ID   A0A1S9B145_9BACT        Unreviewed;       754 AA.
AC   A0A1S9B145;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=B0919_08595 {ECO:0000313|EMBL:OON69532.1};
OS   Hymenobacter sp. CRA2.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1955620 {ECO:0000313|EMBL:OON69532.1, ECO:0000313|Proteomes:UP000189843};
RN   [1] {ECO:0000313|EMBL:OON69532.1, ECO:0000313|Proteomes:UP000189843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRA2 {ECO:0000313|EMBL:OON69532.1,
RC   ECO:0000313|Proteomes:UP000189843};
RA   Kabwe M.H., Vikram S., Govender N., Bezuidt O., Makhalanyane T.P.;
RT   "Draft genome sequence of Hymenobacter sp. CRA2 isolated from the shrubland
RT   biome in South Africa.";
RL   Submitted (FEB-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}.
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:OON69532.1}.
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DR   EMBL; MVBC01000004; OON69532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9B145; -.
DR   STRING; 1955620.B0919_08595; -.
DR   Proteomes; UP000189843; 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, ECO:0000313|EMBL:OON69532.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189843};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU366067}; Signal {ECO:0000256|RuleBase:RU366067}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT   CHAIN           23..754
FT                   /note="Dipeptidyl-peptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU366067"
FT                   /id="PRO_5023153705"
FT   REGION          728..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..754
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  84100 MW;  0F208838FABCD9DA CRC64;
     MPRSLRLCAV LLTLLLPAAA RADEGMWLPL LLKQLNEADM QQKGLKLTAE DIYSVNRGSL
     KDAIVQFGGG CTGEIISNEG LLLTNHHCGY GQIQQHSSVE HDYLTKGYWA MTREQELPNP
     GLTATFIVRM EDVTAPVLQG IQPGIAEADR ERIVQQRSAE LAQKAVQGTH YKAFVRPMFG
     GGEYYLFVTE VFEDIRLVGA PPSSIGKFGG DTDNWMWPRH TGDFSMFRIY AGPDNKPAPY
     SKDNKPFRPR HSLPISLSGV KPGDFTLVFG FPGRTTEYLT SWGVDETFNV SDPARVKVRD
     TKLRILDADM KASDKVRIQY AAKYASLANY WKKWIGEMRG LKRLDAVTRK QQQEQQFRQW
     VQQGDANRKA AYGQILDQLE QQYKLVRPYV VARDYTTEAA MGIEVLAYAN ALQQLVDLIQ
     AKAPQAELLA AIDKARKGTP GSFRNVNVAT DQKVAAALLP LYAEGTPEQL LPDNIKALRK
     QNTTPEAWQR YVADVYRRSR LTSEASALQV LDELAKGNAT ALTADPAYQL IAPIVATYRQ
     KVLPTYTQAQ DQITLLQRTY IAGLRQWQPQ RKFYPDANST LRVAYGQVAG YQPADGVAYE
     YYTTLDGIME KADPTNPDFE VPARLVELYQ KKDYGPYAVD GTVPVAFTAT NHTTGGNSGS
     PVINGRGELI GTNFDRNWEG TMSDIMYDPD RVRNITLDVR YMLFVVDKYA GASHLVKEMN
     LVGGPLSGRA NGSLEQQPKK QKVKVKREKT AAAN
//