ID A0A0N0XXJ2_9ACTN Unreviewed; 1089 AA.
AC A0A0N0XXJ2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=ADL29_16170 {ECO:0000313|EMBL:KPC63298.1};
OS Streptomyces chattanoogensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66876 {ECO:0000313|EMBL:KPC63298.1, ECO:0000313|Proteomes:UP000037982};
RN [1] {ECO:0000313|Proteomes:UP000037982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5002 {ECO:0000313|Proteomes:UP000037982};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KPC63298.1}.
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DR EMBL; LGKG01000134; KPC63298.1; -; Genomic_DNA.
DR RefSeq; WP_053924391.1; NZ_LGKG01000134.1.
DR AlphaFoldDB; A0A0N0XXJ2; -.
DR PATRIC; fig|66876.3.peg.3548; -.
DR Proteomes; UP000037982; 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; 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:UP000037982};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 845..1037
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 531..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 745
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 968
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1026
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 969
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1089 AA; 118393 MW; B368A9B7D45A8FCF CRC64;
MRYPHLHGDL ICFAAEDDLW VAPLAPPGEE PGRAWRLTVD RTRVGHPRFS PDGRQIAFTT
WRSLDPEIHL APVEGGPARR LTYWGSTDAR VCGWTPPYQD GKPHILAVSS HGQPFSYYSW
AYSLPTDGSP GGRLPWGPVS DIAVADVDGE HCTLLLSGKP PHEPASWKRY RGGAMGRMWL
QGARMVPDLD GHLDSVMFVD GRIAFLSDHE GTANVYSCLP DSTDLRRHTD HADFYARHAS
TDGSRIVYQC AGDIWLIDGL SPGARPRKLA VRLGGPRAGR RTYQVPAAAH VTSLAVDATG
RASAVGVRGS LYWLTHRDGP ARTIHDVPGV RVRLPEMLGS TGRIAYVTDA EGEDAIEIVD
LPRAGAVHAP VRLAAGKLGR VHEMVPSPDG EQVAVAAHDG RLLLVDVHPP EDAEKTGPPG
EVTELIVSRN GPVRDLAFSP DSRWLTWSHP GIGRSLRQIK MARLADRSVV DVTNGRFEDE
QPVFTRDGRY LAFLSWRGFD PVYDVHTGDL SFPLGCRPHL VPLSSATPSP FALSPEGRPA
AGGLDPAENP PLGEGPVIVE VEGLENRVTP FPVTASKYSS LEPVAGGGLV WLRWPISGAL
GETFANPAET SGRPTLEHFD LVKARRSELT SSLDSFALSG DGTRLVVNDE GDLRAVPATE
PPDLDSTVLL DLRRILHDVE PPAEWRQAFD EAGRLIRAYF WEPGMCGIDW DGVLAQYRPL
VERVASPDEF ADLLREVLGE LGTSHAYVAP ARRNEGPPHY QRPIGLLGAN FYPRDGHWVV
QRILPGESSD PKARSPLAGT GIREGAALTH VDGRPVDPVA GPNPLLAAAG GTTVELTFAP
PEDDGHPRRV AIVPLIDERP LRYQDWVAKR RAVVRELSDG RCGYLHIPDM GGSGWAQFNR
DLRREMSMPA LIVDVRGNAG GNISELVIEK LTRTIMGWDL TRGAQPVSYT SNAPRGPVVA
VADEMTSSDG DMITAAFKLQ GIGPVVGMRT WGGVVGMTGR HRLADGTQIT VPMNAAWFHQ
YGWSVENHGV EVDIEALRSP LHWAEGKHPT LGVAVRTALE LLERHPASTP PDLSEVPDRA
RPELPPRDG
//
