ZORO_ECO57
ID ZORO_ECO57 Reviewed; 29 AA.
AC Q8X3T7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Small toxic protein ZorO {ECO:0000303|PubMed:24203704};
GN Name=zorO {ECO:0000303|PubMed:24203704}; OrderedLocusNames=Z3289;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP IDENTIFICATION, FUNCTION AS A TOXIN, AND INDUCTION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=20156992; DOI=10.1093/nar/gkq054;
RA Fozo E.M., Makarova K.S., Shabalina S.A., Yutin N., Koonin E.V., Storz G.;
RT "Abundance of type I toxin-antitoxin systems in bacteria: searches for new
RT candidates and discovery of novel families.";
RL Nucleic Acids Res. 38:3743-3759(2010).
RN [3]
RP FUNCTION AS A TOXIN.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=24203704; DOI=10.1093/nar/gkt1018;
RA Wen J., Won D., Fozo E.M.;
RT "The ZorO-OrzO type I toxin-antitoxin locus: repression by the OrzO
RT antitoxin.";
RL Nucleic Acids Res. 42:1930-1946(2014).
RN [4]
RP FUNCTION AS A TOXIN, AND INDUCTION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=27903909; DOI=10.1093/nar/gkw1172;
RA Wen J., Harp J.R., Fozo E.M.;
RT "The 5' UTR of the type I toxin ZorO can both inhibit and enhance
RT translation.";
RL Nucleic Acids Res. 45:4006-4020(2017).
RN [5]
RP FUNCTION AS A TOXIN, CAUSES MEMBRANE DAMAGE, SUBCELLULAR LOCATION,
RP BIOTECHNOLOGY, AND MUTAGENESIS OF 2-ASP--VAL-14; 2-ASP--THR-9;
RP 20-ALA--LYS-29; 20-ALA--LEU-24 AND 25-ILE--LYS-29.
RC STRAIN=O157:H7 / ATCC 43888 / CDC B6914-MS1;
RX PubMed=31277504; DOI=10.3390/toxins11070392;
RA Otsuka Y., Ishikawa T., Takahashi C., Masuda M.;
RT "A Short Peptide Derived from the ZorO Toxin Functions as an Effective
RT Antimicrobial.";
RL Toxins 11:0-0(2019).
CC -!- FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system
CC (PubMed:20156992, PubMed:24203704, PubMed:27903909, PubMed:31277504).
CC Expression in the absence of its cognate antitoxin (small sRNA orzO)
CC leads to cell stasis and a decrease in colony-forming units
CC (PubMed:24203704, PubMed:27903909). Repression of ZorO toxicity
CC requires base pairing between zorO mRNA and sRNA OrzO, as well as RNase
CC III (rnc), suggesting the mRNA is degraded. Base pairing occurs between
CC 18 bases in the 5' UTR of zorO mRNA and the 5' end of OrzO sRNA. sRNA
CC OrzP, which differs only in 4 of these 18 bases, does not repress ZorO
CC toxicity (PubMed:24203704). Integration of the protein into the inner
CC membrane damages membrane integrity and affects membrane potential. It
CC leads to increased levels of hydroxyl radicals (PubMed:31277504).
CC {ECO:0000269|PubMed:20156992, ECO:0000269|PubMed:24203704,
CC ECO:0000269|PubMed:27903909, ECO:0000269|PubMed:31277504}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:31277504}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expressed during exponential growth in rich medium and at
CC lower levels in exponential and stationary phase in minimal medium
CC (zorO mRNA cannot be distinguished from zorP mRNA by these assays as
CC they are practically identical) (PubMed:20156992). Translation of this
CC mRNA is repressed by secondary structures in its 5' UTR and partially
CC by OrzO sRNA. Processing of the 5' UTR increases its translation in
CC vitro and comparative toxicity in vivo (PubMed:27903909).
CC {ECO:0000269|PubMed:20156992, ECO:0000269|PubMed:27903909}.
CC -!- BIOTECHNOLOGY: A short internal peptide (AARL, residues 20-24) is toxic
CC against B.subtilis, S.aureus and the yeast Candida albicans but not
CC against E.coli, green monkey (Vero) or hamster cells (BHK) cultured
CC cells. It functions in various growth media and might be used as an
CC antimicrobial peptide. The intact protein is not toxic under any tested
CC conditions when added to growth medium. {ECO:0000269|PubMed:31277504}.
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DR EMBL; AE005174; AAG57182.1; -; Genomic_DNA.
DR PIR; B85840; B85840.
DR AlphaFoldDB; Q8X3T7; -.
DR SMR; Q8X3T7; -.
DR EnsemblBacteria; AAG57182; AAG57182; Z3289.
DR KEGG; ece:Z3289; -.
DR PATRIC; fig|83334.175.peg.1043; -.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Toxin-antitoxin system;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..29
FT /note="Small toxic protein ZorO"
FT /id="PRO_0000450222"
FT TRANSMEM 10..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 2..14
FT /note="Missing: Wild-type toxicity."
FT /evidence="ECO:0000269|PubMed:31277504"
FT MUTAGEN 2..9
FT /note="Missing: Wild-type toxicity."
FT /evidence="ECO:0000269|PubMed:31277504"
FT MUTAGEN 20..29
FT /note="Missing: Not toxic."
FT /evidence="ECO:0000269|PubMed:31277504"
FT MUTAGEN 20..24
FT /note="Missing: Not toxic."
FT /evidence="ECO:0000269|PubMed:31277504"
FT MUTAGEN 25..29
FT /note="Missing: Wild-type toxicity."
FT /evidence="ECO:0000269|PubMed:31277504"
SQ SEQUENCE 29 AA; 3263 MW; 4909328607F73679 CRC64;
MDTLTQKLTV LIAVLELLVA LLRLIDLLK
