MNTA_SHEON
ID MNTA_SHEON Reviewed; 139 AA.
AC Q8ECH7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein adenylyltransferase MntA;
DE EC=2.7.7.n1 {ECO:0000269|PubMed:33045733};
DE AltName: Full=Antitoxin MntA {ECO:0000303|PubMed:33045733};
GN Name=mntA {ECO:0000303|PubMed:33045733}; OrderedLocusNames=SO_3165;
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 AN ANTITOXIN, POSSIBLE FUNCTION AS A REPRESSOR, SUBUNIT,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
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 HEPT, FUNCTION AS AN
RP ANTITOXIN, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 98-GLN--HIS-113.
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 HEPT AND MAGNESIUM,
RP FUNCTION AS AN ANTITOXIN, FUNCTION AS AN ADENYLYLTRANSFERASE, CATALYTIC
RP ACTIVITY, COFACTOR, SUBUNIT, AND MUTAGENESIS OF 27-GLY-SER-28 AND
RP 39-ASP--ASP-41.
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 HEPT.
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: Antitoxin component of a type VII toxin-antitoxin (TA)
CC system. Upon overexpression in situ or in E.coli neutralizes the effect
CC of cognate toxin HepT (PubMed:26112399, PubMed:29555683,
CC PubMed:33045733). Neutralization is mostly due to tri-AMPylation of
CC toxin by this enzyme. Successively tri-AMPylates HepT on 'Tyr-104'
CC (PubMed:33045733). Binds its own promoter, probably repressing its
CC expression. The TA system confers plasmid stability in E.coli
CC (PubMed:26112399). {ECO:0000269|PubMed:26112399,
CC ECO:0000269|PubMed:29555683, ECO:0000269|PubMed:33045733}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC Evidence={ECO:0000269|PubMed:33045733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + O-(5'-adenylyl)-L-tyrosyl-[protein] = diphosphate + O-
CC [5'-(adenylyl-(5'->3')-adenylyl)]-L-tyrosyl-[protein];
CC Xref=Rhea:RHEA:66528, Rhea:RHEA-COMP:13846, Rhea:RHEA-COMP:17046,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83624,
CC ChEBI:CHEBI:167160; Evidence={ECO:0000269|PubMed:33045733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + O-[5'-(adenylyl-(5'->3')-adenylyl)]-L-tyrosyl-[protein]
CC = diphosphate + O-[5'-(adenylyl-(5'->3')-adenylyl-(5'->3')-
CC adenylyl)]-L-tyrosyl-[protein]; Xref=Rhea:RHEA:66532, Rhea:RHEA-
CC COMP:17046, Rhea:RHEA-COMP:17047, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:167160, ChEBI:CHEBI:167161;
CC Evidence={ECO:0000269|PubMed:33045733};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:33045733};
CC Note=Binds 2 Mg(2+) per subunit. {ECO:0000269|PubMed:33045733};
CC -!- SUBUNIT: Forms a complex with cognate toxin HepT, may form a homodimer
CC by itself (PubMed:26112399). Forms a heterooctamer with cognate toxin
CC HEPN with stoichiometry HepT(6):MntA(2). The 2 MNT subunits do not
CC contact each other in the heterooctamer, each contacts 3 HEPN subunits,
CC blocking access to the toxin active site (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 autocontrol by MntA. {ECO:0000269|PubMed:26112399}.
CC -!- DOMAIN: Has 2 alpha-helices that are important for interaction with
CC cognate toxin HEPN; deletion of helix 2 (residues 52-65) or the C-
CC terminus of helix 4 (residues 114-125) reduces antitoxin function about
CC 100-fold, while deletion of the N-terminus of helix 4 (residues 98-113)
CC reduces antitoxin function over 1000-fold.
CC {ECO:0000269|PubMed:29555683}.
CC -!- DISRUPTION PHENOTYPE: When mntA-hepT is deleted, has a sight reduction
CC in swimming motility. This gene cannot be deleted when the hepT gene is
CC intact. {ECO:0000269|PubMed:26112399}.
CC -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR EMBL; AE014299; AAN56165.1; -; Genomic_DNA.
DR RefSeq; NP_718721.1; NC_004347.2.
DR RefSeq; WP_011073052.1; NZ_CP053946.1.
DR PDB; 5YEP; X-ray; 3.00 A; A=1-139.
DR PDB; 6M6U; X-ray; 2.35 A; A/F=1-139.
DR PDB; 6M6V; X-ray; 3.08 A; A=1-139.
DR PDB; 6M6W; X-ray; 2.61 A; A/F=1-139.
DR PDB; 7AER; X-ray; 3.00 A; A=1-139.
DR PDB; 7BXO; X-ray; 2.77 A; A/E=1-139.
DR PDBsum; 5YEP; -.
DR PDBsum; 6M6U; -.
DR PDBsum; 6M6V; -.
DR PDBsum; 6M6W; -.
DR PDBsum; 7AER; -.
DR PDBsum; 7BXO; -.
DR AlphaFoldDB; Q8ECH7; -.
DR SMR; Q8ECH7; -.
DR STRING; 211586.SO_3165; -.
DR PaxDb; Q8ECH7; -.
DR DNASU; 1170859; -.
DR KEGG; son:SO_3165; -.
DR PATRIC; fig|211586.12.peg.3070; -.
DR eggNOG; COG1669; Bacteria.
DR HOGENOM; CLU_130257_1_0_6; -.
DR OMA; EVIYCED; -.
DR OrthoDB; 1831955at2; -.
DR BioCyc; SONE211586:G1GMP-2944-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR041633; Polbeta.
DR Pfam; PF18765; Polbeta; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; Repressor;
KW Toxin-antitoxin system; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..139
FT /note="Protein adenylyltransferase MntA"
FT /id="PRO_0000452436"
FT MOTIF 27..41
FT /note="GSX(10)DXD motif"
FT /evidence="ECO:0000269|PubMed:33045733"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33045733,
FT ECO:0007744|PDB:7BXO"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33045733,
FT ECO:0007744|PDB:7BXO"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33045733,
FT ECO:0007744|PDB:7BXO"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:33045733,
FT ECO:0007744|PDB:7BXO"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:33045733,
FT ECO:0007744|PDB:7BXO"
FT MUTAGEN 27..28
FT /note="GS->AT: No longer AMPylates HepT, reduced ability to
FT neutralize HepT."
FT /evidence="ECO:0000269|PubMed:33045733"
FT MUTAGEN 39..41
FT /note="DID->EIE: No longer AMPylates HepT, reduced ability
FT to neutralize HepT, still binds HepT."
FT /evidence="ECO:0000269|PubMed:33045733"
FT MUTAGEN 98..113
FT /note="Missing: Significantly reduces antitoxin function,
FT reduced ability to neutralize HepT, decreased ability to
FT AMPylate HepT."
FT /evidence="ECO:0000269|PubMed:29555683"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:6M6U"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:6M6U"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:6M6U"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:6M6U"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:6M6U"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:6M6U"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6M6U"
FT HELIX 97..125
FT /evidence="ECO:0007829|PDB:6M6U"
SQ SEQUENCE 139 AA; 15567 MW; 779F5B152FDD3D33 CRC64;
MQQLNENKII KLLRDNIPKL QLIYLFGSYS QGTQHRNSDI DIAVLAADTL DNIARWELAQ
KLASALDSDV DLVDLRSAST VLCQQVVTQG KQLWGTQQDD ELFAVKTISM YQHLQAERQA
IIDDVMANTA AKAHRGESL
