ID   W7Y160_9BACT            Unreviewed;       717 AA.
AC   W7Y160;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=JCM21142_301 {ECO:0000313|EMBL:GAF01687.1};
OS   Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC   Saccharicrinis.
OX   NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF01687.1, ECO:0000313|Proteomes:UP000019402};
RN   [1] {ECO:0000313|EMBL:GAF01687.1, ECO:0000313|Proteomes:UP000019402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF01687.1,
RC   ECO:0000313|Proteomes:UP000019402};
RA   Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA   Iida T., Darby A., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT   Anaerobe Isolated from Marine Mud.";
RL   Genome Announc. 2:e00206-14(2014).
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:GAF01687.1}.
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DR   EMBL; BAMD01000002; GAF01687.1; -; Genomic_DNA.
DR   RefSeq; WP_027472651.1; NZ_KI912107.1.
DR   AlphaFoldDB; W7Y160; -.
DR   STRING; 869213.GCA_000517085_03199; -.
DR   eggNOG; COG3591; Bacteria.
DR   OrthoDB; 9805367at2; -.
DR   Proteomes; UP000019402; 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   Reference proteome {ECO:0000313|Proteomes:UP000019402};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           22..717
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023127629"
SQ   SEQUENCE   717 AA;  81253 MW;  078FDF9C8952337D CRC64;
     MKKLTVLFIA FVMAFAGTAK ADEGMWLLPL ISKLNMNKMN DMGLKLTAED IYSVNNSSLK
     DAIVIFGRGC TAEIISDQGL ILTNHHCGYG NIQALSSVDH NYLKDGFWAK SLDQELPAEG
     LSITFLKRME DVTAKVLEGI DDNTKTSKRN ELIINNIEAI KKEAQKDNDY SIEVKSYFEG
     NQYFLLQYEK YNDIRFVGAP PSSIGKFGFD TDNWMWPRHT GDFSMFRVYA DKDGKPAAYS
     KDNVPLKPKH HLPISLKGVQ LNDFAMTLGY PGSTNRYLTS WGIEERMNIV NDARIVPRGL
     KQDLWQEDML ADEKINIQYA SKFSRSSNYW KNSIGMNRGL KKLNVVAQKR EIEKDFAQWV
     AASPERTKLY GKVLGNLKQA YAERAGDLKA QSYLIECMLR GTEIISLGSK TLKLEKDLEG
     DDQEKALSTA KKIASELDAF FKDYSAPTDH KVFAAMLKLY YDEINEKYHP DFFKDVVVKK
     YKGDFKKYAD VVFAKSVFVN QENLEAFLAA PNLKKLRKDP VFIAAKSTIE TYRKLYGKVI
     AANSLEEENN RLFLKGLMEM KSDKVFYPDA NFTMRLSYGK VGNYEPKDAV IYKHYTTLTG
     VMEKYQPGNF EFEVPAKLMD LYESKDYGQY ADADGTMHVC FTTDNDITGG NSGSPVINAN
     GELFGLAFDG NWEAMSGDIA FETELQKCIN VDIRYVLFII DKYAGATNLI DEMTLVK
//