ID A0A1F3LVG6_9BACT Unreviewed; 726 AA.
AC A0A1F3LVG6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=A2X18_02100 {ECO:0000313|EMBL:OFY44417.1};
OS Bacteroidetes bacterium GWF2_40_14.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797347 {ECO:0000313|EMBL:OFY44417.1, ECO:0000313|Proteomes:UP000176561};
RN [1] {ECO:0000313|EMBL:OFY44417.1, ECO:0000313|Proteomes:UP000176561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OFY44417.1}.
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DR EMBL; MEOK01000004; OFY44417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3LVG6; -.
DR STRING; 1797347.A2X18_02100; -.
DR Proteomes; UP000176561; 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 Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}.
SQ SEQUENCE 726 AA; 82395 MW; A67A838A947A955B CRC64;
MKKRIITLVL TFFILTPFAI ADEGMWLVNL LDKQLYGQMK SKGLKLKANE IYNEEGGALS
DAIVAIDGGS CSGSIISPEG LMITNHHCAY GDVHSLSTAT KNYLEDGFWA MKRDQEVSIK
GKTVTFLRRV IDITDEVVKV IDSLDKAGPR GLFFMNKVSA VFEKRYEAIP YEKSLESMWR
GSKYYLYFYE TYKDIRLVGA PPVSVGAFGG ETDNWGWPQH KGDFAMYRVY ASKDGKPAEY
SKDNVPLQAK RFLKVSAQGV KKDGFTMVLG YPGRTNRYMS SYELTEKFEI LNPVASGVRR
AKLDVWKKYM DASPAIRLKY SDKYFGVSNY TDYAKWENIC LERYKVVDEL TAVEKQLDEW
IKSDNSRNEK YGNVLANLKK GYEISAGIVK IREYFRESMV RGAELVALGQ RFNALVNTLE
RAKKDSMSIS DKEIDVFVTQ NAMPAFRSID VAADRELFKV MLKYFTTEVP EKYYDKGFAD
LLHSFNGDVV KLADYVYDNS ILTDSTRMVN FFNKKRPVKD ILSDPVTIIV KTTGIRPYNS
TEDAIMKNAN IDLGKERSSF VRALYEMKKD KGVVMYPDAN STMRLTFGEV GPIEPADGIY
YHYQTTTKGL EEKYNPKNYE FNMKPDMRSL LKSGDWGKWG QNGKLYVNFL SDNDITGGNS
GSAVMNGKGE LIGLAFDGNR ESMSGDVYFK EGYCKSVCVD IRYVLWVIDK YAGANHLIDE
MTITTK
//
