ID E6SMT2_BACT6 Unreviewed; 719 AA.
AC E6SMT2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=Bache_0623 {ECO:0000313|EMBL:ADV42648.1};
OS Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / CCUG
OS 15421 / P 36-108).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=693979 {ECO:0000313|EMBL:ADV42648.1, ECO:0000313|Proteomes:UP000008630};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P 36-108;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Bacteroides helcogenes P 36-108.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADV42648.1, ECO:0000313|Proteomes:UP000008630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / CCUG 15421 / P 36-108
RC {ECO:0000313|Proteomes:UP000008630};
RX PubMed=21475586; DOI=10.4056/sigs.1513795;
RA Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brambilla E.,
RA Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Bacteroides helcogenes type strain (P 36-
RT 108).";
RL Stand. Genomic Sci. 4:45-53(2011).
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; CP002352; ADV42648.1; -; Genomic_DNA.
DR RefSeq; WP_013546263.1; NC_014933.1.
DR AlphaFoldDB; E6SMT2; -.
DR STRING; 693979.Bache_0623; -.
DR MEROPS; S46.001; -.
DR KEGG; bhl:Bache_0623; -.
DR PATRIC; fig|693979.3.peg.665; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_013776_0_0_10; -.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000008630; Chromosome.
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:UP000008630};
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..719
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023157621"
SQ SEQUENCE 719 AA; 81629 MW; 485EED7AB0B3691C CRC64;
MKLKFAIIAA CCLFTLAGQA DEGMWMLGNL NRKTRESMKE LGLQMPAAEL YSPKRPSLKD
AVVSFGGFCS GVVVSEDGLV FTNHHCGFSS IQQHSTVEHD YLKDGFVARS KSEELPNPEL
YVRFLLKQED VTRRVLGAVA PDMDEAVRSA VVDSMMLLVG EEVSSKDSTL VGVVDAYYGG
NEFWLSVYRD YNDVRLVFAP PSSVGKFGWD TDNWEWPRHT GDFSVFRIYA DSSNRPADYS
PDNVPYHPEY VAPISLDGYR EGSFCMTLGY PGSTDRYLSS FGIEEMVQNT NQAQIDVRGV
KQAIWKREMD KRDSVRIKYA SKYDESSNYW KNSIGVNRAV RKLHVLDKKR AMEQELRRWI
RQTPGEQEQL LHLFSDLELN YKNRRETNRA QAYFVEAFLN GPELIQQALS LLNFDFEGEE
KTVIAGLKAI VEKYANLDLD MDKEVFTALL KEYRSKVDAT YLPAPYQAID TLYGGNCRAY
VDSLYAHSEL TTPRGLKRFL EQDSTYHIYD DPAITLGIDL ITKLFEMNMQ VQQASGEIQR
NERLLNAAVR RMYASRNFYP DANSTMRLSF GTVCGYAPFD GVEYAYYTTA KGVLEKVRAH
VGDVDFEVQP EIRSLLSSGD FGRYADEKGE MKVCFISDND ITGGNSGSAM FNARGELLGL
AFDGNWEAMS SDILYEPKMQ RTIGVDVRYM LFMIEKYGKA ENLIKELLLP GRRMQKAQL
//
