ID A0A101GJI1_9BACT Unreviewed; 719 AA.
AC A0A101GJI1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=XD81_0837 {ECO:0000313|EMBL:KUK59552.1};
OS Bacteroidetes bacterium 38_7.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1635292 {ECO:0000313|EMBL:KUK59552.1, ECO:0000313|Proteomes:UP000053999};
RN [1] {ECO:0000313|Proteomes:UP000053999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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:KUK59552.1}.
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DR EMBL; LGGC01000089; KUK59552.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101GJI1; -.
DR PATRIC; fig|1635292.3.peg.700; -.
DR Proteomes; UP000053999; 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 719 AA; 82523 MW; BAD3AB4F633519AD CRC64;
MKHIIRNIFT FLLGLVFSLN LYADEGMWLP YLLDQIQIEN MQSMGMKLSA EDIYNINHSS
LKDAIVIFGR GCTGEVVSAD GLVFTNHHCG FGAIQSSSSI ENDYLKEGFW ARNLKEEIPI
TGLTVQFLIN VTDVTNEMLD GVNFQMPENQ CDSILKFNEK RLLEAILAQD GMAGVIKEFY
AGNQYYLFVY QTYKDIRLVG APPTAIGKFG GDTDNWMWPR HTGDFSVFRI YTSPSGKPAT
YQVNNIPLKA KRYLTINAGG ITKGDFAMIM GYPGRTDRYA TSWGVAQAMN LTNPSIIKIR
DKKLEILRNS MAANDEIRIK YAAKYAGISN YWKYYIGQNK QLKRLKVYEK KKQQEKEFAD
WVSADPQRHE KYGGVLTGFE QAYQLLNQTA KPLVYIREAA FGPEIISFAS RSESLINQSV
NKNRNNLLEN LLLSAKEMGD SFFRNFDQST DKKLFAAMMS MYYNDMDPQF VPKVLLSANK
KYKGQWDKYA DKVYQKSIFS SMESFTKFLN NPSINIIKDD PIYQLAVAFK EMRRKIEAMN
VEARDQLKRN KRLYVEAVQL MYPNRSFYPD ANQTLRLTYG TIQDYQAADA IEYNYFTTHF
GILEKEDPSN PDFQVPYSLK EVFNQKYFSP YYKNDTVVTC FLTNNDITGG NSGSPVLNGD
GELIGLAFDG NWEAMSGDIA YEPELQRTIN VDIRYVLFLI DKYAHSHHIM RELSIKYER
//
