ID A0A0K0XW07_9GAMM Unreviewed; 1091 AA.
AC A0A0K0XW07;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=HNQ63_000781 {ECO:0000313|EMBL:MBB6086344.1}, WM2015_1519
GN {ECO:0000313|EMBL:AKS41889.1};
OS Wenzhouxiangella marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Wenzhouxiangellaceae; Wenzhouxiangella.
OX NCBI_TaxID=1579979 {ECO:0000313|EMBL:AKS41889.1, ECO:0000313|Proteomes:UP000066624};
RN [1] {ECO:0000313|EMBL:AKS41889.1, ECO:0000313|Proteomes:UP000066624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42284 {ECO:0000313|EMBL:AKS41889.1,
RC ECO:0000313|Proteomes:UP000066624};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6086344.1, ECO:0000313|Proteomes:UP000581413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103414 {ECO:0000313|EMBL:MBB6086344.1,
RC ECO:0000313|Proteomes:UP000581413};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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; CP012154; AKS41889.1; -; Genomic_DNA.
DR EMBL; JACHIC010000001; MBB6086344.1; -; Genomic_DNA.
DR RefSeq; WP_049725495.1; NZ_JACHIC010000001.1.
DR AlphaFoldDB; A0A0K0XW07; -.
DR STRING; 1579979.WM2015_1519; -.
DR KEGG; wma:WM2015_1519; -.
DR OrthoDB; 9758793at2; -.
DR Proteomes; UP000066624; Chromosome.
DR Proteomes; UP000581413; 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; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
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; IPR029414; Tricorn_PDZ.
DR InterPro; IPR012393; Tricorn_protease.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
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 Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 2.
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:UP000066624};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1091
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005454348"
FT DOMAIN 857..1048
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 545..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 756
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 1037
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 980
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1091 AA; 121144 MW; C338E190EFAB866C CRC64;
MLQSQFLPRL LALTALLLAA SSAAANTKLL RFPDVHGDRV VFSYGGDLWG APVQGGTAYR
LTSHPGLELF AKFSPDGRWI AFTGQYGGDE QVYVMPASGG EPRQLTWYPA TGPLPARWGY
DHQVYGWTPD GSAVLFRSQR DAWGSSSSTL YTVPVDGGLP EAMPMPVSGA GTFTEDGSAV
FYSPLFRDFR TWKRYEGGWA QDLWLFDLEA GQARQLTDHP RTDRDPMWID GQGYFVSDRD
GKLNLYRVDP DGGAVEQLTR HSEWDVRWAS SDERSRIIYE LDGELRLYNV QDGSDTAIEI
TVPDDGVNTR PRWVDVSDQI NGAHLSPTGQ RVLFEARGNL FNAPVGEGVT RSLTGRSTAH
DREAAWFPDG QSIVFVSDIS GEEELYVVPA DGSEAPRALT SGHETRFYQP IVSPDGEHIA
VSDKEGRIFI LPADGDGEMV EVGRDPGWRN RDYVWAPAGD VLAFSQTQES GMRAIYLHTL
SDGETRRISD GMFSEYRPAF SPDGQYLYYL GDREFAPQIS SIEWNFATNR TTGIFAFALS
SDAPNPFAPE DAEEPGVVAN GNDNGNGDDE ENGDSEATHI DFDGLAQRLI RLPVDAGNYW
SLSVVEGGVL FMEGSAFYYG RAPESQPKLR FFKFEDQEVV DFPNGRQFTD LSLDGKRLLA
RQGSNWQVLD VAKEGRDPEA VATNGLRTRI DPVAEWATAF DEVWRRFRDY FYVPNMHGYD
WEALREQYRP LLAHVAHRSD LNYVMGEMIG ELNISHAYVS GGDEGLPERH PVALLGARFE
ADRGRYRISR ILEGQNDEPR YRSPLTEAGV NIAVGDYLIA INGHEISAEE NIYQRLMLPP
GEPVALTVSE RRDGRDARTV MVNPINDETS LFYLAWVLDN HRYVSEATDG RVGYLHIPDM
GPDGIREFIK WYYGQIRKQG LVIDVRSNGG GNVSQMLIER LSRRPLALGY ARTNPYPSTY
PNEAFNGHLV ALLDENSASD GDIFPWQFRN AGLGPLIGQK SWGGVVGITS HGPLIDGGSV
NVPEFGFSDV NGNWVVEGEG VTPDIEVEND PASVIAGRDP QLERAIQEVM QKIESDPPRF
PARPAPPVKT D
//
