ID B7C798_9FIRM Unreviewed; 374 AA.
AC B7C798;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Trypsin {ECO:0000313|EMBL:EEC91383.1};
GN ORFNames=EUBIFOR_00045 {ECO:0000313|EMBL:EEC91383.1};
OS Holdemanella biformis DSM 3989.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Holdemanella.
OX NCBI_TaxID=518637 {ECO:0000313|EMBL:EEC91383.1, ECO:0000313|Proteomes:UP000004315};
RN [1] {ECO:0000313|EMBL:EEC91383.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC91383.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEC91383.1, ECO:0000313|Proteomes:UP000004315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3989 {ECO:0000313|EMBL:EEC91383.1,
RC ECO:0000313|Proteomes:UP000004315};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium biforme (DSM 3989).";
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:EEC91383.1}.
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DR EMBL; ABYT01000005; EEC91383.1; -; Genomic_DNA.
DR RefSeq; WP_003863862.1; NZ_DS996837.1.
DR AlphaFoldDB; B7C798; -.
DR STRING; 518637.EUBIFOR_00045; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_0_0_9; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000004315; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 262..358
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 374 AA; 39198 MW; DD3E60AF863F2915 CRC64;
MQTPPKFKPK TYVPVRNKIL TTAGIILLSG IVGFGAGYAG SHLSNNANVT IQQQTNKSNS
GTIQVADVSD IVEKCKDSVV EITTESVSSG NSIFGQYVSQ GAGSGVIISE DGYIVTNNHV
VSGATSLKVT TTDGTEYDAS IIGTDSQTDL AVIKIEAQNL LAATLGDSDI LQVGDPAIAI
GNPLGELGGT VTTGIISATD RQITIDNETM TLLQTDAAIN PGNSGGGLFN ADGNLIGIVN
AKESSTGIEG LGFAIPITPA KDVITELMQN GSVTSRPALN VSLYDYTSSN QTQNSKYEDG
CYIVQIVKNG AADKAGLKQN DRIIRFDGEK IQSTSDVKAI LKKHKIGDNV KMVVDRDSKE
IEVEIVLQAQ TQAN
//
