ID A0A069CYG1_9BACE Unreviewed; 716 AA.
AC A0A069CYG1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=JCM15093_348 {ECO:0000313|EMBL:GAK35267.1};
OS Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK35267.1, ECO:0000313|Proteomes:UP000027601};
RN [1] {ECO:0000313|EMBL:GAK35267.1, ECO:0000313|Proteomes:UP000027601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK35267.1,
RC ECO:0000313|Proteomes:UP000027601};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(2015).
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:GAK35267.1}.
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DR EMBL; BAJS01000001; GAK35267.1; -; Genomic_DNA.
DR RefSeq; WP_027317666.1; NZ_BAJS01000001.1.
DR AlphaFoldDB; A0A069CYG1; -.
DR STRING; 1121097.GCA_000428125_00219; -.
DR eggNOG; COG3591; Bacteria.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000027601; 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:UP000027601};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}.
SQ SEQUENCE 716 AA; 81395 MW; AB5B9C55E3837375 CRC64;
MSLKKIRKQL AILLLLSVNL TVCAHEGMWM LGRLNKQTTQ SMKELGLKLP ADKLYHPNKA
TLKDAVVSFG GFCSGVVVST DGLVFTNHHC GFGAIQQHST VQKDYLKDGF VARSKEEELP
NPELYVRFLI RTEDVTQRVL GSVSPNMSEA DRRSVIDSVM LAIQEEVHTK DSSVVGVVDA
YYGGNEFWLS VYRDFNDVRL VFSPPSFIGK FGWDTDNWMW PRHTGDFSVF RIYADKNNQP
ADYSPDNVPY KPQYVAPIST QGYQEGSFCM TLGYPGSTER YLSSFGVQEM VEGMNQAMID
VRGVKQAIWK REMNKRQDIR IKYASKYDES TNYWKNSIGT NKAIKDLKVL EKKREMESSL
KQWIQQAPGA DSLSIQLLST LELNYKNRKQ TNRAMAYLGE SFMNGPELVQ LALEILNFDF
EAEEKVVVSK IKDIMEKYAN LDLDIDKEVF TAMLREYPQH VDSVYLPEMY NTIAKEYGGD
YKVYVDSLYA RSEITSPRGL QRFFERDTTY NLMDDPAISL GIDLIVKYFE MNQSINEASQ
NIEKGERLYN AAIRRMYADR NFYPDANSTM RLSFGTVKGY SPMDGVDYSY YTTAKGILEK
ARTHHPDPDF ALGANLISLL KEQNYGKYAD EKGEMKVCFI SDNDITGGSS GSAMFNAKGE
LLGLAFDGNW EAMSGDILFE PKLQRCVGVD IRYILFVIDK YANASNLIQE LQPSLK
//
