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Database: UniProt
Entry: A0A1C5EE20_9ACTN
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ID   A0A1C5EE20_9ACTN        Unreviewed;      1096 AA.
AC   A0A1C5EE20;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE            EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN   ORFNames=GA0115254_125914 {ECO:0000313|EMBL:SCF93479.1};
OS   Streptomyces sp. Ncost-T10-10d.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839774 {ECO:0000313|EMBL:SCF93479.1, ECO:0000313|Proteomes:UP000198750};
RN   [1] {ECO:0000313|Proteomes:UP000198750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ncost-T10-10d {ECO:0000313|Proteomes:UP000198750};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-2016) 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; FMDF01000214; SCF93479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5EE20; -.
DR   OrthoDB; 9758793at2; -.
DR   Proteomes; UP000198750; 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; 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; 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; 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:UP000198750};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|PIRNR:PIRNR036421}.
FT   DOMAIN          854..1046
FT                   /note="Tail specific protease"
FT                   /evidence="ECO:0000259|SMART:SM00245"
FT   ACT_SITE        754
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT   ACT_SITE        977
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT   ACT_SITE        1035
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT   SITE            978
FT                   /note="Transition state stabilizer; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ   SEQUENCE   1096 AA;  118961 MW;  0EE1E0DA87B1E32E CRC64;
     MSDDVAYLRF PHLHEDLLCF AAEDDLWVAP LAAEGQRPGR AWRLTVDRTR VSHPRFSPDG
     SRIAFTTWRS LDPEIHLAPV EGGPARRLTY WGSTDARVCG WTPDPPDASQ ILAVSSHNQP
     FSHVSWAYTV PTDGSPGGKL PWGPVSDIAV ADIDGERRTL LLTGKPPHEP ASWKRYRGGA
     MGRLWLHGER LLPDIGGHLD SPMFVGGRIA FLSDHEGVGN LYSCLPDGSD LRRHTDHDAF
     YARHASSDGS RIVYQCAGDV WLVDDLESPD AVSRKLEVRL GGPRAGRRTY QVSAASNVDS
     LSVDETGRAS AVSVRGSLYW LTHRDGPART IADTPGVRVR LPEMLGSGGQ VAYVTDADGE
     DAIEIAYLPR ASGDREPRRL ASGRIGRVHE LISDPDGERL AIATNDGRLL LLDTDEESTG
     EPTELIRSVN GPVRDMAFSP DGAWLTWSHP GIGRSLRQIK LARILGSGAP VIVDVTNGRF
     EDENPVFTGD GRYLAFLSWR GFDPVYDVHT GDLSFPLGCR PYLVPLSSAT PSPFALSPEG
     RPAAGGLDPA DDVVVEAGTG EGPSTVTVEF EGLESRVTPF PVSASKYSAL RPVSGGGLVW
     LRWPISGALG ETFANPADMS GRPTLEHFNI SKARKTELVG HLDWFAVSGD ATRLVVMDEG
     ELRAVPATET GDSDSTVYID LRRILHEVDP GAEWRQAYGE GGRIIRAYFW EPDMCGIDWD
     GVLDQYRPLV ERVASPDEFA DLMREVLGEL GTSHAYVAPA RRNEGPPHYQ RAIGLLGANL
     VCRDGDWTIR RILPGDSSDS KARSPLAGTG IREGAVLTHV DGRPVDPVTG PYPLLAAAGG
     TTVELTFRPS GGEGHSRRVA IVPLVDERPL RYQDWVAKRR EVVRELSGGK CGYLHIPDMG
     GSGWAQFNRD LRGEVSRPAL IVDVRGNAGG HISELVVEKL TRTILGWDLT RNAQPVSYAS
     NAPRGPVVAL ADEATSSDGD MITAVFRLLK LGPVVGQRTW GGVVGMTGRH RLGDGTVITV
     PMNAAWFDAY GWSVENYGVE PDLEALRTPL DWAEGRYAVL DDGVRVALDL LAAHPAATPP
     TYDDVPDRRR PPLPPR
//
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