ID A0A1F3ECH1_9BACT Unreviewed; 724 AA.
AC A0A1F3ECH1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidase S9 {ECO:0000313|EMBL:OFX52296.1};
GN ORFNames=A2X13_02255 {ECO:0000313|EMBL:OFX52296.1};
OS Bacteroidetes bacterium GWC2_33_15.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1797324 {ECO:0000313|EMBL:OFX52296.1, ECO:0000313|Proteomes:UP000177978};
RN [1] {ECO:0000313|EMBL:OFX52296.1, ECO:0000313|Proteomes:UP000177978}
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 -!- 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:OFX52296.1}.
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DR EMBL; MENN01000005; OFX52296.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F3ECH1; -.
DR Proteomes; UP000177978; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..724
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009488472"
FT DOMAIN 97..440
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 529..724
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 724 AA; 83838 MW; AE7BFBBA27ECA40F CRC64;
MKSFIFCSLT FILLFFSTEI VAQQEIKKIT LEDIFKDKVF TEKTVSGLRS MNDGEHFTLL
ENDNQIVKYS YKTGDVVSII FNAFSNEIDV KDYEFSGDES KILIATNEEY IYRRSYKADY
SIYDLTAKTC EKLSENGAQM FASFSPDNSK VAFVRDNNIF IKDLIQKTEQ QITFDGMFNY
IINGGTDWVY EEEFVFTRAF FWSPDGNQIA YYKFDESNVP VFNMTKYKSE IYPENYAFKY
PKAGESNSVV SIHVYDLISG KTKTMDIGPE KDQYIPRIKW TPGNKLAIIR ENRLQNKIEI
LLSNPNDGTH KIIYKESNKY YIERIDDSYM TLTRDGRYFI INSEKDGWNH FYLYDINGEF
INQITKGAWE VTSFIGLDSK TNTIYYHAAE ESPLVKDVYS IKLDGTKKKK LSSLKGTNKA
VFSTGFKYYI NYYSNANTPT VITLHDNKGK LLRTLEDNLK LKETAKQYNF VPVEFLTINT
PSSNWDLNAY MIKPSDFDPN KKYPLFMFLY GGPGSQEVTD GWSREWYWFQ MLAQKGYIIA
CVDNRGTGAR GEEFKKMTYG QLGKYETIDQ VEAAEYLSSL PYIDKNRTGI WGWSYGGFMS
ALCLFNGSHV FEMAIAVAPV TNWRFYDSIY TELYMGLPKD NAEGYDNNSP LNHADKLQGK
FLLVHGTADD NVHFQNAIEL SEKLVQANKQ FEEQFYMDKG HGIRGKNTQL HLYTRMTNFI
LENL
//
