ID A0A1T5AJ41_9FLAO Unreviewed; 1057 AA.
AC A0A1T5AJ41;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=SAMN05660866_00997 {ECO:0000313|EMBL:SKB34849.1};
OS Maribacter arcticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Maribacter.
OX NCBI_TaxID=561365 {ECO:0000313|EMBL:SKB34849.1, ECO:0000313|Proteomes:UP000190339};
RN [1] {ECO:0000313|EMBL:SKB34849.1, ECO:0000313|Proteomes:UP000190339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23546 {ECO:0000313|EMBL:SKB34849.1,
RC ECO:0000313|Proteomes:UP000190339};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUYL01000002; SKB34849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5AJ41; -.
DR STRING; 561365.SAMN05660866_00997; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000190339; 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; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR028204; Tricorn_C1.
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; 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 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1057
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013001714"
FT DOMAIN 756..817
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 538..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 746
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 1019
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 1057 AA; 120830 MW; F00666C7A1C90D2D CRC64;
MYFKPFLVLL FGFLVSNLQA QEAYFLMDPT VSPDAKTIVF SYDTDLWSVP ATGGTAVRLT
AMDGEETLPR ISPDGKWLAF SATQFGNRDI FVMPMEGGSI QQLTFNDAAD DMDSWAWDSK
SLYFTSSRNN RYSGYEVAVM GGTPKRLFEN FFNTVANIAI HPKTEEVFFN ESWEAKIFTH
RKRYKGAYNP DIKSYNPKTK TYKEYTNYAG KDLWATLDLD GNLYFVSDEA NGEYNLYEMV
NGAKVQHTKF ETSIGRPQVS ANGELVVFGK DYQVYGYNVA TKTATKIPIK ITENSTLTKT
QDFKVQGNIS NFSVSPDNKK LAFISRGELF VSDVKGKFIK HITTDPAERV LEITWLKDNK
TLLYNRTYKG YTNLFTIAAD GSVPEKQHTN DLRNNVNIVL DPDLSKALYI SGRDELRLLD
LSNFKSETVV KDEFWALYAP QPHFSPNGKY IAYNAIRNFE NDVFVIRLSD KKITNLTNTG
VTESDPVWSP DGKYLYMMAN LTKPSYPYGL NESQIYQMPL DKYEDAFTYE KYDELFKEEE
KEKEDDKDDK DEKDEKKDKA EEEKKKPITI TINPDGIMER ITAISPAFGK QTSPTVIEKE
EAMHVLYISN HDEGKSKLWK TIIKPFEKNK IEMVLDDELN GYQLAGAKDS YYLLGKGNLH
TLDIEKNKTE KIEMDFTFRR NLSEEFRQMF QEAWAGFEEN FYDGDFHGED WTLLRKKYEQ
YLPYLTNRNQ LRVLFNDMLG ELNTSHFGFN SSGDEENVFY KTKTLAVGIE FSNENPFTVE
SIIADSPADV TGKNLKKGDV LVAVNGQAID PKKNREAYFN EPSLDKEIQM DFKRDGKTIA
INLHPISNTA QRNLLYDTWV DANQKYVDEH GNKKIAYVYM KNMGGSELEH FKREMVSETN
QREALILDLR FNTGGNVHDE VLQFLSQKPY LKWKYRDGGL APQPNFAPAV KPIILLMNEQ
SLSDAEMTAA GFKALKLGKT LGTETYRWII FTSGKGLVDG SFYRLPAWGC FTLDGQDLEK
TGVAPDITVP ENFKQRLEGE QPQLDAAIAE ILRQLKG
//
