ID A0A060RD93_9BACT Unreviewed; 702 AA.
AC A0A060RD93;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=BN938_1935 {ECO:0000313|EMBL:CDN32013.1};
OS Mucinivorans hirudinis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Mucinivorans.
OX NCBI_TaxID=1433126 {ECO:0000313|EMBL:CDN32013.1, ECO:0000313|Proteomes:UP000027616};
RN [1] {ECO:0000313|EMBL:CDN32013.1, ECO:0000313|Proteomes:UP000027616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|Proteomes:UP000027616};
RX PubMed=25657285; DOI=10.1128/genomeA.01530-14;
RA Nelson M.C., Bomar L., Graf J.;
RT "Complete Genome Sequence of the Novel Leech Symbiont Mucinivorans
RT hirudinis M3T.";
RL Genome Announc. 3:e01530-e01514(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}.
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DR EMBL; HG934468; CDN32013.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060RD93; -.
DR STRING; 1433126.BN938_1935; -.
DR KEGG; rbc:BN938_1935; -.
DR PATRIC; fig|1433126.3.peg.1912; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_013776_0_0_10; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000027616; Chromosome I.
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:UP000027616};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 21..702
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023103853"
SQ SEQUENCE 702 AA; 79056 MW; F7FB66EA39A76364 CRC64;
MKKLFIAAVA LFVTVFTARA DEGMWLLPFV KDLNIKDMQK KGFKLSAEQI YSLNQNALKD
AIVIFGGGCT GEIISPEGLV LTNHHCGYGT IQSHSTVEHD YLKNGFWAKT KEQEIPSPGL
GVIFVRKIED VTTRVLEGVT DKMTEQERAA KIRENSLQIV TKNTNKEENL TANVSSMFGG
NQYLMFINER FGDVRFVGAP PSSIGKFGGE TDNWMWPRHT GDFSLFRVYA NGENKSTDNY
EKTNKPYQPK EHLKVSLKGY KEGDYAMIMG FPGRTNRYMT TWEIDQTLEQ DNPIRIYVRG
ERQKLMWEDM IASDEVRIKY ANKYAGSSNY WKNSIGMSRG LKKLDVRSKK QAEQDVFVAW
VNADPSRKAK YGDALVLIEE AVKGRRPAAR ELQYISEALM NVESFQLASR ANAILNQKMA
PEKQKEELLK AGEAFFKNYN QSTDRKITPK LLEIFVADSK SPLINQMQGL NATQLTKEIF
DNSVFVDQDK YNAWVATLSN IDSDPAIMAV RAIMARGGEL SQGQATYNQK FAEGHRKYLA
GLLEMNKGKK SMYPDANFTM RMTYGQVLPY WAADAVFYNY YTTLGGVVAK RNNDDPEFVV
PDKLVELWKS KDFGQYAVNG DVPVALLSNN DITGGNSGSP VMNGKGELIG LAFDGNWEAM
SGDIAFEPEL QRTISVDIRY VLFIIDKFAG ANNLIQEMTI VK
//
