ID   A0A285IE60_9GAMM        Unreviewed;       718 AA.
AC   A0A285IE60;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=SAMN06297280_1065 {ECO:0000313|EMBL:SNY46259.1};
OS   Arsukibacterium tuosuense.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Arsukibacterium.
OX   NCBI_TaxID=1323745 {ECO:0000313|EMBL:SNY46259.1, ECO:0000313|Proteomes:UP000219353};
RN   [1] {ECO:0000313|EMBL:SNY46259.1, ECO:0000313|Proteomes:UP000219353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12461 {ECO:0000313|EMBL:SNY46259.1,
RC   ECO:0000313|Proteomes:UP000219353};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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}.
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DR   EMBL; OBEB01000001; SNY46259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A285IE60; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000219353; 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..17
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           18..718
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023087873"
SQ   SEQUENCE   718 AA;  79080 MW;  5EAEE38C4A12292D CRC64;
     MKRSLLLLAL ASSMAMADEG MWMPQQLPDI AAELETAGLA LNPANLTKLT EFPMAAIVSL
     GGCSASFVSP EGLVVTNHHC VYNSIAHNST PENDLLANGF LASKMADEVP AAPGSRVYVT
     KAVDNVTTQV IDAATAKLSG KKRIDAIEVN QKKLIAECEQ DEGHRCRVAA YYGSLEYYLI
     KQLEIKDVRL VHAPAEGVGK FGGDTDNWMW PRHTGDYGFL RAYVSPDGKS ADYHQDNVPY
     KPDHYLKLAA KGLEEGDFVM ALGYPGRTNR HRLPSEVSET FEWSYPNTVQ QFKDTLAIID
     RVTSTNKDAE LKYASRVAGL NNYMKNRQGM LDSFAESDFL QRKTAEHQAL TSWVNSSRDN
     KKAYAKDLIT IDKLLAEQHL KARADYALNN ATPRLLTVSR YLYRLAQEST KPDTERKAGY
     QQRDIPRFKA FVAGMERNFD VSVEKALDLH NLTKYVALPK KQRNADFDSA LGIKGSMSNS
     ELAALIDSWY ANTGLTELSN RTALIDSTPA QFSQSADPFV SAAVALYKAD LKQEAEEEEL
     GGKIQQAYAS YMRAKMAFMQ AQGKAVYPDA NSTLRVTYGN VKGRAHGNED GNAWAPFTTL
     RGITAKATGE GEFNAPAEQL AAIKAKNYGR YLEPGLNSVP VNYLATLDIT GGNSGSAILN
     SKGEFVGLAF DGTLDSIISD WDYNPANTRS IQVDHRFMLW QMQQVDKATA LLKEIGVQ
//