ID A0A1I7L084_9FIRM Unreviewed; 510 AA.
AC A0A1I7L084;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Serine protease Do {ECO:0000313|EMBL:SFV02984.1};
GN ORFNames=SAMN02910342_03080 {ECO:0000313|EMBL:SFV02984.1};
OS Butyrivibrio sp. INlla21.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520811 {ECO:0000313|EMBL:SFV02984.1, ECO:0000313|Proteomes:UP000198910};
RN [1] {ECO:0000313|EMBL:SFV02984.1, ECO:0000313|Proteomes:UP000198910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INlla21 {ECO:0000313|EMBL:SFV02984.1,
RC ECO:0000313|Proteomes:UP000198910};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; FPCC01000042; SFV02984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7L084; -.
DR STRING; 1520811.SAMN02910342_03080; -.
DR Proteomes; UP000198910; 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; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFV02984.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SFV02984.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 81..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 381..470
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 53903 MW; 0E814BCD78BC3B9E CRC64;
MYEDEKKSYN NSGYGQNSNY SGYSYENNSS SYNSNPYSQG QSSYGYGSNS QGYGTYQYST
NQNANNQPPQ PPKKKKKVGP IVALVLVVLL LVGGAGFAAF RIFNGLGLPG GSQQSVAQVE
EKEDQSATEN SAAGTQEEKK DDQKVQTTTT TAGETRVVVT DVTGVVEEVM PAMVMIHNNF
TQSANFFGYV QQEEAQASGS GIIVGHNDTE LLIATNYHVI DGADSLEVIF NDDTSVGAAV
KGTNSDMDLA VIAIMLDEIP ENTLNAIKEA KLGDSNALKL GEPAIAIGNA LGYGQSVTTG
VISALNREVE TQQGGDKHTF IQTDAAINPG NSGGALLNLN GEVIGINSNK LGGNVIEGMG
YAIPISDAKP IIDQLMNEET KIKVAEEERG YIGIQGYSVP SDVTESFGIP QGAYVDKITP
GGGAEAAGLV KGDVIVKFEG HDITSMDDLQ TRLQYYKAGT TVKLGIMRTD GSEYKETEVE
LTLGKAPSSD DSKAASNEKD DASSEGSSDN
//
