ID A0A1N7LPI9_9BACT Unreviewed; 1080 AA.
AC A0A1N7LPI9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=SAMN05421761_10410 {ECO:0000313|EMBL:SIS75773.1};
OS Belliella pelovolcani.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=529505 {ECO:0000313|EMBL:SIS75773.1, ECO:0000313|Proteomes:UP000186026};
RN [1] {ECO:0000313|EMBL:SIS75773.1, ECO:0000313|Proteomes:UP000186026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46698 {ECO:0000313|EMBL:SIS75773.1,
RC ECO:0000313|Proteomes:UP000186026};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Degrades oligopeptides. {ECO:0000256|PIRNR:PIRNR036421}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR036421}.
CC -!- SIMILARITY: Belongs to the peptidase S41B family.
CC {ECO:0000256|ARBA:ARBA00008524, ECO:0000256|PIRNR:PIRNR036421}.
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DR EMBL; FTOP01000004; SIS75773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7LPI9; -.
DR STRING; 529505.SAMN05421761_10410; -.
DR Proteomes; UP000186026; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd07562; Peptidase_S41_TRI; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR028204; Tricorn_C1.
DR InterPro; IPR029414; Tricorn_PDZ.
DR InterPro; IPR012393; Tricorn_protease.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43253; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR PANTHER; PTHR43253:SF1; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR Pfam; PF07676; PD40; 4.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR036421};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036421};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR036421};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1080
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012636646"
FT DOMAIN 837..1031
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 537..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 738
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 962
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1020
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ SEQUENCE 1080 AA; 121598 MW; D8BDD4795606FEB9 CRC64;
MIKKYIPMLL LILLSDLAMA QGTRLLREPT ISKDYIVFVY ANDLWRVSKS GGDAIRLTSN
EGAENRPHFS PDGKHIAFTA QYDGNTDVYV IPVEGGEPRR LTWHPGPDIA AGWTPDGKEV
LFNSSRANVP TKESKFYTIP LEGGMEKELP IPRAVNGRLS ADAKHIAYQQ IAFWDPEWRN
YRGGQAKPIW IVNMDDYSLQ MTPQTDNERH TMPVWHGSKV FFLSELDYAN NIWSYDPESK
DLKQETFHTD FDIKNLDSNG SEVVYEQGGY LHILTPANGQ TKQLEVNVRG DFHWARERWE
SVSGSRLSNP AISPSGQRAL FEYRGEIITV PKDKGDARNL TQSSRIAERS PVWSPDGQQI
AWFSDESGEY HLMIGDQEGL TQPKKIELPT KTFYFKPEWS PDGKFIAYTD TDYNLWFVNV
ASGVAKIADT DRFAHPNRSL NPVWSPDSKW VAYARLLDSQ FKAIFVYNIE TGKKIQVTDG
MADAISPIWD ANGEYLYYLA STNFGLNTGW LDMSSYDRPT TRGLYVTVLS KNGVTPFLPE
SDEEKPKSEA KTDEKKNGTK AVVIDEEGLW DRIVAVDIPI RDYPALVMGP EQTVFYMESI
PNQRGLTLHK YNFKDKKSDV FMTGVSNAVV SLDRKSMLYQ ANGNWGIVDT NGNGKKPGDG
ALKAISSLQV KINPKEEWEQ IYREGWRYQR DFLYVDNVHG APWDEIYEWY KPWVDHVRHR
SDMNYVIDIL GGEVAVGHSY TSGGDFPSVK SVSIGLLGAD YEVHQGKVRI KKIYNGENWN
PNLTAPLAHP GLKISEGDYI LEVNGVAVDS QVNFYSYFEG MANKQVKLKV NDKPDVAGAR
SITVVAIANE SGLRNIDWVE GNRRKVDELS NGQLAYVYVP NTGQPGYTSF NRYYFAQQDK
KGAVIDERNN GGGSAADYMV DIMARQLHGY FNSRANDRKP FTTPMAGIWG PKVMLINERA
GSGGDLLPYL FSKMEIGPLI GTQTWGGLVG TWDTPSFIDG GRMVAPRGGF FDVDGEWAVE
AVGVAPDIKI EQTPKDVIEG RDPQLERAVQ EALKLMETES IELKPEPKAP IRYFRPEKKN
//