ID A0A1D7VW34_9ACTN Unreviewed; 1120 AA.
AC A0A1D7VW34;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=SL103_03465 {ECO:0000313|EMBL:AOP50957.1};
OS Streptomyces lydicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=47763 {ECO:0000313|EMBL:AOP50957.1, ECO:0000313|Proteomes:UP000094094};
RN [1] {ECO:0000313|EMBL:AOP50957.1, ECO:0000313|Proteomes:UP000094094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=103 {ECO:0000313|EMBL:AOP50957.1,
RC ECO:0000313|Proteomes:UP000094094};
RA Jia N., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Complete genome sequencing of Streptomyces lydicus 103 and metabolic
RT pathways analysis of antibiotic biosynthesis.";
RL Submitted (SEP-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; CP017157; AOP50957.1; -; Genomic_DNA.
DR RefSeq; WP_069573349.1; NZ_CP017157.1.
DR AlphaFoldDB; A0A1D7VW34; -.
DR KEGG; slc:SL103_03465; -.
DR OrthoDB; 9758793at2; -.
DR Proteomes; UP000094094; Chromosome.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000094094};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 867..1059
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 422..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 767
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 990
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1048
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 991
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1120 AA; 121595 MW; C4CD6FEAEFA52CC7 CRC64;
MPTTPPAPPG GYLRFPHLHG ELLCFAAEDD LWVAPLAPDG QEPGRAWRLT VDRTRVGHPR
FSPDGRHIAF TTWRSLDPEV HLAPVEGGPA RRLTYWGSTD ARVCGWTPPD HEGASHVLAV
SSHGQPFSYY SWAYSVPTDG SPGGKLPWGP VADIAVSEVD GERRTLLLTG KPPHEPASWK
RYRGGAMGRM WLHGTRLLPE LYGHLDSVMF VGGRIAFLSD HEGIANVYSC LPDGTDLRRH
TDHADFYARH ASTDGERIVY QCAGDLWLVD DLGPDAVPRK LAVRLGGPRA GRRTYQVPAA
SHVTSLAVDT TGRASAIGVR GSLYWLTHRD GPARTIHDTP GVRVRLPEML GSTGRIAYVT
DAEGDDSVEI TNLPRASAPG EPRRLAVGQL GRVHEMASSP DGERLAVASN DGRLLLVDVT
RPDEEPTEED RSAEEQAAGP GGVTELIRST NGPVRDLAFS PDSRWLTWSH PGIGRSLRLI
KMARLSDRHV VDVTNGRFED EQPVFTRDGR YLAFLSWRGF DPVYDVHTGD LSFPLGCRPY
LVPLSSATPS PFALSPEGRP AAGGLDPDEN PPPGGEGPVL VEVEGLENRV TPFPVAASKY
SSLQPVSGGG LVWLRWPISG ALGETFANPD NTSGKPTLEH FDLTKARRTE LTSSLDGFAV
SRDATRLVVN DEGELRAVPA TEPGDSDSTV YLDLRRILHD VDPGAEWRQG FEEAGRIIRA
YFWDPRLSGI DWDAILAQYR PLVERVASPD EFADLLREVM GELGTSHAYV TGARRNEGPP
HYQRAIGLLG ANLVQRDGRW ILQRILPGES SDSKARSPLA GTGIREESAL THVDGRPVDP
VTGPAPLLAA AGGTTVELTF APADGDGPAR RVAVVPLIDE RPLRYQDWVA RRRAVVRELS
GGRCGYLHIP DMGGSGWAQF NRDLRKEVAR PALIVDVRGN AGGNISELVI EKLTRTIIGW
DLTRDAEPVS YAGNAPRGPV VAVADEMTSS DGDMITAAFK LLGIGPVVGM RTWGGVVGMT
GRHRLADGTA ITVPMNAAWF RLYGWDVENH GVEPDIETLR SPMHWAEGRH PTLGVAVRTA
LELLERHPAA TPPDLSDVPD RRRPPLPPRN AGEEEGAEGA
//
