ID   W4UQV2_9BACE            Unreviewed;       695 AA.
AC   W4UQV2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=JCM10512_1227 {ECO:0000313|EMBL:GAE82983.1};
OS   Bacteroides reticulotermitis JCM 10512.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE82983.1, ECO:0000313|Proteomes:UP000019131};
RN   [1] {ECO:0000313|EMBL:GAE82983.1, ECO:0000313|Proteomes:UP000019131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE82983.1,
RC   ECO:0000313|Proteomes:UP000019131};
RA   Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT   Isolated from the Gut of a Termite.";
RL   Genome Announc. 2:e00072-14(2014).
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:GAE82983.1}.
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DR   EMBL; BAIV01000006; GAE82983.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4UQV2; -.
DR   STRING; 1445607.JCM10512_1227; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000019131; 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:UP000019131};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   695 AA;  78679 MW;  3EC12AA715841C7D CRC64;
     MWLLQLMQEQ HSIDMMKKQG LKLDAKDLYN PNGVSLKDAV GIFGGGCTGE IISPEGLILT
     NHHCGYASIQ QHSSVEHDYL TDGFWAASRD KELATPGLKF TFIERIEDIT DLVNAKIAAK
     EITESESFTG PFLEKLAMSL YQQSDLKGKK GIVPQALPFY AGNRFYIFYK KIYSDVRMVA
     APPSSIGKFG GETDNWMWPR HTGDFSIFRI YADANGEPAE YAATNTPLKT QKHLSISLKG
     LKEGDYAMIM GFPGSTSRYL TVSEIKERME STNDPRIRIR GARLSVLKEV MNASDKIRIQ
     YANKYAGSSN YWKNSIGMNK AIIDNDVLGT KAEQETLFAA FAQKQNNSDY VKVVSQIDNH
     IAQTSPLNYQ FTSLREVFFA AIEFGNNQLT TLREALVAKN DSLIKVRLQE LKEAYAEVHN
     KDYDHEVDRK VAKALFPLYA EMIPAEQRPS IYRVIEQKYK GDYNKFIDEM YDHSIMANQT
     NFDNFVKKPT VKVIDQDLAI QYCQSKYDAY RQLASQLQEL NKDLALLHKT YIRGLNEMKL
     PVPSYPDANF TIRLTYGNVK AYSPKDGVHY NYYTTTNGIL EKENPEDREF VVPAKLKELI
     ENKDYGRYAL PNGEMPVCFL STNDITGGNS GSPVLNENGE LIGCAFDGNW ESLSGDINFD
     NSLQRCINLD IRYVLFILDK LGNCGHLINE MTIVE
//