ID A0A0S2I5S2_9BACT Unreviewed; 1076 AA.
AC A0A0S2I5S2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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=L21SP5_03934 {ECO:0000313|EMBL:ALO17525.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO17525.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO17525.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO17525.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-2015) 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; CP013118; ALO17525.1; -; Genomic_DNA.
DR RefSeq; WP_057954779.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2I5S2; -.
DR STRING; 1307839.L21SP5_03934; -.
DR KEGG; blq:L21SP5_03934; -.
DR PATRIC; fig|1307839.3.peg.4200; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000064893; 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; 2.120.10.60; 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; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' 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:UP000064893};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 841..1033
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT ACT_SITE 739
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 963
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1022
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 964
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1076 AA; 122900 MW; CE6F582DEA2A710C CRC64;
MVHYRVLVIA LIFGLFQQLN GQEARLMRFP DFHQNKVVFT YAGDLYLADR DGGVARRLTS
HPGYEMFARF SPDGSKIAFT GQYDGNTEVY VMPAEGGTPQ RLTHTATLSR DDVSDRMGPN
NMVMSWTPDG NNIVYRSRGI SFNSFVGHLF KVPVEGGLSE RLPLSTGGFH TWSDDGNQLA
FNRVMREFRT WKYYKGGMAD DVWLFDFNTK ETKQLTDNVA QDIFPMWYKG DVYFASDRDR
TMNLFVYKSE SEEIEKITDF DTYDVKFPSL GTDGIIFENE GYLYIYNFTD NETEKLNIQI
DNDQVYGRKA YIDASEFVDD VNISPQGNRV VFGARGDIWS VPANEGVTYN LTQSSGVHDR
EPAWSPDGKY LAWISDKTGE DQIYILENKE GAKPKKLTNL STYIFNIDWS PNSKMLAWTD
QNYNLSYIDI ASGDTKQVIH GDHGKIWSYN WSPDSKWLTY TKPQENEMTV IQLYNLENDR
HYPVTESWYD AGSPIFSPKG KYLYFVSARD FSPTYNDVEW NYAYKNMNRI YMVPLAKSTK
SPFAPENNKV KVVEENGKSE KSENEEIVID TDGLSDRVVD LPVEPAYYYN LQPSEGKLYY
NTMKSGDRKY MLKMYDLEKK KEKAIGEQIS MQITANGKKV LVRYHGKNYV EKLPGGKLKP
QNKVDQSKMK LWVDKKAEWE QIYTESWRQM REFFYANNMH GLDWKVIHDK YAKLLPWVNH
RNDLNYLIGE MIGELNIGHA YVNGGDRPDV ERIKTGLLGA QITADKSGYF KIEKILDGEN
WRDNARSPLT QPGADVKAGD YILAVDDNST KNVQDIYSLL TGKANQVVEL TVNSKPSENG
AKDILAKTID DESELYYYNW VQTNIEKVND ATNGQVGYIH IPDMGPKGLN EFVKHFYPQL
TKKALIIDDR GNGGGNVSPM IMERLRRELV FYSMRRNQKS VEPSPNQIMA GPKVLLINNY
SASDGDLFPY RFKSHETGPV IGVRSWGGVV GITGSLPFID GGQLRKPEFA PFAKDGSKFI
IEGHGVDPDI VIDNDPYKEY MGEDAQLQKA IEVVLKKLEE NPLETPEIPP FPDKSK
//
