ID E6SPB3_BACT6 Unreviewed; 721 AA.
AC E6SPB3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=Bache_2935 {ECO:0000313|EMBL:ADV44870.1};
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:ADV44870.1, 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:ADV44870.1, 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; ADV44870.1; -; Genomic_DNA.
DR RefSeq; WP_013548457.1; NC_014933.1.
DR AlphaFoldDB; E6SPB3; -.
DR STRING; 693979.Bache_2935; -.
DR MEROPS; S46.002; -.
DR KEGG; bhl:Bache_2935; -.
DR PATRIC; fig|693979.3.peg.3076; -.
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; 2.
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..23
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 24..721
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023154782"
SQ SEQUENCE 721 AA; 81363 MW; 6AA02083758C10EF CRC64;
MKITFKKCLL AATAALTVCS VRADEGMWLL QLMKQQNSID MMKKQGLKLE ADDLYNPGGV
SLKDAVGIFG GGCTGEIISP EGLILTNHHC GYASIQQHSS VEHDYLTDGF WAMNRNEELP
TPGLKFRFVH RIEDATDLVN QKIKAGEVDE IHAMTRPFLR KLAKEQLEKS DLKGKPGIEE
EILPYYAGNK YYLVYYKVYS DVRMVAAPPS SVGKFGGETD NWMWPRHTGD FSMFRIYADA
NGEPAEYSAS NVPLKTPKFL PISIKGLNEG DYAMIMGFPG STERCLTQSE VKQRMNAMNQ
PVIDMRGVRL EVLRKYMDAS DKTRIQYANK FAGSSNYWKN SIGMNKAIVD NDVLGAKAEI
EKRYAEFAKG KPEYEGVVEK IDAIIEKSTP TLRQLYYINE ALRGAIEFGS FYLIMDNIKQ
ALQEKNDSLL QVWKGRLDKA YSGMHNKDYD HEVDRAVAKA ILPALAKVLK ADELPSFYQT
IQNDFKGNFD AYVDNLYDNS ILSSRENLDK FLAKPTVKAI EKDPATAYSR SKNEKMQELG
KQYQELGNGL ELLHKAYIRG LGEMKQPIPS YPDANFTIRL TYGNVKAYNP RDAVHYKYYT
TTDGILEKEN PEDREFTVPA KLKELIQKKD FGRYAMKDGT MPVCFLTTND ITGGNSGSPV
INGEGQLIGC AFDGNWESLS GDINFDNNLQ RCINLDIRYV LFILEKLGGC EHLIKEMNII
E
//
