ID   A0A1I2LT52_9BACT        Unreviewed;       703 AA.
AC   A0A1I2LT52;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=SAMN05216383_10197 {ECO:0000313|EMBL:SFF82562.1};
OS   Prevotella sp. KH2C16.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1855325 {ECO:0000313|EMBL:SFF82562.1, ECO:0000313|Proteomes:UP000198560};
RN   [1] {ECO:0000313|Proteomes:UP000198560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2C16 {ECO:0000313|Proteomes:UP000198560};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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   ---------------------------------------------------------------------------
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; FOOW01000001; SFF82562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2LT52; -.
DR   STRING; 1855325.SAMN05216383_10197; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000198560; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198560};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           20..703
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023150024"
SQ   SEQUENCE   703 AA;  80513 MW;  71FD46DF3EB9F8FD CRC64;
     MKKSTLILAG LLAVNVANAD EGMWTLYNLP QAVYQTMQTE GFQLPYSALY SGENAIKNAV
     VNFSGYCSGV VVSPDGLVFT NHHCGFEAIR SHSTVEHDYM LNGFYAKSYE EELPNENMFV
     SFMVAQKDIT DEVLAGGFYY KTPEAQEEFI DSLTNAYTRE VKRQDSTLHV DIDPFYEGNK
     FYATTYQDFT DLRLVFTVPK SMGKFGGETD NWMWPRQTCD FSVFRIYADP KTNGPAKYSK
     DNVPYHPKSW APVSLQGYKE GDFAMTVGYP GSTSRYLSSY GIRERRDAIN APRAQVRGVK
     QEIMLKHMQA DEAVRIKYDS KYAQSSNYWK NSIGMNKCID SIGLIGQKRQ FEEQIARWQD
     STKYLQGKLD FKKMEELYNK CFEAGKTMTY FTETFRGTSE FSNRAMRLNY IEVQGPQDKP
     KKQYVEFKDN SDAWDAALDK EVFAALLKNY RDKVQAKYLP AFYKTIDTKF GGNYAAYVDY
     LYEKSFLMRS GERIYVNKKG YQKDPGVQYS LDLLEVIGDI RNDMASVIDE IDEQERYLCD
     AKIRMEQDKP HYSDANFTMR LSYGQVGGFE LSGKPSGYYT TAESIVEKMN HGDDNFEYQA
     EPVMKELMSA KDFGRYQDKT SGKMQLCFLT NNDITGGNSG SPMFDGKGRL IGLAFDGNWD
     SLSSDINFDA RLARCIGVDI RYVLYLMDKW GHADRLLREI NPQ
//