ID C7M853_CAPOD Unreviewed; 721 AA.
AC C7M853;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN OrderedLocusNames=Coch_1768 {ECO:0000313|EMBL:ACU93313.1};
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:ACU93313.1, ECO:0000313|Proteomes:UP000006650};
RN [1] {ECO:0000313|EMBL:ACU93313.1, 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; ACU93313.1; -; Genomic_DNA.
DR RefSeq; WP_015782816.1; NC_013162.1.
DR AlphaFoldDB; C7M853; -.
DR STRING; 521097.Coch_1768; -.
DR MEROPS; S46.002; -.
DR GeneID; 29675370; -.
DR KEGG; coc:Coch_1768; -.
DR eggNOG; COG3591; 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 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:UP000006650};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}.
SQ SEQUENCE 721 AA; 82242 MW; 3FF76DD9E0345AAD CRC64;
MKKISLILLA FLLLTPIAKA DEGMWFLMFI ERLNQRDMQK LGLQLTAQEI YSINNNSLKD
AIVQFNGGCT ASIISKDGLV LTNHHCGYGN IAQLSTPENN HLKNGFWARS HAEELSPKQS
FVRFFVRMDN VTDRMLSVVK PSMNEKEREA ALNQEMAKIQ KENSEGGKYV VSVRPFFQGN
EYYYFVYQDF KDVRLVGTPP ESIGKFGGDT DNWEWPRQTG DFSLFRVYTD KDGNAADYSP
NNVPLKAKRY LKVSLKGVQD KDFAMIMGYP GRTNRWESSY WVDQNVKYAY PAWVEASKTA
MDAMKRFMDK DDAVRLQYAS QYSSIANYWK NRQGMIDALT AHKTAATKRK TEAIFAKWAN
KAENKAEYGD VLNTLSNFFE KTNAKSADEN YLGMLWRASF FVKIPTRYIS LVSNAKKGGM
PTDELEKRVD DLLTEYDKVN LDVEKAILAD MLKLYTNKGT DVPSELKTIK TQYKGDFNKY
VEELLAKSIY RSKETAKEGV FPKNKVFQNE KQINMALASD PILALSIALF VNYRNPSEEQ
LSLEDSYAKA FRKFIKGMRD SKISTILYPD ANSTLRLTYG TVIPLAADKR NPDVKKNYYT
TFNTLMAKYK KGDAEFDMPQ RMLDLYKKKE FGRYIDKDGS MHVNFLTNND ITGGNSGSPV
MNGKGELIGL AFDGNIEAMA GDVIFDKQLQ RTINVDIRYV LWVIDIYAGA KNIINEIETV
Q
//