ID A0A1H9C378_9FLAO Unreviewed; 1080 AA.
AC A0A1H9C378;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=SAMN05444005_10417 {ECO:0000313|EMBL:SEP95411.1};
OS Flavobacterium urocaniciphilum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1299341 {ECO:0000313|EMBL:SEP95411.1, ECO:0000313|Proteomes:UP000198648};
RN [1] {ECO:0000313|EMBL:SEP95411.1, ECO:0000313|Proteomes:UP000198648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27078 {ECO:0000313|EMBL:SEP95411.1,
RC ECO:0000313|Proteomes:UP000198648};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOEI01000004; SEP95411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9C378; -.
DR STRING; 1299341.SAMN05444005_10417; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000198648; 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; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR012393; Tricorn_protease.
DR PANTHER; PTHR43253; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR PANTHER; PTHR43253:SF1; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR Pfam; PF07676; PD40; 5.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 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:UP000198648};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1080
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011680526"
FT DOMAIN 847..1054
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 569..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 769
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 986
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1043
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 987
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1080 AA; 121087 MW; C07384515CECC1E7 CRC64;
MNIKTTLFCL QLFLLTSFSF AQEALWMRYP SISPDGKTIA FGYKGDIYLV NAQGGTAVPL
TIHEAHDMMP IWSNDGKSIA FASDRHGNFD VFIMAVSGGT PTRLTYNSAA DYPYDFSPDD
KNVLFGSSRQ TSSANIRFYS PRLFQNLYTV NATGGKPILI TEGGIEFAKY NKAGNQIIFQ
DRKGYEDPWR KHHTSSVTRD VWSYDVNGQT FSKISNYIGE DKEPVYSADE KSIYYLSEAD
GSNQNVYKYN VASKAVTGLT SFKNNPVRHL SISNDNKLCF SYDGQIYTML EGGTPQKVAV
TIQNDGKTNV EKNLPLSGNI SEFVPSPDGK EIAFISRGEV FVVNAEGGST KRITNTPEQE
RYVQWSPDGK KLIYAGERGD SWDIYVATIE RKEEKYFYAS TILKEEKIIG SDKEEYMPKF
SPDGKEIAYI EERNIVKVYN VATKASRVVL PEGRNYSYSD GDFGFNWSND SKWLFIDDAM
GNFAIAHTAM IKADGSETKY PIMSGFGEDS AKQQMGGKAL AWLSSKEGRK SLAYQGSREV
DVYAVFFDKK EYENFKLSKE DAALLKEKED AAKKEKEGDD KKSDKSKTEK KDEPKPWNPD
LTNLETRKVR VTINSSSIAD FVFNEDGSKL FYLASFEKGY DVWVTETRTK ETKILAKLGG
TASQLFLSKD GKSLFVNNGG KLMKIEAEGG KTSSVDVSSD MVLNTQAERT YIFNHMWRQT
AKKFYDPKLH GVDWKMYKDT YARFLPHINN NYDFQELLSE ILGELNASHT GGRYNPQMSN
PDVTATLGLL YDQKSKDAGL KVTEVIQGGP FDKADSKVKA GATITKIDDQ TITNDVDWAK
FLNRKVGKNT LVSGVDANGV AFQESVKPIA FGEETALMYN RWIKKMNAMV EKLSDGKVGY
VHVQGMNDGS FREVYDQVMG KNFEKKALIV DTRFNGGGWL HDDLFTLLNG KRYLDFAPQG
NIVKDAEPVG KWTKPSCVLM SEGNYSDAFI FPYIYKQNGV GKLIGMGVPG TGTAVWWETQ
IDPTLIFGIP MVATIGKERR ATENLQVDPD IQVNLSYEDF LKGKDTQLEK AVEEMLKSIK
//
