ID   ENTM_BACFG              Reviewed;         405 AA.
AC   P54355;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Fragilysin;
DE            EC=3.4.24.74;
DE   AltName: Full=Enterotoxin;
DE   Flags: Precursor;
GN   Name=btfP;
OS   Bacteroides fragilis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VPI 13784;
RX   PubMed=9011050; DOI=10.1016/s0378-1097(96)00488-0;
RA   Kling J.J., Wright R.L., Moncrief J.S., Wilkins T.D.;
RT   "Cloning and characterization of the gene for the metalloprotease
RT   enterotoxin of Bacteroides fragilis.";
RL   FEMS Microbiol. Lett. 146:279-284(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 224-402.
RC   STRAIN=VPI 13784;
RX   PubMed=7806355; DOI=10.1128/iai.63.1.175-181.1995;
RA   Moncrief J.S., Obiso R.J. Jr., Barroso L.A., Kling J.J., Wright R.L.,
RA   van Tassell R.L., Lyerly D.M., Wilkins T.D.;
RT   "The enterotoxin of Bacteroides fragilis is a metalloprotease.";
RL   Infect. Immun. 63:175-181(1995).
RN   [3]
RP   3D-STRUCTURE MODELING.
RX   PubMed=9310661; DOI=10.1086/516240;
RA   Obiso R.J. Jr., Bevan D.R., Wilkins T.D.;
RT   "Molecular modeling and analysis of fragilysin, the Bacteroides fragilis
RT   toxin.";
RL   Clin. Infect. Dis. 25:S153-S155(1997).
CC   -!- FUNCTION: Diarrheal toxin that hydrolyzes gelatin, azocoll, actin,
CC       tropomyosin, and fibrinogen.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Broad proteolytic specificity, bonds hydrolyzed includes
CC         -Gly-|-Leu-, -Met-|-Leu-, -Phe-|-Leu-, -Cys-|-Leu-, -Leu-|-Gly-.;
CC         EC=3.4.24.74;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5.;
CC       Temperature dependence:
CC         Optimum temperature is 37 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M10C family. {ECO:0000305}.
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DR   EMBL; U67735; AAB49835.1; -; Genomic_DNA.
DR   EMBL; S75941; AAB32890.2; -; Genomic_DNA.
DR   AlphaFoldDB; P54355; -.
DR   SMR; P54355; -.
DR   MEROPS; M10.020; -.
DR   KEGG; ag:AAB49835; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.470; -; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR001843; Fragilysin.
DR   InterPro; IPR032273; Fragilysin_N.
DR   InterPro; IPR038176; Fragilysin_N_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   Pfam; PF16376; fragilysinNterm; 1.
DR   PRINTS; PR00997; FRAGILYSIN.
DR   SMART; SM00235; ZnMc; 1.
DR   TIGRFAMs; TIGR03935; fragilysin; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW   Toxin; Virulence; Zinc.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..405
FT                   /note="Fragilysin"
FT                   /id="PRO_0000028869"
FT   ACT_SITE        357
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         366
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CONFLICT        314
FT                   /note="W -> C (in Ref. 2; AAB32890)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   405 AA;  45411 MW;  88417615BB2733DC CRC64;
     MFILNFNKMK NVKLLLMLGT AALLAACSNE ADSLTTSIDA PVTASIDLQS VSYTDLATQL
     NDVSDFGKMI ILKDNGFNRQ VHVSMDKRTK IQLDNENVRL FNGRDKDSTS FILGDEFAVL
     RFYRNGESIS YIAYKEAQMM NEIAEFYAAP FKKTRAINEK EAFECIYDSR TRSAGKDIVS
     VKINIDKAKK ILNLPECDYI NDYIKTPQVP HGITESQTRA VPSEPKTVYV ICLRENGSTI
     YPNEVSAQMQ DAANSVYAVH GLKRYVNFHF VLYTTEYSCP SGDAKEGLEG FTASLKSNPK
     AEGYDDQIYF LIRWGTWDNK ILGMSWFNSY NVNTASDFEA SGMSTTQLMY PGVMAHELGH
     ILGAEHTDNS KDLMYATFTG YLSHLSEKNM DIIAKNLGWE AADGD