ID A0A0A2GC14_9PORP Unreviewed; 715 AA.
AC A0A0A2GC14;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=HQ47_09020 {ECO:0000313|EMBL:KGN72991.1};
OS Porphyromonas macacae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=28115 {ECO:0000313|EMBL:KGN72991.1, ECO:0000313|Proteomes:UP000030103};
RN [1] {ECO:0000313|EMBL:KGN72991.1, ECO:0000313|Proteomes:UP000030103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-192 OH2859 {ECO:0000313|Proteomes:UP000030103};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Horsfall A., Kirkwood N.,
RA Harris S., Eisen J.A., Coil D.A., Darling A.E., Jospin G., Alexiev A.;
RT "Draft Genome Sequence of Porphyromonas macacae COT-192_OH2859.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGN72991.1}.
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DR EMBL; JRFA01000025; KGN72991.1; -; Genomic_DNA.
DR RefSeq; WP_036852173.1; NZ_JRFB01000011.1.
DR AlphaFoldDB; A0A0A2GC14; -.
DR STRING; 28115.HQ47_09020; -.
DR eggNOG; COG3591; Bacteria.
DR OrthoDB; 9805367at2; -.
DR Proteomes; UP000030103; Unassembled WGS sequence.
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; DIPEPTIDYL-PEPTIDASE; 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:UP000030103};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU366067}.
SQ SEQUENCE 715 AA; 81370 MW; 5DB759498877ECD1 CRC64;
MRKTLKLFLI SSLLLIVFGF RAFADKGMWI MSELNKQNIE RMRELGFKLP IDSLYSLDKP
SITNAVVIFG NGCTGITVSN EGLIFTNHHC GYEAIQSQST VDHDYLRDGF VSQNFAQELP
IAGLEVRYLR SVRDVTKEIT DSLTSCKTEM ERLQKAKILC SKIAIAEQNK LGDNVEVIVE
PFYANNAYYM IAYDVFKDVR MVFAPPSSIG KFGGDTDNWM WPRHTGDFSV FRVYAGKDNK
PAGYNKENKP FRPKYYAAVS LAGVSKDDYA MTVGFPGSTS RYIPSWGIRS RIDNTNTPRI
EVRGIKQEIW KEAMSADQAT RIKYASKYAQ SANYWKNSIG MNRGLEKLRV LDRKRMEEDA
FQKWTGTNKK GEQYKETLSL LKNGYENSGS FKRNQTYIQE ALLTGAEVGL IALYANMAAM
TPSSKAELLK HLNENVYKDY LPSLDRKVLP AMLKVVKERV PAEYLPDIYI TIDKDYGGDY
KAYADHLFDT SIIPYADKLN EVMKLPADQL QAKLANDPAV VFCNSVRNIL QDINNKTMEA
TMDISKGNRL YFAGRRVMDP NRQMPSDANF SMRMSYGSVK GYEPSDATWF SYYTTEKGIM
EKYDPKSYEF NVQDEILNLI KKKDFGRYAA KDGHLHIAFL STNDITGGNS GSPVFDKNGR
LIGLAFDGNW EAMSGDIEFE PDLQRTISVD IRYVLWTIDK WGKCPRLIKE LKLMK
//