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Database: UniProt
Entry: A0A1W9P7B1_9BACT
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Original site: A0A1W9P7B1_9BACT 
ID   A0A1W9P7B1_9BACT        Unreviewed;      1093 AA.
AC   A0A1W9P7B1;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE            EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN   ORFNames=B5M54_05420 {ECO:0000313|EMBL:OQX54298.1};
OS   Candidatus Aminicenantes bacterium 4484_214.
OC   Bacteria; Candidatus Aminicenantes.
OX   NCBI_TaxID=1968529 {ECO:0000313|EMBL:OQX54298.1, ECO:0000313|Proteomes:UP000192734};
RN   [1] {ECO:0000313|Proteomes:UP000192734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQX54298.1}.
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DR   EMBL; MZGL01000024; OQX54298.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9P7B1; -.
DR   Proteomes; UP000192734; 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; 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   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|PIRNR:PIRNR036421}.
FT   DOMAIN          868..1050
FT                   /note="Tail specific protease"
FT                   /evidence="ECO:0000259|SMART:SM00245"
FT   REGION          548..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        759
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT   ACT_SITE        982
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT   ACT_SITE        1039
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ   SEQUENCE   1093 AA;  123273 MW;  849328E38CED42A7 CRC64;
     MRRQKLRLTL GICVILLCFF PLKAIDVHDT KLLSQPAITQ GKIAFVYAND IWICNWQGKN
     VFRLTSHPGV ESNPVFSPDG QWVAFSGEYD GNTDVYLVPV EGGIPKRLTW HPGADIVRGF
     TPDSRKVIFI STRNSFTYAH NKLFTISIKG GMPEELPLPY VYKASFSPDG QKMAYVPLRE
     AFHQWKHYRG GTVSTIWIIK LSDLSVQKIP QPEGRCNDTD PMWIGDKIYF RSDRAGEFNL
     FVYDLSTEKI MQLTHFDDFP VLSVAAGAGK IIFEREGHLF LYDLATNKSE RLVIGVAADL
     LELRPRYAQG EKFIRSSAIS PTGARAVLGF RGEIVTLPAK KGDFRNLTNS PGAHDRYPAW
     SPDGSQIAFF SDASGEYQLY VISQDGQGPV KKFSLPGAGF YDSLAWSPDS KKLTFADNSW
     SLFWIDLETG KVKKIASEYL YGPSEYKSIR GVWSPDSRWV VYTLNTKAYI QKVYVYSLEQ
     DKSFPITDGL SEVSEPVFDP SGHYLYFFAS TDAGPVKHWF AMSNADLRMT KAIYLAVLRK
     DLPSPLAKES DEEKLEGKEE KKGQEEKEQE SSSKPKEEVV TIDFEGLNQR IVALPIPVGS
     YFNLQVAGKG QLYFLEISAS ARGPSRPGAK LHYFDLKARQ DKVLAEGLYS FSLSANGKKL
     LYRARNQLGI VATGQKFRPG EGKLNTESIK IKINPQEEWR QIFFEAWRIN RDYFYDPYFH
     GIDWPAMKDK YAVFLDHLAC RNDLNRVIQW MCSELGVGHH RVAGGDTLAR TERIPGGLLG
     ADFEVDHGRY RFKKVLGGLN WNPELRSPLT EPGVNVRAGE YLLAVEGKEL IPPDNIYRYF
     ENTAGKIVEI TVGPFPDGKE ARQVLVVPLA NEYSLRNRDW VEANIRKVDE ATGGRVAYVY
     VPNTAGLGYT YFKRYFFPQS HKEAIIVDER FNGGGQVADY YIDILRRPFV CMWAMRYGAD
     LKTPSASIQG PKVMLINESA GSGGDLLPWM FRKFKLGKLI GKRTWGGLVG ILGFPVLMDG
     GYVTAPNLAI WTEDGWVVEN EGVPPDIEVE QWPALVAQGR DPQLEKAIEV VLEELKKNPP
     PQLKRPPYKK INR
//
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