ID A0A108TC02_BACSE Unreviewed; 729 AA.
AC A0A108TC02;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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};
DE Flags: Precursor;
GN ORFNames=AA415_00548 {ECO:0000313|EMBL:KWR57092.1};
OS Bacteroides stercoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=46506 {ECO:0000313|EMBL:KWR57092.1, ECO:0000313|Proteomes:UP000056419};
RN [1] {ECO:0000313|EMBL:KWR57092.1, ECO:0000313|Proteomes:UP000056419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR57092.1,
RC ECO:0000313|Proteomes:UP000056419};
RX PubMed=26768901; DOI=10.1186/s12864-016-2377-z;
RA Coyne M.J., Roelofs K.G., Comstock L.E.;
RT "Type VI secretion systems of human gut Bacteroidales segregate into three
RT genetic architectures, two of which are contained on mobile genetic
RT elements.";
RL BMC Genomics 17:58-58(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:KWR57092.1}.
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DR EMBL; LRGC01000002; KWR57092.1; -; Genomic_DNA.
DR RefSeq; WP_060385204.1; NZ_LRGC01000002.1.
DR AlphaFoldDB; A0A108TC02; -.
DR STRING; 46506.AA415_00548; -.
DR PATRIC; fig|46506.5.peg.591; -.
DR Proteomes; UP000056419; 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:UP000056419};
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..729
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023160617"
SQ SEQUENCE 729 AA; 82125 MW; 6C81AECA84A58AC5 CRC64;
MRRIILSLFL TSGILSAHAD EGMWMLTDLK QQNEVAMTEL GLLIPAEQIY NPNGIALKDA
VVHFGGGCTG EVISAEGLVL TNHHCGYGAI QQHSSVEHDY LTDGFWAMSR SEELPCKGLT
VTYIDEIMDV TDYVNDQLQI DSDPNGTNYL SPKYLAMIAD RFLSAQGITL TSGRKAELKA
FYGGNKYYLF LKTTYSDIRM VGAPPSSIGK FGADTDNWMW PRHTGDFSLF RIYAGKDGQP
AAYNPDNVPL QVKKHLTISL AGYREGDFTF VMGFPGRNWR YMISDEVEER MQTTNFMRHH
VRDIRQKALM EQMLKDDAVR IHYASKYASS ANYWKNAIGM NEGLVRLKIL DTKRAQQEQL
LARGRALNDS SYQKAFDQIR GIVKHRRNAL YHQQAIQEAL VTGLDFMRIP STAALVSALK
SKDKARIKTA ADSLQVAADK YFASVPFPEV ERIVGKKMLQ TYMKYIPAEQ RIGIFKVIDK
RFKGDSDAFI NACFEYSIFG SKENFAKFIR KPSLYKIGND WMTLLKYSIT DGLLQTTIAM
MDANRNYNAA HKVWVKGMMD MKREAGTPIY PDANSTLRLT YGRVLPYKPA DGVEYGYYTT
LKGAMEKEDP DNWEFVVPAK LKQLYQTKDF GRYAMPDGEM PVCFIVNTDN TGGNSGSPVF
NAKGELIGTA FDRNYEGLTG DIAFRPSSQR AACVDIRYTL FIIDKYAGAS HIIKELTISE
AEPDMTKSN
//
