ID   G2EH95_9FLAO            Unreviewed;       711 AA.
AC   G2EH95;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=BZARG_482 {ECO:0000313|EMBL:EGV42225.1};
OS   Bizionia argentinensis JUB59.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Bizionia.
OX   NCBI_TaxID=1046627 {ECO:0000313|EMBL:EGV42225.1, ECO:0000313|Proteomes:UP000003730};
RN   [1] {ECO:0000313|EMBL:EGV42225.1, ECO:0000313|Proteomes:UP000003730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JUB59 {ECO:0000313|EMBL:EGV42225.1,
RC   ECO:0000313|Proteomes:UP000003730};
RX   PubMed=18842857; DOI=10.1099/ijs.0.65599-0;
RA   Bercovich A., Vazquez S.C., Yankilevich P., Coria S.H., Foti M.,
RA   Hernandez E., Vidal A., Ruberto L., Melo C., Marenssi S., Criscuolo M.,
RA   Memoli M., Arguelles M., Mac Cormack W.P.;
RT   "Bizionia argentinensis sp. nov., isolated from surface marine water in
RT   Antarctica.";
RL   Int. J. Syst. Evol. Microbiol. 58:2363-2367(2008).
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:EGV42225.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFXZ01000067; EGV42225.1; -; Genomic_DNA.
DR   RefSeq; WP_008639677.1; NZ_AFXZ01000067.1.
DR   AlphaFoldDB; G2EH95; -.
DR   STRING; 1046627.BZARG_482; -.
DR   MEROPS; S46.002; -.
DR   PATRIC; fig|1046627.3.peg.2872; -.
DR   eggNOG; COG4717; Bacteria.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000003730; 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   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; 2.
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:UP000003730};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           18..711
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023104680"
SQ   SEQUENCE   711 AA;  80575 MW;  A83944E7B07AEC21 CRC64;
     MKLLRLLVLF IVFQASAQQG GMWIPSLLEG MNEDEMTALG SKLTAQDIYD VNNSSLKDAI
     GHFNGGCTSE VISDQGLILT NHHCGFGQIQ SHSSLENDYL KDGFWAMNFE DELPNNGLYI
     EFIVRIEDVT DQVLNGVTDS MTEKERQSTV DKNSNKLQTT VTKEAWHDTK VKSFYKGNQY
     FLFVTERFND IRLVGAPPTS IGKFGSDTDN WVFPRHTGDF ALFRIYADKD NRPAEYSKDN
     VPYKPKHHLP ISLDGVEEGD FTMVFGFPGT TDEYLPAVAI EHITQEFNPS NIAIREAAVK
     IIDAEMKVND DVRIKYASKQ ARIANAWKKW IGENLGIKKS NAIAERRAFE ASFTKALKEK
     GLEDKYGHIL PEFDRLYKDF ADVDIKRRNF IEVFLVTNEL MTMTYRAYQV EQSLLQSPES
     IEKGREYITG VLEGIHKNYD VKVDKGVYEN VMPFYSKNNV DPTIYDKTAF TDLDSALALF
     EGSADDVIKK LNDDTAYAYA KPFIEEFFNT IDAEFQQKNE PITALQTEYM TALMIALPEE
     RYFPDANGTL RVTYGQVNGY SPSDAVHYSP VSYLDGVIEK YIPGDYEFDV PQKLIDLYEA
     KDYGQYADTN GKVPVCFLGT NHTTGGNSGS PAIDAHGNLV GLNFDRVWEG TMSDMNYDPE
     ICRNIMVDVR YVLFIVDKFA GAQHLIDEMT LVNPKTGKSK SKKRKNKKNR K
//