ID   A0A1M6I0I5_9FIRM        Unreviewed;       422 AA.
AC   A0A1M6I0I5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Serine protease, S1-C subfamily, contains C-terminal PDZ domain {ECO:0000313|EMBL:SHJ27925.1};
GN   ORFNames=SAMN02745751_02160 {ECO:0000313|EMBL:SHJ27925.1};
OS   Dethiosulfatibacter aminovorans DSM 17477.
OC   Bacteria; Bacillota; Tissierellia; Dethiosulfatibacter.
OX   NCBI_TaxID=1121476 {ECO:0000313|EMBL:SHJ27925.1, ECO:0000313|Proteomes:UP000184052};
RN   [1] {ECO:0000313|EMBL:SHJ27925.1, ECO:0000313|Proteomes:UP000184052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17477 {ECO:0000313|EMBL:SHJ27925.1,
RC   ECO:0000313|Proteomes:UP000184052};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQZL01000015; SHJ27925.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6I0I5; -.
DR   STRING; 1121476.SAMN02745751_02160; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000184052; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:SHJ27925.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SHJ27925.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184052};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        61..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          328..405
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  45527 MW;  D1946B991A398E49 CRC64;
     MNKGEFEGKT SKENSEEILE DVSEETIGES TEEIHGELAN EQMAESYGQP SYRKKGYGRK
     YFFTALAGAL AGVIIGGLGV YYYIDSNIEE INDNLGIVKE INVDTSDNLY YASAVAEKSM
     DTVVGIVTTE KVNSMLWGTQ TYEGMGSGVI VDSDGYILTN SHVISDGDAD TIRVKFIDGS
     ESAGTLLWNN STIDLAIVKV DRTGLPAAEF GDSDDLIIGE PVVAIGNPLS LELDRTVTAG
     IISGLNRSIQ IDEYTVMEPL IQTDASINPG NSGGPLFNSE GLVIGINTAK MTSAEGLGFS
     IPINMAKGII DEVIENGEVT DVYLGIKGVD VSVYEKQLNV DLTPEYGVVV VEIFKDSPAQ
     TAGLMAGDVI QEIDGEEIDD MSDVQRQLFN YKPGDEVLMK VIRNGDAVDL ELVFQKKPDN
     FN
//