ID   A0A1G2V9T6_9BACT        Unreviewed;       713 AA.
AC   A0A1G2V9T6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=Dipeptidyl-peptidase {ECO:0000256|RuleBase:RU366067};
DE            EC=3.4.14.- {ECO:0000256|RuleBase:RU366067};
GN   ORFNames=A2749_02745 {ECO:0000313|EMBL:OHB18392.1};
OS   Parcubacteria group bacterium RIFCSPHIGHO2_01_FULL_45_26.
OC   Bacteria.
OX   NCBI_TaxID=1817737 {ECO:0000313|EMBL:OHB18392.1, ECO:0000313|Proteomes:UP000178084};
RN   [1] {ECO:0000313|EMBL:OHB18392.1, ECO:0000313|Proteomes:UP000178084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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|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:OHB18392.1}.
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DR   EMBL; MHXB01000005; OHB18392.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2V9T6; -.
DR   STRING; 1817737.A2749_02745; -.
DR   Proteomes; UP000178084; 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   PANTHER; PTHR38469; -; 1.
DR   PANTHER; PTHR38469:SF1; PERIPLASMIC PEPTIDASE SUBFAMILY S1B; 1.
DR   Pfam; PF10459; Peptidase_S46; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU366067};
KW   Hydrolase {ECO:0000256|RuleBase:RU366067};
KW   Protease {ECO:0000256|RuleBase:RU366067};
KW   Serine protease {ECO:0000256|RuleBase:RU366067}.
SQ   SEQUENCE   713 AA;  77870 MW;  4CBDD3031A5065F9 CRC64;
     MGALLTLQGG QVQKLRGTLS TMTTLVFCML LATQVRAGKT NATTDPCEQI LMARGMYTLN
     ALPKGLENCA GWDTLNEHLA TARAAMVRIN KEQGATGVMT GPNKLETNQH VAKSYVPETN
     AGVIETGCLA STPEEALPLE GIKVLVSNEP SAENATLTTN AINSTVTPAM SVTEAGKARR
     EAIEKLEREC EHRLGKGYIC IVDKRRPGLE YALYEHRVYT NVALVFLPPE VVAYRDSDNF
     EHGQGRGRVD QAELAVYNDD GTPVRLPFVP VLDYEYIEGD RGFAIGTPGI TYWNRSASLV
     EANRVFSEIA LERSLWAKDL CHKTAERRPE LSGAVKKVQV DVENSIKIFL AELADSPAVL
     AYRQKRERYY HYSLLAHDRS GLIMVEADKV GKLDADPVVS VATNWAERFV SLGLYGQRFK
     TAWALHRWAR VSQLPKEVRP KGWVTEAEVR ERIGEPTQDI DIELINSGSS LALMAKYLPE
     VAWVLGDGRY ETVASVLWTS YLNDQEEGLR LLQAGPNATC TSSDPLMQVA KAVEEIGWQS
     RPLRGRIEEA RKNAEQLIGL ATSGRASLPN ASGHPRLILS KVRGHKESGG PIPPFATLGA
     LAGRTNIGLP EWFVSGAAGD KTVINVEAEF FVVGGVSGSP HYTIVGDKLF VVGWAFDGNK
     DGITNRTWQG GPEARGLVVT ARGVRRFREI AGACGWPGCG PRRLPPCKQP SGK
//