ID   A0A255Z2G8_9FLAO        Unreviewed;       714 AA.
AC   A0A255Z2G8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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=CHU92_10535 {ECO:0000313|EMBL:OYQ35703.1};
OS   Flavobacterium cyanobacteriorum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2022802 {ECO:0000313|EMBL:OYQ35703.1, ECO:0000313|Proteomes:UP000216605};
RN   [1] {ECO:0000313|EMBL:OYQ35703.1, ECO:0000313|Proteomes:UP000216605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH021 {ECO:0000313|EMBL:OYQ35703.1,
RC   ECO:0000313|Proteomes:UP000216605};
RA   Cai H.;
RT   "Flavobacterium cyanobacteriorum sp. nov., isolated from cyanobacterial
RT   aggregates in a eutrophic lake.";
RL   Submitted (JUL-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:OYQ35703.1}.
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; NOXV01000280; OYQ35703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255Z2G8; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000216605; 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:UP000216605};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   714 AA;  81082 MW;  9780A9C85C5A0C5D CRC64;
     MKKLILFLTM SFMVLPVRAD EGMWFLMFIE RLNHRDMQKM GLQLTPQEIY SINNHSLKDA
     IVQFNGGCTA ELISKDGLVL TNHHCGYDAI AELSTPEANY LKNGFWAKDR RAELKPKDLY
     VRFFVRMDDV SKRILSKVND KMTEAEREKA IQQEIALIEK ENNEGGKYTV SVRSFFQGNE
     YYYFVYQDFK DVRLVGTPPE SIGKFGGDTD NWEWPRHTGD FSMFRIYADA NGNPAEYSPN
     NVPLKPKHYL PVSLKGVKEG DFAMILGYPG RTNRWMPSGG IEQNVKFAYP AWVESSKLGM
     DKMKVHMDKS DQVRLNYASQ YASVANYWKN RQGMIDALTK HKTAATKAKS EAEFNKWGNK
     PENKERYGNV IATLNNYYSK TNEKARHDNY LVGMLRTSTF AALPYSLGRG LEAYAGAGAA
     ERANMRQELE EAINESYKTI YEPLEKDVLA AQLNLYATKS AGYDIAPLVA KIAKENNNDF
     TSYVNNSFAN SIFASKQKLT EFLNNPNADV VKNDPLYQLS TDLLTKYRAK SEEQAKLDAD
     YSKAFRLLVE GMRKANPNAK YYPDANSTLR LTYGKVRPLP ADKRNDAKVN YYTTLAGTVK
     KYKPNDEEFD LPKKLIELND KKDFGQYADK AGYMPVNFLT DNDITGGNSG SPVLNGKGEL
     IGLAFDGNIE AMAGDVIFDK ELQRTINVDI RYVLWVIDKF SGAKHIVDEM TIIR
//