ID   A0A0F6TQK7_9GAMM        Unreviewed;       722 AA.
AC   A0A0F6TQK7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=TQ33_1256 {ECO:0000313|EMBL:AKE52212.1};
OS   Kangiella geojedonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC   Kangiella.
OX   NCBI_TaxID=914150 {ECO:0000313|EMBL:AKE52212.1, ECO:0000313|Proteomes:UP000034071};
RN   [1] {ECO:0000313|EMBL:AKE52212.1, ECO:0000313|Proteomes:UP000034071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCS-5 {ECO:0000313|EMBL:AKE52212.1,
RC   ECO:0000313|Proteomes:UP000034071};
RA   Kim K.M.;
RT   "Complete genome sequence of Kangiella geojedonensis strain YCS-5T.";
RL   Submitted (FEB-2015) 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; CP010975; AKE52212.1; -; Genomic_DNA.
DR   RefSeq; WP_046561308.1; NZ_CP010975.1.
DR   AlphaFoldDB; A0A0F6TQK7; -.
DR   STRING; 914150.TQ33_1256; -.
DR   KEGG; kge:TQ33_1256; -.
DR   PATRIC; fig|914150.5.peg.1273; -.
DR   HOGENOM; CLU_013776_0_0_6; -.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000034071; 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   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; 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:UP000034071};
KW   Serine protease {ECO:0000256|RuleBase:RU366067};
KW   Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           22..722
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023153798"
SQ   SEQUENCE   722 AA;  81110 MW;  6DD343C42C73BEFB CRC64;
     MKKLLSVAAI SVAAATSPLM ADEGMWQPSQ LPLIEDQLED AGLNIDPEDL SKLTEFPMGA
     VISLGGCTAS FLSPQGLVAT NHHCAYGSIQ FNSTAENNLL EKGFLAKELS EELAAAPGSR
     VYVTTEVTDV TDAINDGLTD EMSGMERYKA VEKKEKALVA DCEAEDGYRC NVYTFHGGLE
     YRLIKQMEIR DVRLVYAPSS HIGKYGGDVD NWMWPRHTGD FAFYRAYVGK DGKPADFSKD
     NVPYEPEHFL KVNASGVEKG DFVMVTGYPG RTNRYRTSAE VENQFEWSYP TFRTILHKYI
     DIIKENAPEG SDARVKYAST LAGLNNAEKN WGSMIESYGK GDLLARKQKL EADLEAWLLD
     NPAMKEKHGD ALSQLDALIK EDIKDQAVEL KKWGMNRDTL SGTAARLYRL AIESQKPDAE
     REPGYQERDL IRIKEGLKRM NRRWDADVEK ALYKHFVAVY AELPEEDRVQ SYDKFMGIDE
     EFNAEKFNGK VDKMFAETGL TDEETRLSWV GKSVDEFKAS DDPFIQLAVA TFEEKHQKEL
     EEKEQSGKFK KLRPQYMAAI IDYYESQDKA VYADANSTLR VTYGNVKGYS PKDGIFATPF
     TTLEGLAAKH TGEEPFNSPA KQLELIKDKQ YGKYQDETLN SVQVNFLSTV DTTGGNSGSP
     TMNGDAEFVG LLFDGVYESI IGDWDYNPNL NRSIHVSSAY MLWVMEHIDG AQNLIKEMKI
     VR
//