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Database: UniProt
Entry: A0A1N7LPI9_9BACT
LinkDB: A0A1N7LPI9_9BACT
Original site: A0A1N7LPI9_9BACT 
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
//
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