ID A0A1G1B9S6_9BACT Unreviewed; 713 AA.
AC A0A1G1B9S6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN ORFNames=A2X65_01490 {ECO:0000313|EMBL:OGV79503.1};
OS Stygiobacter sp. GWF2_38_21.
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Melioribacteraceae; Stygiobacter.
OX NCBI_TaxID=1801612 {ECO:0000313|EMBL:OGV79503.1, ECO:0000313|Proteomes:UP000176810};
RN [1] {ECO:0000313|EMBL:OGV79503.1, ECO:0000313|Proteomes:UP000176810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV79503.1}.
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DR EMBL; MHBR01000023; OGV79503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1B9S6; -.
DR Proteomes; UP000176810; 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; 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 Serine protease {ECO:0000256|RuleBase:RU366067};
KW Signal {ECO:0000256|RuleBase:RU366067}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT CHAIN 23..713
FT /note="Dipeptidyl-peptidase"
FT /evidence="ECO:0000256|RuleBase:RU366067"
FT /id="PRO_5023158793"
SQ SEQUENCE 713 AA; 81292 MW; 9E17AC570A2CA960 CRC64;
MKKLNFALLF IILFAFILPL QAQLKVDTVK AQKYDNGKMW PFDYPPVEYL KETYDLKTDE
AWYEDVRLSA LRLPGCTSSF VSEDGLMMTN HHCARGLLER MSKEGEDLIK DGFYAKTLAD
ERKIPEFFPG KPYYADQLVM IKDVTAEIQT AENTGTTIAE KAANKKAKIK EITEKMNKET
GLVCELYSLY NGGKFSLYGY KRYTDIRLVF APDMQIAYFG GDFDNFTYPR YNLDCTFYRA
YENDKPVKST NYFKFSFDGI KPGEPIFTVG NPGTTNRLKT VAQLEYARDI AYRNNAFLFD
SYYYALEDLI KEDDSRKKEL EDLRVDLGNS QKVIATTLKG LKDTYVYAKK MDFQKKLQEA
VWNNSELKEQ YGKVWENIEK TRAEMRKVGP QMAAYSIGFN GLFGSKYFAL AKSLNDLVKE
LQKPEDQREA KFKAAKLDST LEAMFPDKVD KLLENTKLWI NVEYMALNLG KDDPVVKKLS
GGKSGKAIAE NLLDESIFGD MDDVIDLAKE GADAILKSED PILMYVREAA KRTTELQKQV
QEINDTENIY DDMLGQVIVK IHNTELPPDA NFTLRLSDGT LKPFEYNGTV APDFTTFYGM
YDRFFSFRKT YPWDLHSRWA KVPSGLDLST PFNFVSSNDI VGGNSGSPVI NKNAEVVGLA
FDGNIDSIIG NYIYIPYNNR MVAVDSRAMV HAMDEVYDAE RIADELKSGK ISE
//
