ID A0A402B7S5_9CHLR Unreviewed; 1089 AA.
AC A0A402B7S5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN Name=tri1_1 {ECO:0000313|EMBL:GCE27453.1};
GN ORFNames=KDA_29370 {ECO:0000313|EMBL:GCE27453.1};
OS Dictyobacter alpinus.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=2014873 {ECO:0000313|EMBL:GCE27453.1, ECO:0000313|Proteomes:UP000287171};
RN [1] {ECO:0000313|Proteomes:UP000287171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno16 {ECO:0000313|Proteomes:UP000287171};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-2018) 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}.
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:GCE27453.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BIFT01000001; GCE27453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402B7S5; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000287171; 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; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000287171};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 852..1045
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 513..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 753
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 976
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1034
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 977
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1089 AA; 122506 MW; 6C7F4FA7F710F814 CRC64;
MPSQGYVRFP NIFQDRIVFV AEDDLWLVSS EGGRAERLTA GVGEVRYPHF SPDGELLAFV
GREEGPSEVY VMPAEGGPAQ RLTFQAGNCR VLGWSPDGTE ILYSSNSGQF AGRFEVIYAV
KPDGGEPRQL PMGMANDISY SSDGGVVIGR NINIREFSHW KRYRGGTAGH LWCDREGKGS
FTRLLQLNGN VADPCWIGER IYFLSDHEGV GNIYSCTPDG EDLRQHTQHT DFYARHLSSD
GKRLVYHSGA DLYLFDPQSE QLTHLEISLP SIRTQRSRKF VPAANYMDTY ALHPQGHMLA
LTARGKAFTL GNWEGPVLQY GEPDGVRYRY LEWLSDGKRL VAIHDAPGHE ELIIFTPDAS
TEPQTFPEIE FGRVTNLVVS PTENAVAISN HRNELILVNL DKSTAQVLDR SDAGKIQGID
WSPDGAWVAY GFALTANKVA IKLCQIASGE THQVTNPILE DTRPSFDPEG KYLYFLGQRI
FNPVYDNLHF DLGFPRGVKP YALMLRKDLR SPFIPETKNP DEKEKEKEES REKQARDDTE
ISQNGNEEGK EKKEESGKQT PAITIDLDGI SERILPFPVA EGRYASVRGI KGKVLFLSRP
VEGSIQHNSN SRGTLEYYDF DTYKTEKLFD GVGSFDLARD GKMLVYSANH RLRVVKAGEK
LKPEANNNDR PSRESGWIDF QRIKISVQPS AEWKQMFAEA WRLQREQFWA EDMSGIDWEG
IYKQYAPLVE RVSSRSELSD LLWELHGELG TSHAYEMGGD TRHGPHYRQG FLGVDWSYDA
EQERYRIARI LKGDPSESQT TSPFTSPGLN VNVNDAVLAI NGQRVGPARG PQELLVNLAG
QEVQLTIEDA ESKETRVVVV KALANETPAR YREWVESNRR RVHEVSDNRV GYIHIPDMGG
NGYAEFHRGF LSEYDYPALL VDVRWNGGGH VSGLLLEKLA RRRIGYDFPR WGQPESYPSE
APRGPMVALT NEHAGSDGDI FSHSFKLMGL GPLIGKRTWG GVIGINPSHK LVDGTVTTQP
EYSFWFKDVG WNVENYGTDP DIEIDIAPQD FVQQLDPQLD RAIAECLRLV EEYPTLEPKP
GERPRLGRL
//
