HEPT_SHEON
ID HEPT_SHEON Reviewed; 133 AA.
AC Q8ECH6;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=mRNA nuclease HepT;
DE EC=3.1.-.- {ECO:0000269|PubMed:29555683};
DE AltName: Full=Toxin HepT {ECO:0000303|PubMed:33045733};
GN Name=hepT {ECO:0000303|PubMed:33045733}; OrderedLocusNames=SO_3166;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP FUNCTION AS A TOXIN, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-15; HIS-56; ARG-70; VAL-94; ARG-97; ASN-98; HIS-102;
RP TYR-104; LEU-107 AND HIS-118.
RC STRAIN=MR-1;
RX PubMed=26112399; DOI=10.1111/1751-7915.12294;
RA Yao J., Guo Y., Zeng Z., Liu X., Shi F., Wang X.;
RT "Identification and characterization of a HEPN-MNT family type II toxin-
RT antitoxin in Shewanella oneidensis.";
RL Microb. Biotechnol. 8:961-973(2015).
RN [3] {ECO:0007744|PDB:5YEP}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH MNTA, FUNCTION AS A
RP TOXIN, FUNCTION AS AN RNASE, AND SUBUNIT.
RC STRAIN=MR-1;
RX PubMed=29555683; DOI=10.1074/jbc.ra118.002421;
RA Jia X., Yao J., Gao Z., Liu G., Dong Y.H., Wang X., Zhang H.;
RT "Structure-function analyses reveal the molecular architecture and
RT neutralization mechanism of a bacterial HEPN-MNT toxin-antitoxin system.";
RL J. Biol. Chem. 293:6812-6823(2018).
RN [4] {ECO:0007744|PDB:6M6U, ECO:0007744|PDB:6M6V, ECO:0007744|PDB:6M6W, ECO:0007744|PDB:7BXO}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) IN COMPLEX WITH MNTA, FUNCTION AS A
RP TOXIN, SUBUNIT, MASS SPECTROMETRY, TRI-AMPYLATION AT TYR-104, AND
RP MUTAGENESIS OF TYR-104.
RC STRAIN=MR-1;
RX PubMed=33045733; DOI=10.1093/nar/gkaa855;
RA Yao J., Zhen X., Tang K., Liu T., Xu X., Chen Z., Guo Y., Liu X.,
RA Wood T.K., Ouyang S., Wang X.;
RT "Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT
RT toxin/antitoxin system.";
RL Nucleic Acids Res. 48:11054-11067(2020).
RN [5] {ECO:0007744|PDB:7AER}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH MNTA, AND
RP TRI-AMPYLATION AT TYR-104.
RC STRAIN=MR-1;
RX PubMed=33290744; DOI=10.1016/j.molcel.2020.11.034;
RA Songailiene I., Juozapaitis J., Tamulaitiene G., Ruksenaite A., Sulcius S.,
RA Sasnauskas G., Venclovas C., Siksnys V.;
RT "HEPN-MNT Toxin-Antitoxin System: The HEPN Ribonuclease Is Neutralized by
RT OligoAMPylation.";
RL Mol. Cell 0:0-0(2020).
CC -!- FUNCTION: Toxic component of a type VII toxin-antitoxin (TA) system. A
CC bacteriostatic toxin; upon overexpression in situ or in E.coli inhibits
CC cell growth. Cells swell slightly. Neutralized by cognate antitoxin
CC MntA (PubMed:26112399, PubMed:29555683, PubMed:33045733). Cleaves mRNA
CC in a probably endonucleolytic manner; has no activity on rRNA, tRNA,
CC ssDNA or dsDNA. The TA system confers plasmid stability in E.coli
CC (PubMed:29555683). Neutralization is mostly due to tri-AMPylation by
CC MntA (PubMed:33045733). {ECO:0000269|PubMed:26112399,
CC ECO:0000269|PubMed:29555683, ECO:0000269|PubMed:33045733}.
CC -!- SUBUNIT: Forms a complex with cognate antitoxin MntA (PubMed:26112399).
CC Forms a heterooctamer with cognate antitoxin MntA with stoichiometry
CC HepT(6):MntA(2). Two HepT molecules dimerize to form a cleft with 2
CC Rx4-6H active site motifs in close proximity that probably bind
CC substrate; in the heterooctamer 3 HepT dimers form (PubMed:29555683).
CC {ECO:0000269|PubMed:26112399, ECO:0000269|PubMed:29555683}.
CC -!- INDUCTION: Expressed during exponential growth, part of the mntA-hepT
CC operon. Under control of MntA. {ECO:0000269|PubMed:26112399}.
CC -!- PTM: Tri-AMPylated by cognate antitoxin MntA on Tyr-104; this rotates
CC the residue nearly 180 degrees. Modified protein has much less RNase
CC activity. {ECO:0000269|PubMed:33045733}.
