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Database: UniProt
Entry: A0A0P0NLA0_9SPHI
LinkDB: A0A0P0NLA0_9SPHI
Original site: A0A0P0NLA0_9SPHI 
ID   A0A0P0NLA0_9SPHI        Unreviewed;      1107 AA.
AC   A0A0P0NLA0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE            EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN   ORFNames=AQ505_25720 {ECO:0000313|EMBL:ALL08561.1};
OS   Pedobacter sp. PACM 27299.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL08561.1, ECO:0000313|Proteomes:UP000062859};
RN   [1] {ECO:0000313|EMBL:ALL08561.1, ECO:0000313|Proteomes:UP000062859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL08561.1,
RC   ECO:0000313|Proteomes:UP000062859};
RA   Gilbert D.G.;
RL   Submitted (OCT-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; CP012996; ALL08561.1; -; Genomic_DNA.
DR   RefSeq; WP_062550790.1; NZ_CP012996.1.
DR   AlphaFoldDB; A0A0P0NLA0; -.
DR   STRING; 1727164.AQ505_25720; -.
DR   KEGG; pep:AQ505_25720; -.
DR   OrthoDB; 9815657at2; -.
DR   Proteomes; UP000062859; 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; 2.
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; SSF69304; Tricorn protease N-terminal 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:UP000062859};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..1107
FT                   /note="Tricorn protease homolog"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006052256"
FT   DOMAIN          870..1064
FT                   /note="Tail specific protease"
FT                   /evidence="ECO:0000259|SMART:SM00245"
FT   REGION          557..598
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        771
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT   ACT_SITE        995
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT   ACT_SITE        1053
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ   SEQUENCE   1107 AA;  123121 MW;  F0E1AAF950514A81 CRC64;
     MTFLKPNQLS FLAAAALSVT MTLAFTLSAN AQKQETLLIR SPAVSANHLA FVYGGDIWIS
     DKDGSNPRRL TVNPAVEQNP LFSPDGKQIA FTGNYDGNTD VYVIPIEGGA PKRVTYHPAA
     DVMRGWLDNN QLYFTSTRDY QFALSPRLHQ INIDGTAEKA LPMPEAVQGT PSADKRYWAY
     IKNTDPTERS NVAFKRYRGG GMPQIWIFDT QTKDIEIIPG VGSNNVKPQW VGNKVYFLSD
     RDLTMNLFSY DVKSKKTEKL TDFKDYDIKT LTAGPGVIAF EQAGKAHLLE TANHKVRDIS
     INIQADAPYK RPHYIDMASN IRNSEISPTG VRALFESRGE IYSVPKEKGD ARNLSNSPGS
     YDKFPAWSPD GKYISYLSDK DGNYQLVLLN QATKEAPIYI PLGKTAFYYQ PVWSPDSKKL
     FYGDAHLNLF YIDINARKPI LVKADKDGSS PGRSFSALQP AWSPDSKWIS YVATLPNSVS
     AVYLYNLDKE SHTQVTDGMS EVSSPNFSRD GKYLFFLAST DVGLTNSGLH MSAYQRPVNY
     NAYALILSKK TPSIYKTESD EEVIKSEDSP AKKKEEPKKE SSKKDKKGKE AEKPAAPPVK
     APIEIDLADL RSRIIPLPIS GSINGLDGGV DGMLLYYKND ELGALDLKKM ESSTLVSGIS
     SLSISADGKS MLYGSRGNYY IVDAGKKPGS SEAGKLKLDG IKVLVDPTAE WKQMFDEVWS
     MEKDFFYVEN MHGTDWPAMK VKYEKFLPYV NHRSDLSYVF NEMMGEMVVG HNYISPGDEP
     GAPSVSVGLL GADYEVDNGF YKIKKIFTRL DWNPTFKAPL AEPGLNIKEG DYIVAVEGVP
     LTSKTSIYSL FDFKAGKQVA IKVNSKPSLD GAREVVVVPV AAPQEFELRK MDWVENNRKR
     VDKISDGKIA YVYMPNTGPD GYTYFNRYYF SQMDKKALLM DERNNGGGWV ADYVIDLLSR
     ELMSYWGIRD GKSFTTPGNG IFGPKAMLIN ENAGSGGDMM PYMFKKKGLG KLVGRTTMGI
     LVGISGYPLL LDGGSITSPN FGVYDTDGKW IIENEGVAPD IFVEQTPKDL LEGRDPQLER
     TIKVLQEEIK TYKYPNVTKP KDPIRGH
//
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