ID   R6QVZ1_9BACT            Unreviewed;       713 AA.
AC   R6QVZ1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=BN637_01857 {ECO:0000313|EMBL:CDC26102.1};
OS   Prevotella sp. CAG:386.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262925 {ECO:0000313|EMBL:CDC26102.1, ECO:0000313|Proteomes:UP000018046};
RN   [1] {ECO:0000313|EMBL:CDC26102.1, ECO:0000313|Proteomes:UP000018046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:386 {ECO:0000313|Proteomes:UP000018046};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDC26102.1}.
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; CBEZ010000131; CDC26102.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6QVZ1; -.
DR   STRING; 1262925.BN637_01857; -.
DR   Proteomes; UP000018046; 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:UP000018046};
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..713
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023070371"
SQ   SEQUENCE   713 AA;  81766 MW;  4BFC680AD381E68A CRC64;
     MKKKATVLIA SIMAFCGINT AHADEGMWTI YNLPNAVYEM MQREGFSMTY NQLYNGEDAL
     KNAVVNFSGY CSGVVVSPDG LVFTNHHCGF EAIRSHSTVE HDYMLNGFFA KSFEEELPNE
     DMFVSFMIDQ KDVTDKLMSL GYEKLDNKKR SELTDSLENA MTQEVKKNDS TLHVSIKPFY
     EGNKWYATTY RDFTDLRLVF TVPKSMGKFG GDTDNWMWPR QTCDFSVFRI YADPKTNGPA
     AYSKDNVPYK PKRWAQVSLQ GYKDGDYAMT MGYPGTTERY LSSYGIQTMR DAENAPRAQV
     RGVKQEVMQK HMRADEAVRI KYDSKYASSS NYWKNALGMN KCIDSIGIIN LKREYEARLR
     TWQDTAKAAN DLAHKVDFDK LAQLYKQSAD VKYAWTNFAE SFTRRSNVEF STRALKLQSN
     MEVKGPEKNK KKQYHEFDDN SDEWDMALDK EVLATLLKNY KEHVDTKWLP KFYATIDTQF
     SGDYTKYVDY LWKKSLLMKK GAKLYFNKKG FEKDPGVSYG MDLNDIYADF VEKMGAVSDS
     IAEQEKYLCA AKLRMEEDLP HYSDANFTMR LSYGQVGGFD LGGKPSGYYT TAESIVEKMK
     QGDKVIDYYA EPIMHELLSE KDFGKYQDKE TGKMQLCFLT NNDITGGNSG SPMFNGKGEL
     IGLAFDGNWD SLSSDINFDK RLARCIGVDI RYVLYLMDKW GHADRLLKEI NAK
//