ID A0A2V2QEP3_9ACTN Unreviewed; 1152 AA.
AC A0A2V2QEP3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=DKT74_04815 {ECO:0000313|EMBL:PWS47527.1};
OS Streptomyces sp. ZEA17I.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS47527.1, ECO:0000313|Proteomes:UP000245984};
RN [1] {ECO:0000313|EMBL:PWS47527.1, ECO:0000313|Proteomes:UP000245984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZEA17I {ECO:0000313|EMBL:PWS47527.1,
RC ECO:0000313|Proteomes:UP000245984};
RA Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT "Genome sequencing and identification of chitinase family genes of
RT Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
RL Submitted (MAY-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:PWS47527.1}.
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; QGMS01000309; PWS47527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V2QEP3; -.
DR Proteomes; UP000245984; 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; cd00988; PDZ_CTP_protease; 1.
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; 2.
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; 2.
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; SSF69322; Tricorn protease domain 2; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
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}.
FT DOMAIN 908..1100
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 420..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 809
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1031
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1089
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 1032
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1152 AA; 124472 MW; C007CFB671A59930 CRC64;
MSDDVAYLRF PHLHQDMLCF AAEDDLWVAP LAPAGHRPGR AWRVTVDRTR VSHPRFSPDG
TSLAYTTWRT LDPEIHLAPV DGGPARRLTH WGSTDARVCG WTPDPPDASQ ILAVSSHNQP
FSYFSWAYSV PTDGSPGGRL PWGPVSDIAV ADLDGERRTL LLTGTPPHEP AAWKRYRGGA
MGRLWLHGER LLPDIDGHLA SPMFVGRRIA FLSDHEGVGN LYSCRTDGTD LRRHTDHDAF
YARHASSDGH RVVYQCAGDL WLVEDLDSPD ATPRKLEVRL GGPRTGRRCH QVPAASNVDS
LSVDETGRAS AVTVRGSLYW LTHRDGPART ISDTPGVRVR LPEMLGSGGR VAYVTDADGE
DAVEIGYLPR ASGDRAPRRL ASGQLGRVQE MVSDPDGERL AIASNDGRLL LLDTGEPEET
GAVATTGAAD GSGTAGVTEE TEEIRERPRT GSTRADLYAA TGGAVPDSIT ASVDEHPGLT
ELIRSVNGPV RDLAFSPDGS WLTWSHPGIG RSLRQIKLAR ISGPGAPVIV DVTNGRFEDE
NPVFTEDGRY LAFLSWRGFD PVYDVHTGDL SFPLGCRPYL VPLSSATPSP FALSPDGRPA
AGGLDPIDVP EAGGTGEGST VMVEFEGLES RVTPFPVSAS KYSALHPVSG GGLVWLRWPI
SGALGETFAN PADMSGRPTL EHFNIAKARK TELVDHLDWF AVSGDCSRLV VMDDGELRAV
PATEPGDGDS TVYLDLRRIL HEVDPGAEWR QAYGEAGRII RSYFWEPDMC GIDWDGVLEQ
YRPLVQRVSS PDEFADLLRE VLGELGTSHA YVTPARRNEG PPHYQRAIGL LGANLVCRDG
SWVVQRILPG DSSDSKARSP LAGTGIREGA VLTHVDGRPV DPVTGPYPLL TAAGGTTVEL
TFTPAGGGPS RRVAIMPLVD ERPLRYQDWV AKRRDVVREL SGGKCGYLHI PDMGGSGWAQ
FNRDLRLEVS RPALIVDVRG NAGGHISELV VEKLTRKILG WDLTRNAQAV SYASNAPRGP
VVALADEATS SDGDMITAAF RLLKLGPVVG QRTWGGVVGM TGRHRLGDGT VITVPMNAAW
FDTYGWSVEN HGVEPDVKAL RTPLDWAEGR YAVLDDAVRV ALDLLAAHPA STPPTYDTAP
DLRRPPLPPR SS
//
