ID   A0A1G8LTU8_9FLAO        Unreviewed;       712 AA.
AC   A0A1G8LTU8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=SAMN05421846_11055 {ECO:0000313|EMBL:SDI59142.1};
OS   Chryseobacterium taeanense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=311334 {ECO:0000313|EMBL:SDI59142.1, ECO:0000313|Proteomes:UP000198869};
RN   [1] {ECO:0000313|Proteomes:UP000198869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17071 {ECO:0000313|Proteomes:UP000198869};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FNDW01000010; SDI59142.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8LTU8; -.
DR   STRING; 311334.SAMN05421846_11055; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000198869; 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   InterPro; IPR019500; Pep_S46.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           20..712
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023160160"
SQ   SEQUENCE   712 AA;  80751 MW;  52A58BA03E8F8833 CRC64;
     MTKKILLSVF LLPAVMTFAQ QYGGMWIPTE LNEKEMKDLG MKISAKDIFN PQKASIKDAV
     VQFNGGCTAE IISPKGLLLT NHHCGYGQIQ AHSTVQNDLL SNGFWAKNTE GELPNPGVTV
     DFIVDIKEVT NQILQGTDNL TEPKLSKQIA KNIEIYKNSQ KTEPYQSISV KSMYYGNKFY
     AYTIETYKDI RLVGAPPQSI GKFGSDTDNW VWPRHTGDFS MFRIYADKNN KPAEYSKDNV
     PYVPKHYLPV SIKDKNENDF TFVFGFPGRT TEYLPAIAVE KIMKEIDPAR IAVRDVALKT
     LDEKMRTDDA TRIQYASKYA SVANYWKKWI GEVEGLKKSN AVEKKVMYEG SLVSKNPEIK
     TTLDQLNKLY NDQAPFALNN AYYSETLRNA ETLMLANLYY NYITAVEAGR MDEKNTTSFK
     NRLTSFYKDY NAELDAKVTA KLLALYANKT DAQFLPAGFE KFKNEAQNIQ VIEDASKNSI
     ITGRSEVNGA SLSKDIEKAF SNQDKLIKTL KKDPVFQIYM AMRDTYMTKA DPQFTSLQTK
     IDALQKTYMA QQMATDKDRK FFPDANSTMR VTYGKVKGSS PRDAVSYNYQ THLAGVMEKY
     IPGDYEFDVP KKLIDLYSKK DFGNYKDKTG DVPVGFTATN HTTGGNSGSP ALDAYGNLVG
     LNFDRQWEGT MSDINYDPRF SRNIMVDTKY ILFIIDKFAD SKWLINEMKI VK
//