ID A0A1M7LM90_9FLAO Unreviewed; 1053 AA.
AC A0A1M7LM90;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=SAMN05720268_0562 {ECO:0000313|EMBL:SHM79156.1};
OS Polaribacter sp. KT 15.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1896175 {ECO:0000313|EMBL:SHM79156.1, ECO:0000313|Proteomes:UP000190644};
RN [1] {ECO:0000313|EMBL:SHM79156.1, ECO:0000313|Proteomes:UP000190644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT 15 {ECO:0000313|EMBL:SHM79156.1,
RC ECO:0000313|Proteomes:UP000190644};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT670850; SHM79156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7LM90; -.
DR Proteomes; UP000190644; Chromosome i.
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; cd00987; PDZ_serine_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; 2.
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; IPR029414; Tricorn_PDZ.
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; 4.
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; SM00228; PDZ; 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; SSF69322; Tricorn protease domain 2; 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 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..1053
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012884382"
FT DOMAIN 750..820
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 733
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 960
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1016
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ SEQUENCE 1053 AA; 118526 MW; 8ED291408E599699 CRC64;
MTKKTILIIA FLCNLTLLSA QNTLIRTPTI SPDASKMAFG YHGDIWVLDL NTNQKNRLTI
NQAYESNPIW NFKSNEIVFM SNRKGSRNIF KTDLNGGIPN QLTFYPTTDT PSQWQENGDI
IFSSNRIFKG TERESSIYKI NEKGETPTRF MTALGSQASV SPNGKLVAFV KGTCRISRED
YNGPAQRDVW IYNIKTKGYH QITTSKKNDH TPLWDANNNL YYISAQSGRY NIYKTTLNEN
GSKLGVENQL TNLKVDGVLS FSVSNNGTII YNSGIEVFKM LNGKTTKINL NLATDNRFNL
EETKTVTDGI RDLSVSPNGK LIALSINGEI FVKENNKDKT KTNNVSNHPY KDDNPFWIDN
NTLGFLSDRS GQNELYKVVS TDENVNLHRS LKTKVTQLTN SKIDVFEPIL SPNRKKLAYR
IGRGQLVIAD VINGKLSKPK SYSDTWAAAN SVAWSPDSKF ISYSQSDLNF DSEIYIQSVE
NPSNKMNVSM HPRSDSNPVW SPDGKKLSFV SNRAGDRGGI NYDTWMVWLQ KSDWEKTKSD
YKEGDYYQPK TEKKKDKKEV VVKIDEDKIY DRLVQLTSWA GNEYGAIFSA DSKSIYISAT
NPATRKNGYY KVDLLGGTPK EIKGVTYLGG NSLNKETLYY SSRGKLKSLN LKTDKVSSFL
HAATYTVDNY KLNEQVFYEG VRAITAGFYD PQYHGYNWDK IVKRYTPWVL SAATKQDYTF
MYNNMLGQLN ASHMGYRGSS PEEVSSDRVG LLGLAVSNVN NGVKIDYILP NSAATKTNVS
LNIGDVITAV NGKKINKNTN FYSVLRNTSG NEILLTLADK KEVVVRTEST RTISGLRYEE
WINSRKKLVE KYSNGQLGYI HIQGMNLPSF ERFERELKAS GYGKKGIVID VRNNGGGWTT
DRLLAVLTYQ QHAYTVPRDA TGNLQKNNLK YKENYPFNER AVLSVNTKPL VALSNQSSYS
NAEIFAHAFK SLKLGKLVGQ PTFGAVISTG SHRLQDGAIR MPYRAWYVKE SGLNMEHGPA
VPDVLVENKP GWKARNEDDQ LKKAVEVLLQ DLK
//
