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Database: UniProt
Entry: A0A2Z3GXG7_9BACT
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Original site: A0A2Z3GXG7_9BACT 
ID   A0A2Z3GXG7_9BACT        Unreviewed;       696 AA.
AC   A0A2Z3GXG7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Peptidase S9 {ECO:0000313|EMBL:AWM36197.1};
GN   ORFNames=C1280_03670 {ECO:0000313|EMBL:AWM36197.1};
OS   Gemmata obscuriglobus.
OC   Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC   Gemmata.
OX   NCBI_TaxID=114 {ECO:0000313|EMBL:AWM36197.1, ECO:0000313|Proteomes:UP000245802};
RN   [1] {ECO:0000313|EMBL:AWM36197.1, ECO:0000313|Proteomes:UP000245802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5831 {ECO:0000313|EMBL:AWM36197.1,
RC   ECO:0000313|Proteomes:UP000245802};
RA   Franke J., Blomberg W., Selmecki A.;
RT   "G. obscuriglobus.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP025958; AWM36197.1; -; Genomic_DNA.
DR   RefSeq; WP_010044740.1; NZ_CP042911.1.
DR   AlphaFoldDB; A0A2Z3GXG7; -.
DR   KEGG; gog:C1280_03670; -.
DR   OrthoDB; 9812921at2; -.
DR   Proteomes; UP000245802; Chromosome.
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; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B_N.
DR   PANTHER; PTHR11731:SF118; BLR1971 PROTEIN; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245802};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..696
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016425725"
FT   DOMAIN          121..409
FT                   /note="Dipeptidylpeptidase IV N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00930"
FT   DOMAIN          497..688
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          81..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   696 AA;  78238 MW;  8C8E987913702A55 CRC64;
     MPRVFALLAL LTFAHIGAAQ GTKQDYERAN SVGKWTAGKV TATKVAPNWT PDGQQFWYQN
     ANKEFVLVDM VKGTREVVAE DKLPKDAKPT PPPKKKRFDA ADEGGDTFVR LAQPPRRGAE
     SPDGKWATFL KDSNVWLRDT KTKEETQLST DGKPGDSYGT VFWAPDSQKL IAIKTKAGGD
     RKVTLVESSP RDQLQPKTST LNYLKPGDPI PLSKPHLFDV AAKKEVATSD ELFPNPWDTG
     FEHWAPDSKR FYFTYNQRGH TVMRLLAIDA ESGKVTAVVN EECKTFFDYA NKLFVQYLDD
     TNEAVWMSER DGWNHLYLID LATGKARNIT KGEWVVRGVE RVDVKNREVW FRALGVHPDQ
     DPYHVHFCRI KLDGTGLVKL TDGDGTHTVE YSPDRKHLID TYSRVDLPPV VELRRTADGK
     KVCDLEKADA AELLKTGWRY PERFVAKGRD GTTDIHGYIV RPSNFDPSKK YPVIEHIYAG
     PHDHHVRKGF SPAPYEQRMA ELGFIIVKID GMGTNWRSKA FHDVCWKNLG DSGFPDRILW
     IKAAAEKYKE MDLSKGVGIF GGSAGGQSST RAVLAFGDFY TVAVSDCGCH DNRMDKIWWN
     ELWMSWPVGP HYAEQSNVTQ AHKLKGKLLL VVGELDRNVD PASTLQVANA LIRADKDFEL
     LVVPGGGHGI AESPYGSRRR MDFFVRNLMG VEPRAR
//
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