ID A0A316TPY7_9BACT Unreviewed; 1075 AA.
AC A0A316TPY7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=DDZ15_11880 {ECO:0000313|EMBL:PWN05878.1};
OS Rhodohalobacter mucosus.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2079485 {ECO:0000313|EMBL:PWN05878.1, ECO:0000313|Proteomes:UP000245533};
RN [1] {ECO:0000313|EMBL:PWN05878.1, ECO:0000313|Proteomes:UP000245533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8A47 {ECO:0000313|EMBL:PWN05878.1,
RC ECO:0000313|Proteomes:UP000245533};
RA Liu Z.-W.;
RT "Rhodohalobacter halophilus gen. nov., sp. nov., a moderately halophilic
RT member of the family Balneolaceae.";
RL Submitted (MAY-2018) 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:PWN05878.1}.
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DR EMBL; QGGB01000008; PWN05878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TPY7; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000245533; 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; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; 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; 7.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 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:UP000245533};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1075
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016331131"
FT DOMAIN 701..768
FT /note="Tricorn protease C1"
FT /evidence="ECO:0000259|Pfam:PF14684"
FT DOMAIN 893..1045
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|Pfam:PF03572"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..588
FT /note="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 980
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1036
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 981
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1075 AA; 121753 MW; 627D4DFD31880900 CRC64;
MRTLLTILIA LVTYSISHAT DNPQWIRYQS ISPDGNTIVF TYKGDLYRVP SRGGVARQLT
FHEAHDYMPV WSSDGRHIAF ASDRYGNFDI FLMEAYGGPA TRLTYHSNDE SPFSFSADDE
NVIFGAVRQD RAEHRQFPTG SQPELYSVPV SGGRIGQIFT VPAEYVQVNG DGNRMIYHDK
KGGENEWRKH HTSSITRDIW MYDAATDEHS MLTSFEGEDR QPVFSPDEQS FYYLSEESGS
FNVHKMSISA APQNEQLTDF DLHPVRFLSH GNGTLAFGYD GELYTMREGE EPQKVNVVIR
TQTASNPDSY ITINGGVREM EISPNGKEIA FVARGEVFVT SVDGSLTKRI TNTPEQERFV
TFTPDGKGVV YASERNGRWS IFKTTKVRDD EPFFYASTLL SEEPVVMNDE DNYLPAYSPD
GEKLAYIADR RTLRIQDLES GDTTDLLTPD DLFHMRDGDK YFRWSPDSKW LLVDWSKKLH
NSEVLLMAAD GSERINLTES GYNDSSPKWM NDGKQMIWFT NRDGLRSYAT SGRTERDVYA
MFFSQEAWDM FNLSEEDYKL WKQIQEVSDA EDDENGDSDD EESEEDNAEE MVIDRRGMKD
RTARLTNHSS SLSDAVLSKD GSKLYYLSSF EDNYNLWETD LRTKDTKMLI RLNTGFGSLQ
WDPDMENLYL LSRGSISKLN LTGGSSTPVS IRGEMTYDAD AERLAMFEHV YIRTKNIFYE
PTFHGNDWDM LYEEYSKYVP HIGNSYEFAE MLSEMLGELN VSHAGARYNR SIDNADATAS
LGIFMDYDYE GDGIRIVEVL DGGPLDKAAF EVDSGMIIQR IDGEQITSDR DVASYLNRKA
GDFVLLDVTD GDGDNLQQIT VKPITLGQER SLLYQRYIRI NEEEVDEKSN GTLGYVHIPG
MGDGPFRYVI QEMLGKYPER DAVIVDTRFN GGGDLVADLA MFFTGVEFNT YATADMDVGG
EPTSRWTKPT LSLYNEAMYS DGHCYASAYS ELEIGLTVGM PVPGTCSFAG WEGLPDGTRW
GVVPVSARNM SGEWMENNQT EPMIRVKNDP EVISEGRDQQ LERAIEELMN QVSGE
//
