSQS RIGGTLWEKP
     LRFLENSPIF FADKVNTPLL MMHNDEDGAV PWYQGIEYFM ALRRLGKPVW MLNYNKEAHG
     LTQRQNRKDF AIRMYQFFDY YLKDAPMPEW MKKGVPMLEK GVNKGLTLMN EEKE
//