ID A0A0N0MXI4_9ACTN Unreviewed; 1093 AA.
AC A0A0N0MXI4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=OK006_4271 {ECO:0000313|EMBL:KPI11391.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI11391.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI11391.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI11391.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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:KPI11391.1}.
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DR EMBL; LJCU01000165; KPI11391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0MXI4; -.
DR PATRIC; fig|1592326.3.peg.5288; -.
DR Proteomes; UP000037912; 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; 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 Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 849..1054
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 236..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 763
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 985
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1043
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 986
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1093 AA; 117391 MW; DA9DA89FDB7F6D70 CRC64;
MTQSASSASS VSPAYLRFPH LHGELVAFTA EDDVWVAPLD GGGRAWRVSA DNMPVNHPRF
SPDGTTVAWT STRDGAPEVH AAPLEGGPST RLTYWGSSKT QVRGWTPDGR VLALSTQGQA
SLRRTWARAV PLDGGPATTL PYGPVGDVVH GDPGVLLLSA PMGREAAWWK RYRGGTAGKL
WIDRAGGDGA GAGEFVRLHE DLDGNLEYPL WVGERVAFLS DHEGVGALYS SLADGSDLRR
HTPGGGTSRS SEAESGGGFY ARHAATDGAR VVYASAGELW LLDDLDGAEP RRLDLRLGGQ
RVDQQPHLVS ASRWFSAAAP DHTGRGSAVS VRGAVHWVTH RSGPARALAA RPGVRARLPR
AFRVEGEEYV VWVTDAAGDD ALEFAPATGL APGATPRRLA AGQLGRVLGL AMAPDGSRAA
VASHDGRVLL VERETGEVRE VDRSEDGEVS GLVFSPDSAW LAWSHPGPRP LCQLKLANTA
DLSVTEATPL RFRDYAPAFT LDGKHLAFLS ARSFDPVYDE HVFDLAFVGG SRPYLITLAA
TTPSPFGPQR HGRPFEAPDK DETPDSEGAP TTRIDLDGLA DRIVPFPVEA ARYSTLRAAK
DGLLWLRHPV VGVLGASRAT PDDPDPKTEL ERYDLAQQRV EHLAADADHF AVSGDGKRVL
LWTDGKLKVV PSDRRASNDD ESDTNITVDL SRVRQTVDPA AEWRQMYDET GRLMRDNFWR
PDLGGVDWEG VLERYRPVLE RVATHDDLVD LLWEVQGELG TSHAYVTPRG GWGGGDRAQG
LLGADISRHE DGSWRIDRIL PSETSDPDAR APLAAPGVAV RAGDAIVAVA GQPVDPVAGP
GPLLVGTAGK PVELTISPSG GGDPRHAVVV PLADEEPLRY HAWVADRRAY VHEKSGGRLG
YLHVPDMQAP GWAQIHRDLR VEVAREGLVV DVRENRGGHT SQLVVEKLAR RIVGWDLPRG
MRPYSYPEDA PRGPVVAVAN EFSGSDGDIV NAAIKALGIG PVVGTRTWGG VIGIDSRYRL
VDGTLVTQPK YAFWLDGYGW GVENHGVDPD VEVVQTPQDY AAGRDAQLDE AIRIALAALA
ENPAKAAPTL PEL
//
