ID   A0A136N5V6_9BACT        Unreviewed;       713 AA.
AC   A0A136N5V6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, 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=UZ11_BCD004001916 {ECO:0000313|EMBL:KXK41561.1};
OS   Bacteroidetes bacterium OLB11.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617422 {ECO:0000313|EMBL:KXK41561.1, ECO:0000313|Proteomes:UP000070496};
RN   [1] {ECO:0000313|EMBL:KXK41561.1, ECO:0000313|Proteomes:UP000070496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB11 {ECO:0000313|EMBL:KXK41561.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK41561.1}.
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DR   EMBL; LNFQ01000063; KXK41561.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136N5V6; -.
DR   STRING; 1617422.UZ11_BCD004001916; -.
DR   PATRIC; fig|1617422.3.peg.2084; -.
DR   Proteomes; UP000070496; 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; 2.
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   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   713 AA;  81709 MW;  0CD4C057758567AE CRC64;
     MKSKLLFVLF FLYTFSISAK EGMWLPFLLE KLNEKEMKAM GMKISARDIY DINQGSLKDA
     VVLFGGGCTG EVISDKGLVL TNHHCGYGTV QGLSSLENNY LTNGFWAKNQ QEELPCPGLS
     VTFIVNIIDV TADVLEGTSK INNLDERAKA IAKNIEAIEK EYQKNTGYTS QIKSFFYENE
     YYLFLLEKFN DVRLVGFPPN GIGKFGGDTD NWAWPRHTGD FGLFRIYANQ SNKPANYSKE
     NIPYIPKKSF KINIKGLKEN DFTMVYGFPG RTNEYLTSDG VAETMSILDP ARIKLREARL
     NIMEESMKSS EAIFIQYASK QAGIANYYKK WKGELFGLEV NNAIEKKKIE EKQFQQWVLS
     DNQRKEKYQH LLSDISTIYK QQQNQILLNE YINESIWASE LLRKGSILSR MLTAVDTVKH
     QDSLKKYLNE LQFFQKSVHL ETDYKIAKRL FEYFNQDIFN QSILDKNDSH YISDVNLQSI
     YKTSFVSSTE KLEKLIQVQN KSDFKTLILQ DNAYQTFHFF DSVQKANLVI LKQNTIRLNT
     LYATYINGLK EFHVNKKFYP DANSTLRVTY GKVEGVAASD GIKYTYYTTL DGAVRKANPQ
     TEEFNMPAKL MNLYQQKDYG NYSIIDERGN KTVPIAFLAS NHTTGGNSGS PVINANGELI
     GTNFDRIWEG TMSDILFDPT LCRNISLDIR YTLFIIEKFG GAKWIIDELK IVK
//