ID A0A0S7C2J6_9BACT Unreviewed; 697 AA.
AC A0A0S7C2J6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dipeptidyl aminopeptidase {ECO:0000313|EMBL:GAP44321.1};
GN ORFNames=TBC1_12122 {ECO:0000313|EMBL:GAP44321.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP44321.1};
RN [1] {ECO:0000313|EMBL:GAP44321.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP44321.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
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DR EMBL; DF968183; GAP44321.1; -; Genomic_DNA.
DR RefSeq; WP_062043412.1; NZ_DF968183.1.
DR AlphaFoldDB; A0A0S7C2J6; -.
DR STRING; 1678841.TBC1_12122; -.
DR PATRIC; fig|1678841.3.peg.2799; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000053091; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF07676; PD40; 3.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Aminopeptidase {ECO:0000313|EMBL:GAP44321.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:GAP44321.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053091};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..697
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006633456"
FT DOMAIN 489..697
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 697 AA; 79738 MW; DCF2E0613955717C CRC64;
MKNLRLFMSA FLMAGMTFTG LAQERFTAET MWKLGRVGDV QLAPQGGSII YGVTWYNAET
NKGNRDIYKL DPNAESPRRL TEFTGSEFNA IWRPDGKKIG FLSAESGSVQ LWEMGPHGEN
KEQISNIEGG INGFLYSPDM QYIAYTKDVK IEQDVHDRYP DLPLADALIY DDLMYRHWDS
WHDYAYSHIF IAPYNNGKPG EGKDIMPGEP WDSPMTPFGG MEQIVWSPDS KALAYTCKKL
KGREYAVSTN SDIYLYNLTS GTTENLSESN PGYDQDPVFS PDGSRLVWRS METPGFEADK
DRIMMVEFNP KALEKLKKDL KPKAGQAVSI KSRVYTDLSE GFDQSSSQFS FSADGKYLYF
ISGIHATYQV YKMELASKKI TRLTSGDHDI QSYAIDGNDL IITKMRHDLP TEVFRVRPDG
SEEQLTFTNR HILKNVKLGK SEKRWITTTD GKKMLVWVIL PPDFDPAKQY PALLYCQGGP
QSAVSQFFSY RWNFQMMAAN DYVVVAPNRR GLPTFGQEWN DQISGDYGGQ NMKDYLTAID
SVAAEPWVDE NRLGAVGASY GGFSVYWLAG NHNKRFKTFI SHCGIFNFES MYLETEEMFF
VNFDYKGAFY DNPRPKSYDF SPHNFVGNWD TPMLVVHGGY DFRIPYTQGM QAFNANQLKG
IPSRFLFFPN ETHFVLKPQN SILWQREFFN WLDTYLK
//