ID   A0A1W2DDX0_9SPHI        Unreviewed;       726 AA.
AC   A0A1W2DDX0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=SAMN04488101_106248 {ECO:0000313|EMBL:SMC95705.1};
OS   Pedobacter nyackensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=475255 {ECO:0000313|EMBL:SMC95705.1, ECO:0000313|Proteomes:UP000192678};
RN   [1] {ECO:0000313|EMBL:SMC95705.1, ECO:0000313|Proteomes:UP000192678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19625 {ECO:0000313|EMBL:SMC95705.1,
RC   ECO:0000313|Proteomes:UP000192678};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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}.
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DR   EMBL; FWYB01000006; SMC95705.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2DDX0; -.
DR   STRING; 475255.SAMN04488101_106248; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000192678; 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:UP000192678};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   726 AA;  81610 MW;  BEC07EC479C3E468 CRC64;
     MNKKTLITSL LTCSLLTVGI LQSGYKPWEE GMFPLSEIHK LDLKKAGLKI SQNEIYNPNG
     TSLVDALVNV GGCTGSFISN QGLIITNHHC AFSAVQLAST PEHDYLTNGF VAANREQEIE
     AKGLTCRITD SYEDVSDRVL GAVAQVTDPT SRLKLINDAM KNIVVEAEKK DPTIQAEVSE
     MFIGKTYVLF RYKTIQDVRL VYVPNRQIGE FGGETDNWVW PRHTGDFSFM RAYVAADGSP
     AKYSKKNVPY TPKKFLKVNA NGTNEEDFVF ILGYPGKTFR HRPAQFIEYQ QQFVLPYVSE
     LYDFQNTTME NAGKKDKTTE IKLATRIKRN ANTLKNYRGK LQGLKGIDLI SQKKNEDAAL
     AKFINSNIDV KARYGSLMSD IDNLYKLING DAKRDLWLAQ IYNSTSVLGV SRNINAFKTA
     LDAQPENQKE AFFNQNKPRL KSFLAGIYEA YDIDADRKIF KRMLSDASAF SADQSVNAVD
     KLTNKSAYSE KVIEDYVTNT FKNSKLTDTS YVYNTLLKST KSFSSYSDNL LSFEKDIAAQ
     IAALKPEKDR REGVLNKLMG DYVNVKEKFL KKDFVPDANS TLRLTYGYVR GYWPADASYM
     RPYTTIKGIL EKGTSGKPDF SYPAQIRALW EAKDFGPFAK KDLKDVPVAF LYNMDTTGGN
     SGSPIMNAQG ELIGVNFDRA YGATINDYAW NESYSRSIGV DIRYVLWVAS KIDKANFLLK
     EMGVKI
//