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Database: UniProt
Entry: A0A1I6KS66_9FIRM
LinkDB: A0A1I6KS66_9FIRM
Original site: A0A1I6KS66_9FIRM 
ID   A0A1I6KS66_9FIRM        Unreviewed;       527 AA.
AC   A0A1I6KS66;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Serine protease Do {ECO:0000313|EMBL:SFR94072.1};
GN   ORFNames=SAMN05661086_02650 {ECO:0000313|EMBL:SFR94072.1};
OS   Anaeromicropila populeti.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaeromicropila.
OX   NCBI_TaxID=37658 {ECO:0000313|EMBL:SFR94072.1, ECO:0000313|Proteomes:UP000199659};
RN   [1] {ECO:0000313|EMBL:SFR94072.1, ECO:0000313|Proteomes:UP000199659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=743A {ECO:0000313|EMBL:SFR94072.1,
RC   ECO:0000313|Proteomes:UP000199659};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOYZ01000010; SFR94072.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6KS66; -.
DR   STRING; 37658.SAMN05661086_02650; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000199659; 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; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFR94072.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199659};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        136..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          417..506
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          167..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  55658 MW;  53CFA54B4C89E182 CRC64;
     MYNPDDFSNG SGNQDGVNGG DGFEYKVNDV NVVNGKTPEE MAEINHVIHR EMETGYGDSY
     GGKTESLNNN YGTNNYGNNQ HYQNSNNGTT AMLDQGLSNL GNRGAVQNAP MQNGAYYGNA
     VPVPPKKKKA GGGKTFLMVA AIVITICFFG GAGIFGVHLI SEKLNGSQHS GNNTQESLDV
     ADDSDENTIN STESASITED SVSQVVKNVM PAIVSINTTS LEAYDFFGTE YTQPVTGSGS
     GIIIGQNETE VLIATNNHVV AGENPEVKVT FCDDETVTAT IKGTDTTSDL AVIAVLFKDL
     KDSTKESILV ATTGDSDSLQ VGEKVIAIGN ALGYGQSVTV GYVSAKDREV SMEDASMTLL
     QTDAAINPGN SGGALLNAKG EVIGINSVKY ALTEVEGMCF AIPISTAIPI INDLMTRDQL
     DESQQAYLGI IGKDVSEEDS QRIDIPIGIY VNEVTNGSPA DMAGLEAGNV IIGMDGKTIA
     TNEDLKNILS YTRAGTTVDL VVKERRNGKW VEKTLSVTLG SKADANN
//
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