ID A0A1U9NH69_9BACT Unreviewed; 1136 AA.
AC A0A1U9NH69;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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};
DE Flags: Precursor;
GN Name=tri1 {ECO:0000313|EMBL:AQT66950.1};
GN ORFNames=STSP2_00088 {ECO:0000313|EMBL:AQT66950.1};
OS Anaerohalosphaera lusitana.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Anaerohalosphaeraceae; Anaerohalosphaera.
OX NCBI_TaxID=1936003 {ECO:0000313|EMBL:AQT66950.1, ECO:0000313|Proteomes:UP000189674};
RN [1] {ECO:0000313|Proteomes:UP000189674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-NAGAB-D1 {ECO:0000313|Proteomes:UP000189674};
RA Spring S., Bunk B., Sproer C.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (FEB-2017) 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; CP019791; AQT66950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9NH69; -.
DR STRING; 1936003.STSP2_00088; -.
DR KEGG; alus:STSP2_00088; -.
DR OrthoDB; 269409at2; -.
DR Proteomes; UP000189674; 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; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR028204; Tricorn_C1.
DR InterPro; IPR012393; Tricorn_protease.
DR PANTHER; PTHR43253; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR PANTHER; PTHR43253:SF1; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR Pfam; PF07676; PD40; 3.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
DR PROSITE; PS50106; PDZ; 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:UP000189674};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 791..847
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 532..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..575
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..617
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 784
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1002
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1065
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ SEQUENCE 1136 AA; 130293 MW; C3C9003AA52939F2 CRC64;
MALSGRRVAF VVFAFAVVLL SAGICAAQPV KFARYPHTFE GKLAFTYHGD IWVANDDGSD
PYRLTNHMAR DIYPRFSPDG QWIAFSSNRM GNYDIYRVPV TGGEPEQLTF FSGIDVMANW
TPDGERIIFR TDRRGTWGTP LYTVGMDGEL PMPLNMDRGY HGMMSLDGKY LAFNRQSFRY
WRKHYKGNLS TDVWLQDLAT HEITQLTDTN LKNFREHRQD VYPMWGADGM IYFMSERDDT
YNIWKISLEG GDPVQVTKHD KDGIQYPAMS PDGKTLTYEC NFQIWKLDIE SGSTEQVHVD
LGFDPKENLI EFDHVNSQAD GFAPSPKGDY TAVDYHGEIF IVPTDQEVGE KKRVTRSPWR
DRNEKYSPDG KYLAFMSDET GEEELWIYET ETGTTRQLTD QETLKRGYMW SPDSKQIALV
GSNRLFIVDV EQSTVEEVGH NSAYGYYLND WSKDGKWLIY TRWRDDYNQD LYLFNIETRE
EYNISQNPFY DGDGKFSEDE KKVVFRSTRN GDRARVFVVS LAKVTVDRDD PLWREREKNG
ENGKEKKEED EQQEDAPDEP EEDDEKKDDE DEQAAVTDDG GKAQPEDEKE QAEADDSDEG
EEAAEADEAE EEEPTLVIDL DGIERRAEQI SDNCYDVDNL FVKGDKVYFT GRDGSGSGFF
SLKLNGEGER KIAGGSFHNI TPTADKSNVF YKSGNHVYKM RIGSSRGSRV NFSFTVEIDK
PKEWAQILNE AWRVMKYHFY DENMHGYDWD AIRAKYTPLL DYVGSYGEVY ELANEMIGEL
NASHCGVSGP EKRMPNAYNS AILGFEMIPD GDYYKVDHIY REGPADKEWV ELEKGDYVLA
IDGVDVRAGE NYWKILNRTL NDYVTVKVSD DPASGETRDV RIDSTSTGAL GNIKYEEWVE
SNRDYVEKIS DGKIAYVHIK SMNRSCLERF TQEIRRFYDY EGIVVDIRYN GGGNIDQQLL
DILSRRAYQY WTNRWAAPEM GRRHRESIVG PKVMLINWGS ASNSEVTPLG FRDLELGKIV
GNPTAGAVIA TGSYRLINGA RIRTPGGLVV RYNPLRENNY GLNLENYGVA PDIWVENTPE
DRMKGYDREL TVAAETAMDM LREREEKITE MKEAERKKGV EHVRYINSNH ESEDDG
//
