ID A0A1I1TAH1_9BACT Unreviewed; 1095 AA.
AC A0A1I1TAH1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05216167_105309 {ECO:0000313|EMBL:SFD52440.1};
OS Spirosoma endophyticum.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=662367 {ECO:0000313|EMBL:SFD52440.1, ECO:0000313|Proteomes:UP000198598};
RN [1] {ECO:0000313|EMBL:SFD52440.1, ECO:0000313|Proteomes:UP000198598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26130 {ECO:0000313|EMBL:SFD52440.1,
RC ECO:0000313|Proteomes:UP000198598};
RA de Groot N.N.;
RL Submitted (OCT-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; FOLQ01000005; SFD52440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1TAH1; -.
DR STRING; 662367.SAMN05216167_105309; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000198598; 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; 2.120.10.30; TolB, C-terminal domain; 3.
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; IPR024958; GRASP_PDZ.
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; PF04495; GRASP55_65; 1.
DR Pfam; PF07676; PD40; 6.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF75011; 3-carboxy-cis,cis-mucoante lactonizing enzyme; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 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:UP000198598};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1095
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011721594"
FT DOMAIN 781..837
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 770
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 991
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1047
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 992
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1095 AA; 119561 MW; E38A6F7756BC6B25 CRC64;
MHSSTTAALL RSLLLLAIAF PSQGQAQPAT PTPKFAFAEP SLSPDGAEVA FVSGGDIWTV
PTTGGEARLL VSHPDNESRP IYSPDGKYLA FASSRTGNGD IYLLTLETGA IKRLTYDDGG
EVLNGWARDG KMVYFQSTSR DISGMNDIYR VAITGGTPMA ITADRYANEF YGIPAPNGKT
LAFSARGIAS NQWWRKGRSH LDEAEIWLYH LDAKKGDSAY ERVTESGAKE LWPMWSQDGK
TIYYVSDRNQ TQNLWSQPLG GKPTMLTTFT NGRVLWPSIS YDGKTVVFER DFGLWKYDIA
SRQVAPISVR LRGVAASPAA EHLKLTNQFR EMALSPDGKK VAFIAHGDVF AASSKDGGEA
TRISSSAANE SQPVWAANSR SLVYVSTRDG VAHLYRYDFA TRDETKLTDN AQDDGSPVFS
PDGKLLAFVR NGQELRVLDL ASKKEKLLKK GYLGRPPFAT NGSVVWSPDG KWIAFASYGA
KTFRNVSVVP AAGGESKPVS FLANTFGGNL SWSPDGKYIL FTTNQRTETS QVARIDLVPR
APKFREDQFR DLFNEEIPKT LKPAPTTPTT TKTATRDTSA LGDTTAKLGR SGATKIVFDD
IRQRLSLLPV GVDVDAQSIS KDGKTLLLIA TVAGQQNLYT YSLDELGREQ SVARQLTSTP
GSKSGAQFSP DGKEIFYLEQ GKIQSITLDK REPKALAITA EMDVDFGDEK VQVFRQAWDI
QNKGFYDSTF HGVDWKAVRA SYEPLAAGAR TPDELRRLIS LMLGELNASH SGISAPAGSV
QTTTGRLGLR FDRAEYESTG KLKITEVIAL SPAALSGTIN VGDYLLAVDD TKISATTNLD
QLLENQINHR ISLMIASSPT APPQEVTVRP VSLATEKGLL YKQWVQQQRD YVNKVSKGRL
GYVHLFDMSA ESLAQLNIDL DADNHAREGV VVDVRNNNGG FVNAYALDVF TRKGYMTMTP
RGLPSAPART QLGQRSLETP TILVTNQHSL SDAEDFTEGY RTLKVGKVVG EPTGGWIIYT
SAAQLIDGSN VRLPFIKITD NMGKNMELAP RPVDIAVSRP IGESYTDKNS QLDTAVAELL
RELTEAKTSK LSTGK
//