CC -!- MASS SPECTROMETRY: Mass=16191.46; Method=Electrospray; Note=6-His
CC tagged, no AMPylation, probably in situ.;
CC Evidence={ECO:0000269|PubMed:33045733};
CC -!- MASS SPECTROMETRY: Mass=17122.06; Method=Electrospray; Note=6-His
CC tagged, modifed by 3 AMP, probably in situ.;
CC Evidence={ECO:0000269|PubMed:33045733};
CC -!- DISRUPTION PHENOTYPE: When mntA-hepT is deleted, has a sight reduction
CC in swimming motility. No effect when just this gene is deleted.
CC {ECO:0000269|PubMed:26112399}.
CC -!- SIMILARITY: Belongs to the HepT RNase toxin family. {ECO:0000305}.
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DR EMBL; AE014299; AAN56166.1; -; Genomic_DNA.
DR RefSeq; NP_718722.1; NC_004347.2.
DR RefSeq; WP_011073053.1; NZ_CP053946.1.
DR PDB; 5YEP; X-ray; 3.00 A; B/C/D=1-133.
DR PDB; 6M6U; X-ray; 2.35 A; B/C/D/G/H/I=1-133.
DR PDB; 6M6V; X-ray; 3.08 A; B/C/D=1-133.
DR PDB; 6M6W; X-ray; 2.61 A; B/C/D/G/H/I=1-133.
DR PDB; 7AER; X-ray; 3.00 A; B/C/D=1-133.
DR PDB; 7BXO; X-ray; 2.77 A; B/C/D/F/G/H=1-133.
DR PDBsum; 5YEP; -.
DR PDBsum; 6M6U; -.
DR PDBsum; 6M6V; -.
DR PDBsum; 6M6W; -.
DR PDBsum; 7AER; -.
DR PDBsum; 7BXO; -.
DR AlphaFoldDB; Q8ECH6; -.
DR SMR; Q8ECH6; -.
DR STRING; 211586.SO_3166; -.
DR PaxDb; Q8ECH6; -.
DR KEGG; son:SO_3166; -.
DR PATRIC; fig|211586.12.peg.3072; -.
DR eggNOG; COG2445; Bacteria.
DR HOGENOM; CLU_142825_1_1_6; -.
DR OMA; ACEASID; -.
DR OrthoDB; 1967941at2; -.
DR PhylomeDB; Q8ECH6; -.
DR BioCyc; SONE211586:G1GMP-2945-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0110001; C:toxin-antitoxin complex; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR Gene3D; 1.20.120.580; -; 1.
DR InterPro; IPR008201; HepT-like.
DR InterPro; IPR037038; HepT-like_sf.
DR Pfam; PF01934; DUF86; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Toxin-antitoxin system.
FT CHAIN 1..133
FT /note="mRNA nuclease HepT"
FT /id="PRO_0000452433"
FT MOTIF 97..104
FT /note="RX(4)HXY motif"
FT /evidence="ECO:0000269|PubMed:26112399,
FT ECO:0000269|PubMed:33045733"
FT ACT_SITE 97
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT ACT_SITE 102
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT MOD_RES 104
FT /note="O-tri-AMP-tyrosine"
FT /evidence="ECO:0000269|PubMed:33045733,
FT ECO:0000269|PubMed:33290744, ECO:0007744|PDB:6M6V,
FT ECO:0007744|PDB:7AER"
FT MUTAGEN 15
FT /note="C->R: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26112399"
FT MUTAGEN 56
FT /note="H->P: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26112399"
FT MUTAGEN 70
FT /note="R->H: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26112399"
FT MUTAGEN 94
FT /note="V->G: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26112399"
FT MUTAGEN 97
FT /note="R->G: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26112399"
FT MUTAGEN 98
FT /note="N->T: Loss of toxicity; when associated with C-104."
FT /evidence="ECO:0000269|PubMed:26112399"
FT MUTAGEN 102
FT /note="H->A: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26112399"
FT MUTAGEN 104
FT /note="Y->A: No loss of toxicity. No longer AMPylated by
FT MntA."
FT /evidence="ECO:0000269|PubMed:26112399,
FT ECO:0000269|PubMed:33045733"
FT MUTAGEN 107
FT /note="L->H: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26112399"
FT MUTAGEN 118
FT /note="H->P: Loss of toxicity."
FT /evidence="ECO:0000269|PubMed:26112399"
FT HELIX 3..23
FT /evidence="ECO:0007829|PDB:6M6U"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 33..60
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:6M6U"
SQ SEQUENCE 133 AA; 15313 MW; C67F273B099C7F03 CRC64;
MNDIIINKIA TIKRCIKRIQ QVYGDGSQFK QDFTLQDSVI LNLQRCCEAC IDIANHINRQ
QQLGIPQSSR DSFTLLAQNN LITQPLSDNL KKMVGLRNIA VHDYQELNLD IVVHVVQHHL
EDFEQFIDVI KAE
