YEEF_BACSH
ID YEEF_BACSH Reviewed; 669 AA.
AC E0TU96;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Toxin YeeF {ECO:0000303|PubMed:32117125};
DE AltName: Full=DNase YeeF {ECO:0000303|PubMed:32117125};
GN Name=yeeF {ECO:0000303|PubMed:32117125, ECO:0000312|EMBL:ADM36747.1};
GN OrderedLocusNames=BSUW23_03455;
OS Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS subtilis subsp. spizizenii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=655816;
RN [1] {ECO:0000312|EMBL:ADM36747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA Zeigler D.R.;
RT "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT into speciation within the B. subtilis complex and into the history of B.
RT subtilis genetics.";
RL Microbiology 157:2033-2041(2011).
RN [2]
RP FUNCTION AS A TOXIN, FUNCTION AS A DNASE, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, EXPRESSION IN E.COLI, MUTAGENESIS OF HIS-581, AND DNA-BINDING.
RC STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX PubMed=32117125; DOI=10.3389/fmicb.2020.00095;
RA Kaundal S., Deep A., Kaur G., Thakur K.G.;
RT "Molecular and Biochemical Characterization of YeeF/YezG, a Polymorphic
RT Toxin-Immunity Protein Pair From Bacillus subtilis.";
RL Front. Microbiol. 11:95-95(2020).
CC -!- FUNCTION: Toxic component of an LXG toxin-immunity module
CC (PubMed:32117125). These modules promote kin selection, mediate
CC competition in biofilms, and drive spatial segregation of different
CC strains, indicating that LXG toxins may help avoid warfare between
CC strains in biofilms (By similarity). The C-terminus (residues 527 to
CC 669) has DNase activity in E.coli and in vitro, and inhibits growth
CC upon expression in E.coli; does not have RNase activity. Acts on
CC supercoiled, genomic, linear and nicked DNA. By 2 hours post-induction
CC cells have an irregular surface, membrane disruption and elongate. All
CC toxic effects in E.coli are neutralized by cognate immunity protein
CC YezG. Binds DNA in the presence and absence of YezG; substrate-binding
CC and immunity protein-binding must occur at distinct sites on the toxin
CC (PubMed:32117125). {ECO:0000250|UniProtKB:O31506,
CC ECO:0000269|PubMed:32117125}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:32117125};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:32117125};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:32117125};
CC Note=10 uM Mn(2+) or 10 mM Mg(2+) are equally active in vitro.
CC {ECO:0000269|PubMed:32117125};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5 for the C-terminal fragment DNase.
CC {ECO:0000269|PubMed:32117125};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius for the C-terminal fragment
CC DNase. {ECO:0000269|PubMed:32117125};
CC -!- SUBUNIT: The C-terminal fragment is a homodimer (PubMed:32117125). The
CC C-terminus interacts with cognate immunity protein YezG, probably with
CC 2:2 stoichiometry. The second YezG molecules binds with lower affinity
CC (Probable). {ECO:0000269|PubMed:32117125, ECO:0000305|PubMed:32117125}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O31506}.
CC Membrane raft {ECO:0000250|UniProtKB:O31506}. Note=Present in
CC detergent-resistant membrane (DRM) fractions that may be equivalent to
CC eukaryotic membrane rafts; these rafts include proteins involved in
CC signaling, molecule trafficking and protein secretion. Delivery to
CC target cells requires the type VII secretion system (T7SS) and YukE.
CC {ECO:0000250|UniProtKB:O31506}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the LXG family.
CC {ECO:0000303|PubMed:32117125}.
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DR EMBL; CP002183; ADM36747.1; -; Genomic_DNA.
DR SASBDB; E0TU96; -.
DR EnsemblBacteria; ADM36747; ADM36747; BSUW23_03455.
DR KEGG; bss:BSUW23_03455; -.
DR HOGENOM; CLU_023665_0_1_9; -.
DR OMA; YEMEQEW; -.
DR Proteomes; UP000002233; Chromosome.
DR Gene3D; 3.40.570.10; -; 1.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR044927; Endonuclea_NS_2.
DR InterPro; IPR006829; LXG_dom.
DR Pfam; PF13930; Endonuclea_NS_2; 1.
DR Pfam; PF04740; LXG; 1.
DR PROSITE; PS51756; LXG; 1.
PE 1: Evidence at protein level;
KW Cell membrane; DNA-binding; Hydrolase; Membrane; Nuclease; Toxin.
FT CHAIN 1..669
FT /note="Toxin YeeF"
FT /id="PRO_0000456172"
FT DOMAIN 1..235
FT /note="LXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01092"
FT MUTAGEN 581
FT /note="H->A: Loss of DNase activity, no longer inhibits
FT E.coli growth."
FT /evidence="ECO:0000269|PubMed:32117125"
SQ SEQUENCE 669 AA; 74714 MW; 8E90B9D481A0708B CRC64;
MKVLEVKTLL SEATDRAKEY KELRTQMVNL RKALKSVADL GDSEFSGKGA SNIKAFYHDH
VGVTDQWIDY IDMKIAFFNS IAGAAEDKGL SDAYIEESFL EHELANAHKK SKSIMSEQKK
AMKDILNDID NILPLDLFST ETFNDELADA NDKRKKTLEK LDALDEDLKT EYALSEPNEQ
FIKSDFQKLQ EATGKGKNAT PIHYNAKAYR ESDIHKKKGD IEKRTEAYLK IKKEEAKERE
IEKLKERLKN YDYADADEFY EMAKTIGYEN LTAEQQRYFT QIENTRELEA GFKGVAVGLY
DSGKDAVVGL WDMVTDPGGT VEAITGAVAH PIKTYEAISA AIEESYQKDM VNGDTYSRAR
WVSYAVGTVV TSIVGTKGVG AVSKTGTATK VTTKVKTAAS KSATAQKAIT VSKQTIDHIK
QKVNKGIEVS KKHVKTKLNQ IGDLTLADIL PYHPRHDLVP AGVPYNAVNG VTLKEGLQKF
AKVILPKPYG TSSSGRRTPA PVVPPVTVKY GEHYARWSRK KVLKPNIIYK TKEGYTYTTD
NYGRITSVKA DLQLGEAKRN QYAQSHAGKP QDRKPDDDGG HLIATQFKGS GQFDNIVPMN
SQINRSGGRW YEMEQEWAKA LKEEPPQKVN VNIKAIYKGD SLRPDKFIVK FRIGDADFEK
VTIKNQSGG
