ID A0A1H4BYY8_9BACT Unreviewed; 659 AA.
AC A0A1H4BYY8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=SAMN05444145_10499 {ECO:0000313|EMBL:SEA53283.1};
OS Alistipes timonensis JC136.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=1033731 {ECO:0000313|EMBL:SEA53283.1, ECO:0000313|Proteomes:UP000183253};
RN [1] {ECO:0000313|EMBL:SEA53283.1, ECO:0000313|Proteomes:UP000183253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25383 {ECO:0000313|EMBL:SEA53283.1,
RC ECO:0000313|Proteomes:UP000183253};
RA de Groot N.N.;
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; FNRI01000004; SEA53283.1; -; Genomic_DNA.
DR RefSeq; WP_010262147.1; NZ_FNRI01000004.1.
DR AlphaFoldDB; A0A1H4BYY8; -.
DR STRING; 1033731.SAMN05444145_10499; -.
DR GeneID; 78309925; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000183253; 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; 2.
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:UP000183253};
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..659
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023151146"
SQ SEQUENCE 659 AA; 74160 MW; 8790E4F892B094AE CRC64;
MKRTLLTLLT ALFILPALAD EGMWLPSLIS SRIDDMRAKG FRLTAEDIYS VNQASMKDAV
VLFNGGCTGE LISPEGLLLT NHHCGYGAIQ RHSTVEHDYL TDGFWAMSRA EELPNEKLWV
RFLVRMEEVT DRIAAGETAD EIVKKAEAEG PGYKAAVEQM YYGNQQFLFV YEQFDDVRLV
AAPPSSIGKF GGDTDNWIWP RHTGDFSMFR VYASKDNKPA AYSPQNVPYR PKKHFAISTK
GVKEGDFTMI YGFPGNTQEY ILSDAVAYIA ERSDPAKIAI RTGRLDIISK AQESDPALRI
FYAARHASIA NAWKKWQGEV LGIKRRGTVA SKRAYEEAFD AWAQDKLRYR NVVAQLKAEY
ARIADPYFAR EITLETLGAL PIKYSAKERA EAVFAHRKAT ERALYSLQFG EYARRCPAQF
QIPEFLDGVA RYGSPEAFAE EIFTQVWNGS DTTATTALRS GTKRMLDHIT WLTGTKSLRN
LNSKRLNELY TTYIKGLREW DAERAFYPDA NLTLRVAYGT VAGYEYADGE YHKPQTTLDG
IIAKDNPEIY DYDIPQTLRD RYASKEYGRW AATIGGHKTV PVCFLATNHT TGGNSGSPVL
NASGELIGIN FDRTWRSTMS DVAFDPSICR NIAVDIRYVL FVVDRIGGAG YLLKEMKLK
//
