ID   A0A1Q3T6T0_9SPHI        Unreviewed;       717 AA.
AC   A0A1Q3T6T0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=BGO52_10675 {ECO:0000313|EMBL:OJV97907.1};
OS   Sphingobacteriales bacterium 44-61.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895838 {ECO:0000313|EMBL:OJV97907.1, ECO:0000313|Proteomes:UP000186208};
RN   [1] {ECO:0000313|EMBL:OJV97907.1, ECO:0000313|Proteomes:UP000186208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-61 {ECO:0000313|EMBL:OJV97907.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of
CC       oligopeptides. {ECO:0000256|RuleBase:RU366067}.
CC   -!- SIMILARITY: Belongs to the peptidase S46 family.
CC       {ECO:0000256|ARBA:ARBA00010491, ECO:0000256|RuleBase:RU366067}.
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:OJV97907.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MKTW01000018; OJV97907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3T6T0; -.
DR   STRING; 1895838.BGO52_10675; -.
DR   Proteomes; UP000186208; Unassembled WGS sequence.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070009; F:serine-type aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR019500; Pep_S46.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   PANTHER; PTHR38469; -; 1.
DR   PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR   Pfam; PF10459; Peptidase_S46; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU366067}; Hydrolase {ECO:0000256|RuleBase:RU366067};
KW   Protease {ECO:0000256|RuleBase:RU366067, ECO:0000313|EMBL:OJV97907.1};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   717 AA;  80602 MW;  162046CEB99D9217 CRC64;
     MRKITLTFAF FLLLVVRSFA DEGMWLPLLL GQQVYNDMAR KGLKLTKDQL YNINKASLKD
     AIIIFGGGCT GEIVSSEGLV FTNHHCGYDA IANASTMDHN YLKDGFYAKN KGEEIPTTLS
     VQFLLRIDDV TAEVMDSLKG LSGAERVQRQ TSVLASINKR MSDASQNIET RVSPLFKGNQ
     FMAFVYQRYT DVRLVGAPPE SVGKFGGDTD NWEWPRHTGD FSVFRVYAGK NNQPAKYAAD
     NQPLKPKWFL PVSLKPLKDG DFAMIWGYPG STNRYESSYG IALSIDINNP TLVKLRDVRL
     KYMFEEMKKD PAIKLQLASS YASIANYWKF YDGETKQLIK YDILGQKKKA EAAFAAWAKG
     KPEYQDLLTD WGKAYEAWRP YAEHRQYINE GIFGSPLIAF AATLTSVEAA LVRSGNVSQA
     LAAANEARAA FLKGENKISD QRIVAAVTKM FYDDIPKDQH PIGFYGAIKN SYGALDDENT
     YKKLAADIFS KTIIFDDARW KAFVARPDAN VLQDDPAFAY ASAFLSNYTS KYASYYQQFF
     TKNADYGRIY LKGIMEMDTV KAKKMYPDAT FTMRVSYGAV KPYRPKDAVF YDYVTTSKGI
     LEKYIPGDYE FDLPARQIEL LKNKDFGQYA DPIRKDLVAC FITTNDITGG NSGSPVLNGN
     GELIGLAFDG NYEALSHKLA FDKDLNRTIN VDIRYVLWCI DKLGGATNII KELKLVK
//