ID A0A0C5WFZ5_9FLAO Unreviewed; 1074 AA.
AC A0A0C5WFZ5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=AW14_11090 {ECO:0000313|EMBL:AJR04104.1};
OS Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Siansivirga.
OX NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR04104.1, ECO:0000313|Proteomes:UP000032229};
RN [1] {ECO:0000313|EMBL:AJR04104.1, ECO:0000313|Proteomes:UP000032229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR04104.1,
RC ECO:0000313|Proteomes:UP000032229};
RA Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL Submitted (FEB-2014) 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; CP007202; AJR04104.1; -; Genomic_DNA.
DR RefSeq; WP_052647484.1; NZ_CP007202.1.
DR AlphaFoldDB; A0A0C5WFZ5; -.
DR STRING; 1454006.AW14_11090; -.
DR KEGG; sze:AW14_11090; -.
DR PATRIC; fig|1454006.5.peg.2198; -.
DR HOGENOM; CLU_005503_0_0_10; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000032229; 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; 6.
DR Pfam; PF13180; PDZ_2; 1.
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; 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:UP000032229};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1074
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002184354"
FT DOMAIN 758..814
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 538..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 749
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 979
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"
SQ SEQUENCE 1074 AA; 120428 MW; C0CEC3572873ED81 CRC64;
MKLTLRLLFL SLFLSFTNGF AQNPLIHSPA VSPDGKLIAF NYQGDIWTAN ADGSNAKRIT
IHEGYDTNPM WSKDGKTIAF ESNRFGNSDI FLVPFQGGLP KRLTYHSAGD YITDYTDNGD
ILFSTRRDFA QVERESEVFI VNEKGGTPYR FLSSLGFDAT LSPNGKFIAF TKGSCRIARE
AYRGPAQRDI WLYDIKKDSY TQLTTYDGND FSPKWANNNT IYFQSSRSGK YNVHKLSIND
SGAKIGSVSQ VTSLNKFGLF SFNLSKNGND LIAVSGDEVY MYNIATASLK EVKINIGSDY
RFDPIVHKQY SSGINSVAVS ANGKYSALEI RGEIFLTEND KDRRKTVNVS TSAYRDRMPT
WVNDSTLLFV SDRDGQYDFY LLKSDDPKES NLFKTLKHKV IRLTKTSENE TDPVISPDGN
LIAYQRGRGE LVVASINGDK LSNEKVLLNG WSSPSNIAWS PDSIWLSYGL PDLEFNDEIY
IHKADNSMKP VNVSMHPKQD RGAIWSPDGK KLIFSSDRSN GDFDVWFVWL NKKDWQKTPQ
DWEEEASEEN KSKDKKSDKK DDKKKDAVEP ITIDFDNIYE RQVQVTNFIG GELACGVTKD
GETIYYVTGN VSRTDAEMNS DLYKIKWNGK DKKEITSGNS RPSNISQTKD YSHLYLTKSG
TLNKLNLAGD KMESLPVAAK MDVDYITETN QIFEEAWKAI NDGFYDPNFH GQDWGKLKEK
YKPLALKAST RDDFQYIFNL MLGQINASHM GLNGGENRED LQAERTGLLG VELKPQSNGS
LVVTAVTSDM PADREVSKLN TGDIITAVNG VELSANTNVY SLFEGTANDK IYLSVTSNGA
SKEVFIRPQT SNRNENYYAW VKEQKQLTEK YSGGKLGYIH IQGMDWTSFE TFERELTAAG
LGKEGIVIDV RFNGGGWTTD YLMAVLTVKQ HAYTVPRGAT NNLERDHTKF KDHYPYSERL
PLAAWTKPSI ALCNETSYSN AEIFSHAYKS LGIGTLVGVP TFGAVISTGA TRLIDGSFVR
MPFRGWYVKS TEKNMELGPA VPDVIVYNNP DDKAKASDSQ LKKAVEILLS QLKK
//
