ID   A0A1Z5SHH4_9BACT        Unreviewed;       725 AA.
AC   A0A1Z5SHH4;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=CAP35_00525 {ECO:0000313|EMBL:OSZ81787.1};
OS   Chitinophagaceae bacterium IBVUCB1.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae.
OX   NCBI_TaxID=1985173 {ECO:0000313|EMBL:OSZ81787.1, ECO:0000313|Proteomes:UP000194327};
RN   [1] {ECO:0000313|EMBL:OSZ81787.1, ECO:0000313|Proteomes:UP000194327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBVUCB1 {ECO:0000313|EMBL:OSZ81787.1,
RC   ECO:0000313|Proteomes:UP000194327};
RA   Orr R.J.;
RT   "Draft genome sequences of novel bacteria, isolated from environmental
RT   samples.";
RL   Submitted (MAY-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}.
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:OSZ81787.1}.
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DR   EMBL; NFUW01000001; OSZ81787.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5SHH4; -.
DR   STRING; 1985173.CAP35_00525; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000194327; 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:UP000194327};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   725 AA;  81296 MW;  2EC36296E05B913F CRC64;
     MLKQCLFSPT SLKTAILAAL VGYCMPAMGK EGMWLPPTLK NRENDMKKMG LQIPVSQLYN
     EDGTGLNNAV VLFGKGCTGE VISSRGLVLT NHHCGYGTVQ GLSSKENDYF AAGFWAKKDE
     EELPCPGLTV TFVRKMENVT DKIVTGLADT MNEATRQQLV EVRIKNLEKG YKTATGMDAM
     IKPYFNGNQY WVILTETFND IRLVGFPPNG IGSFGGDTDN WMWPRHTGDF SMFRIYAGKG
     NKPAAYAKDN KPYQTKQFFT INPNGYREGD FTMVYGFPGT TMEYISSYQL NQVYSILDPI
     RIESRTQRLN AWTKHMQASR DVFLKYTSKR AGIANGWKKW QGEVRGLRIN NVVGKKQDYE
     AYFQGLASQD QNLPYADDVL ANMAAKSNAV NDALKADEYI KEAVLGIELI QNAAVLDKML
     QVLRAKNIAN KNDSLMKLAK GLEGMYKNYD VATDKEVFEV LMPLFMQKNT GYIPTAFSNQ
     LRERGNNYNA WSSYAFSSIA ANQEKLKSFA ETATAADSNR LIGDPAWQLY NGISKMRQEK
     ITPYVSRYYS DMAYLNRLYM NAQMSLDKQK SFYPDANLTL RLTYGKVAGI DPDGAAGYSY
     QTNLNEAVKK HNPEVEEFNM PAKLMALHNE RDFGKWSVGG SVPIAFIASN HTSGGNSGSP
     VLNAKGELIG TNFDRIWEGT MSDLYFDEKL CRNISVDIRY TLFIIEKFGG AGRLLKEMDI
     VKACD
//