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Database: UniProt
Entry: A0A1G5UZV5_9BACT
LinkDB: A0A1G5UZV5_9BACT
Original site: A0A1G5UZV5_9BACT 
ID   A0A1G5UZV5_9BACT        Unreviewed;      1102 AA.
AC   A0A1G5UZV5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE            EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN   ORFNames=SAMN03080617_00231 {ECO:0000313|EMBL:SDA39150.1};
OS   Algoriphagus alkaliphilus.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=279824 {ECO:0000313|EMBL:SDA39150.1, ECO:0000313|Proteomes:UP000198756};
RN   [1] {ECO:0000313|EMBL:SDA39150.1, ECO:0000313|Proteomes:UP000198756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22703 {ECO:0000313|EMBL:SDA39150.1,
RC   ECO:0000313|Proteomes:UP000198756};
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; FMXE01000002; SDA39150.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5UZV5; -.
DR   STRING; 279824.SAMN03080617_00231; -.
DR   OrthoDB; 9815657at2; -.
DR   Proteomes; UP000198756; 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; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF69322; Tricorn protease domain 2; 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          849..1054
FT                   /note="Tail specific protease"
FT                   /evidence="ECO:0000259|SMART:SM00245"
FT   ACT_SITE        745
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT   ACT_SITE        971
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            972
FT                   /note="Transition state stabilizer; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ   SEQUENCE   1102 AA;  123564 MW;  A9140EC91A909332 CRC64;
     MVLKKWMLTG LASFGLIAFG FSQEKPGYFM YPDIHENTVV FVAEGDLWKT SLNGGEAIRL
     TTHAGEESSP KISPDGKWVA YAATYEGPTE VYLIPISGGL PRRLTYEPAA SIPTAWKSAS
     EVAYVTNQYS TLPRLNTVVI NIENGSKSIV PLDMAAEGSF NASGDTYFFV RPTFHNNVTK
     RYEGGTARQL WKYTSGQAEA VKLTNEYKGE DHHPIYHNGR VYFLSSRDGI QNVWSMNENG
     SDLKQHTKQS SYDVREVSIH GNNLVYRSGA DLYLHELSNG QDKKLAISLT SDFDQLREYW
     IDNPANYIST ISVSDDGEKV ALTARGRVFV FPAKQGRSLR LSQKDGVRYR DAVFSPDGKD
     ILTFSDESGE FEIHQYSGLG LDQGKKITSD GTTLRFGLLP SPDGKKLAYY DLNNELWIQE
     IASGKKVKAN ASDENLSGSM AWSPDSKWLA FGQAASNTFM QLFIFNSETG KRIPLTSDRT
     NSMNPQWSPD GKWIYFMSDR NFESRIGSPW GTRQPEPFWE KQIKIYQVGL KKGLVSPFQP
     KNELKPAEEK KAEGPVTVSI DEEGLIERVR EVPIPAGNYK SLVVTDKALY YHRVGPGMGI
     YYGGGAPNDD NPALMMTPID EKAEQKVFAD KINSFVTSLN NKFAVLRQGN NHYVVELGTS
     PVSDLSKNQL NLSGWKFSVD PREDWRQIYT DAWRMERDYF YDPNMHGVDW DAMYKKYLPL
     VDRVTTRREL SDVMGELIGE LSVLHTSVGG GDLREGDDKI QFGMLGGKFS RNEKLRGYSI
     DHIFKSDPDY PDEMSPLSHP DLNVSIDDVI THIDGVSVMD APDLLYLLRD KANKQVRIKV
     LSSSGADKGD RIILPMTSAA ESNLRYNEWE YTRRLIAEEK SNGEIGYVHL RAMTAPDIGQ
     WYRDFYPQFK KSGLVIDVRQ NRGGNIDSFI LEKLMREVFF YWKSRTGEPY WNMPYAFRGH
     LVLLVDEFTA SDGEAFAEGF RRLDMGQAIG ARTWGGEVWL SGVNTLTDNG VARAPMNGVY
     GVVGEKLVGG DTDQGESVEW LIEGVGFIPD IEVINMPKAT FDGKDAQLDA AIEHLKALIK
     ADPRAVPQAP AYPDKSFKNG KN
//
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