ID A0A3N2N0Z0_9BACT Unreviewed; 1085 AA.
AC A0A3N2N0Z0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=EEL48_03315 {ECO:0000313|EMBL:ROT16093.1};
OS Muribaculaceae bacterium Isolate-102 (HZI).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486470 {ECO:0000313|EMBL:ROT16093.1, ECO:0000313|Proteomes:UP000272558};
RN [1] {ECO:0000313|EMBL:ROT16093.1, ECO:0000313|Proteomes:UP000272558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-102 (HZI) {ECO:0000313|Proteomes:UP000272558};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-2018) 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:ROT16093.1}.
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DR EMBL; RIBI01000001; ROT16093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2N0Z0; -.
DR Proteomes; UP000272558; 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; cd00988; PDZ_CTP_protease; 1.
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; 2.
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; IPR029414; Tricorn_PDZ.
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 Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 2.
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:UP000272558};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1085
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017993127"
FT DOMAIN 714..781
FT /note="Tricorn protease C1"
FT /evidence="ECO:0000259|Pfam:PF14684"
FT DOMAIN 813..867
FT /note="Tricorn protease PDZ"
FT /evidence="ECO:0000259|Pfam:PF14685"
FT DOMAIN 904..1059
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|Pfam:PF03572"
FT REGION 565..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 776
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 992
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1049
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ SEQUENCE 1085 AA; 121909 MW; 29EE2D33AC5C40E4 CRC64;
MKKLFLIAGA IALTSAAEAA ESPLWMRYPA ISPDGKTIAF CYQGDIFTVP STGGRATQLT
TNPAYDTRPV WSPDGKSLAF ASDREGSFDI YIMSREGGAP TRLTTHSASE MPETFLDNEH
VLYTASIQPD VNDSQFPSVQ FPQIYSVSTT GGRPKLYSSL AMENLSISPD GKQLLYNDMK
GYEDTWRKHH TSSITRDIWL CTTDGNRSYR KLTDFNGEDR NPVWKADGSA YYYLSERDGN
FNVYKSTIDG KNTVKITSHP KHPVRFLTTS NDGKLCYGYD GEIYTVTEGS QPAKVSVAIT
SDITEQKLVN RLISSGATDI AVSPSGKEVA FIVHGDVYVT SVEYRTTKQI TDTPQQERNI
DFSPDGRSLV YSAERGETWG IYESSIVRDD DKYFTYAQEI EEKPLVTGDK TSFQPLYSPD
GKEVAFLEDR SAIRVINRKS KDVRTVMEGK YNYSYSDGDQ SFAWSPDGRW FLTEYIGVGG
WNNKDIALIK ADGSGETVNL TESGYSDTNP KWVLDGKAMI WNSDRAGYRS HGSWGSHSDV
YIMFFDDEAW DKFQLSKEEI ALAEEAEKDK KDKESSANDD KKDKKDKKGK GKKDKVEKED
EIKPIKLELD NRRDRIMRLT VNSSNLGDAL LSKKGDKLYY CTSFEGGYDL WLHDLKENST
KLLIKGVGYG PLLTDKDGEK AFLISRGGLT QINIKDANTK SIPFAAEFNY RPAEERDYIF
NHAWRQVNDK FYDPEIHGID WASFREDYSK YLPYINNNYD FRDMLSEMLG ELNGSHTGAR
YYSSTSAPAT ASLGAFYDES YDGDGLKITQ IIAQGPLTKA DNKITKGCII EKINGKTIER
GKDYYPMLAG KAGKSVMLTV LDPSTGKRFE EKVKPISYGT QSDLLYKRWV ENNRKRVEQL
SGGKVGYVHV KGMDSPSFRT VFSDLLGRYR NCDAVIVDTR HNGGGWLHDD LATLLDGKEY
ARYTPRNSYI GSDPFTKWLK PSCVLVCEDN YSNAHGFPWV YKTLGIGKLI GTPVPGTMTA
VWWETQIDPS LVFGIPQVGC KDMDGNYLEN HELQPDIKVY NTPEVQLQGG DTQLETAVKE
MLNTI
//
