ID G8UKD3_TANFA Unreviewed; 716 AA.
AC G8UKD3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=BFO_0377 {ECO:0000313|EMBL:AEW21451.1};
OS Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS 5666 / FDC 338) (Bacteroides forsythus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW21451.1, ECO:0000313|Proteomes:UP000005436};
RN [1] {ECO:0000313|Proteomes:UP000005436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC {ECO:0000313|Proteomes:UP000005436};
RA Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA Shetty J., Torralba M., Gill S., Nelson K.;
RT "Complete sequence of Tannerella forsythia ATCC 43037.";
RL Submitted (DEC-2011) 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; CP003191; AEW21451.1; -; Genomic_DNA.
DR RefSeq; WP_014223835.1; NC_016610.1.
DR AlphaFoldDB; G8UKD3; -.
DR SMR; G8UKD3; -.
DR STRING; 203275.BFO_0377; -.
DR MEROPS; S46.001; -.
DR GeneID; 34757763; -.
DR KEGG; tfo:BFO_0377; -.
DR PATRIC; fig|203275.8.peg.334; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_013776_0_0_10; -.
DR Proteomes; UP000005436; Chromosome.
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:UP000005436};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 24..716
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023160276"
SQ SEQUENCE 716 AA; 81457 MW; 9CE2FD3D9A99892D CRC64;
MKRTNKIWVA VALLLTTVGQ TFADEGMWVL KELNRQNLAR MQELGLTIPV EMLYSETNPC
IANAVVIFGG GCTGITVSDQ GLVLTNHHCG YGAIQRLSSV EHDYLKNGFV SQNMSEELPV
EGLRIQYLKE TVDVSERILS QIEGVDDEFK RITKADSIGQ AICDSIGKDN SSLSARVIPF
YSRNKYYLVV YNVFRDVRLV FAPPSSLGKF GGDTDNWMWP RHTCDFSAFR VYADANNRPA
EYSASNRPYQ PEYVAEISLR GYDEKDYAMT IGFPGRTNRY LCSWGVQQRI EDSNKPRIEV
RGIKQDLWKK AMLASDAVRI KYASKYAGSS NYWKNSIGMN RGLARLNVID RKKTEEAAFT
AWVNQMPARK TQYGDVLHLL EKGYTSSAEY RKYATYLMEA FAGGTEIIRL ARIIRSVDVK
NSTPEEIDER IDGDLRAFYK DYEPALDRHV LAAMMKIVKE RVPASFLPDI YGKVDKKYKG
DYEKYAADVF GNTVLTSFEK VSALLKNPKQ YEKVMKKDPA AVLSLSATLA VYDIQQQVAA
WDNDIDKGER LYWAGLKEMY PDRSFYSDAN FTMRMSYGTI GGYRPYDAAW YNFHTTDRGI
LEKEDPMSSE FRVQPEILNL VKARDFGPYA NEQGELQLCF LSNNDITGGN SGSPVFDKHG
RVIGLAFDGN WEAMSGDIAF EPDLQRTISV DIRYVLWMIE KWGKCTRLIE ELKRVK
//
