ID C7M6H9_CAPOD Unreviewed; 714 AA.
AC C7M6H9;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=Coch_0404 {ECO:0000313|EMBL:ACU91967.1};
OS Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 / NCTC
OS 12371 / VPI 2845) (Bacteroides ochraceus).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU91967.1, ECO:0000313|Proteomes:UP000006650};
RN [1] {ECO:0000313|EMBL:ACU91967.1, ECO:0000313|Proteomes:UP000006650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845
RC {ECO:0000313|Proteomes:UP000006650};
RX PubMed=21304645; DOI=10.4056/sigs.15195;
RA Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., Chen A.,
RA Palaniappan K., Chain P., Hauser L., Chang Y.J., Jeffries C.D., Brettin T.,
RA Detter J.C., Han C., Bristow J., Goker M., Rohde M., Eisen J.A.,
RA Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT "Complete genome sequence of Capnocytophaga ochracea type strain (VPI
RT 2845).";
RL Stand. Genomic Sci. 1:101-109(2009).
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; CP001632; ACU91967.1; -; Genomic_DNA.
DR RefSeq; WP_015781722.1; NC_013162.1.
DR AlphaFoldDB; C7M6H9; -.
DR STRING; 521097.Coch_0404; -.
DR MEROPS; S46.002; -.
DR GeneID; 29675586; -.
DR KEGG; coc:Coch_0404; -.
DR eggNOG; COG4717; Bacteria.
DR HOGENOM; CLU_013776_0_0_10; -.
DR Proteomes; UP000006650; 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 InterPro; IPR019500; Pep_S46.
DR InterPro; IPR009003; Peptidase_S1_PA.
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:UP000006650};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}.
SQ SEQUENCE 714 AA; 81146 MW; D6013130ABC01A94 CRC64;
MKKFISLLLF SFYLLPVTLT AQQGGMWIPS LLEGMNAREM KSLGMKMSVS DIYSVNKSSL
KDAVPHFNGG CTAEMISDKG LLLTNHHCGY GQIQAHSSVQ NDYLTDGFWA KNLSEELPNK
NLEVTFIVRI EDVTQKVLAD TQNLSSESVR ASQIERNIAS LVKNSPKEAW QENRVRAFYE
GNHYILFVVE TFKDVRLVGA PPSAIGKFGS DTDNWVWPRH TGDFSLFRVY ADKNNRPAAY
SKDNVPYRPK HFFPISLKGV KAGDFTMVFG YPGRTEEYLP AVAVEQIVNV LNPAKIGIRD
VVLKVQDGFM RNSNEIKIKY ASKYASVANY WKKWIGETQG LKKSDAVAIK RAQEQKFQKE
IEKAGKTAEY GYILPQFTEK YAQIQNYALA VDLFSELVQR NIDLLANGYK ILQLQNALHE
KGTQSFNDRK KTLLNNFETV FKNYDVNVDK AVFEKAVVYY AQAMPKTLLS PNLQQFEIHT
LADKLYKESF LASKTEMGKV LNLPDEAFER RLKNDIGVQF VQQIVAHFYG TVVPTYRQLD
SEITTLQRTY MKAILEFSKP QDRIFPDANS TLRVTYGKVA GYSPSDAITY DYMTYLDGVM
EKYVPNDYEF NVPAKLRELY EKKDYGIYGK NGKMPVCFIA TNHTTGGNSG SPAIDAQGNL
IGLNFDRVWE GTMSDIHYDP KICRNIMVDI RYVLFIIDKY AGAGYLLNEM KIVK
//
