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
//