ID   F3PPW6_9BACE            Unreviewed;       721 AA.
AC   F3PPW6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=HMPREF9446_00758 {ECO:0000313|EMBL:EGF59008.1};
OS   Bacteroides fluxus YIT 12057.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF59008.1, ECO:0000313|Proteomes:UP000003416};
RN   [1] {ECO:0000313|EMBL:EGF59008.1, ECO:0000313|Proteomes:UP000003416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF59008.1,
RC   ECO:0000313|Proteomes:UP000003416};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) 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:EGF59008.1}.
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DR   EMBL; AFBN01000013; EGF59008.1; -; Genomic_DNA.
DR   RefSeq; WP_009124015.1; NZ_GL882614.1.
DR   AlphaFoldDB; F3PPW6; -.
DR   STRING; 763034.HMPREF9446_00758; -.
DR   MEROPS; S46.002; -.
DR   eggNOG; COG3591; Bacteria.
DR   HOGENOM; CLU_013776_0_0_10; -.
DR   Proteomes; UP000003416; 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:UP000003416};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           24..721
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023153955"
SQ   SEQUENCE   721 AA;  80833 MW;  031D4511D2A62A42 CRC64;
     MNLTFKKCLI AAAAALTVCS ARADEGMWLL QLMKQQNSID MMKKQGLKLE ADDLYNPNGV
     SLKDAVGIFG GGCTGEIISP EGLILTNHHC GYGAIQQHSS VEHDYLTDGF WAMNRSEELP
     TPGLKFRFVH RIVDITDLVN GKIKAGETDE VNAMGYPFLS KLAKEELEKS DLKGKPGIEV
     RALPFYAGNK FYLFYYKVYN DVRMVAAPPS SVGKFGGETD NWMWPRHTGD FSMFRIYADA
     NGEPAEYSKD NVPLKTPKYL PISIKGLNEG DYAMIMGFPG STERYLTQSE VKQRMNAVNQ
     AMIDMRGVRL EVLRKYMDAS DKTRIQYASK FAGSSNYWKN SIGMNKAIID NDVLGTKAEI
     EKKYAEFAKG KPEYEGVVEK IDAIIEKSTP TLRQLYYTNE ALRGAIEFGS TYLVMDNIKK
     ALEEKNDSLL QASKKQLESA YDGIHNKDYD HEVDRAVAKA ILPALAKALN ADELPTFYQT
     INGEFKGDYN AYVDNMYDNS ILSNRKNLDK FLAKPSVKAI EKDPATAYSR SKNEKLQELG
     KQYGELENGM ELLHKAYIRG LGEMKQPVPS YPDANFTMRL TYGNVKSYSP RDAVHYNYYT
     TTDGILEKEN PENREFVVPA KLKELIQKKD FGRYAMADGT MPVCFLTTND ITGGNSGSPV
     INGEGQLIGT AFDGNWESLS GDINFNNNLQ RCIALDIRYV LFILDKLGNC GHLIKEMNIV
     E
//