MNTA_APHF2
ID MNTA_APHF2 Reviewed; 150 AA.
AC A0A0B0QJN8;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Protein adenylyltransferase MntA {ECO:0000303|PubMed:33290744};
DE EC=2.7.7.n1 {ECO:0000269|PubMed:33290744};
DE AltName: Full=Antitoxin MNT {ECO:0000303|PubMed:33290744};
DE AltName: Full=Minimal nucleotidyltransferase {ECO:0000303|PubMed:33290744};
DE AltName: Full=Protein adenylyltransferase MNT {ECO:0000303|PubMed:33290744};
GN Name=mntA {ECO:0000305}; Synonyms=mnt {ECO:0000303|PubMed:33290744};
GN ORFNames=OA07_26450;
OS Aphanizomenon flos-aquae (strain 2012/KM1/D3).
OC Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Aphanizomenon.
OX NCBI_TaxID=1532906;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2012/KM1/D3;
RX PubMed=25593252; DOI=10.1128/genomea.01392-14;
RA Sulcius S., Alzbutas G., Kvederaviciute K., Koreiviene J., Zakrys L.,
RA Lubys A., Paskauskas R.;
RT "Draft Genome Sequence of the Cyanobacterium Aphanizomenon flos-aquae
RT Strain 2012/KM1/D3, Isolated from the Curonian Lagoon (Baltic Sea).";
RL Genome Announc. 3:0-0(2015).
RN [2] {ECO:0007744|PDB:7AE2, ECO:0007744|PDB:7AE9}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEPT, FUNCTION AS AN
RP ANTITOXIN, FUNCTION AS AN ADENYLYLTRANSFERASE, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, PROBABLE ACTIVE SITE, AND
RP MUTAGENESIS OF PHE-31; 44-ASP--ASP-46; ASP-44 AND 127-ASN--VAL-150.
RC STRAIN=2012/KM1/D3;
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 cloning in E.coli neutralizes the effect of cognate toxin
CC HepT. Neutralization is mostly due to di-AMPylation of toxin by this
CC enzyme. Successively di-AMPylates HepT on 'Tyr-109'. In vitro will use
CC ATP, dATP, GTP, dGTP, TTP or UTP to generate a mono-modified protein,
CC but requires a purine nucleotide for the second modification reaction
CC (ATP, dATP or GTP). {ECO:0000269|PubMed:33290744}.
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:33290744};
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:33290744};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:33290744};
CC Note=Mn(2+) works as well as Mg(2+), Co(2+), Ni(2+) and Zn(2+) work
CC less well (PubMed:33290744). Bind 2 Mg(2+) per subunit (By similarity).
CC {ECO:0000250|UniProtKB:Q8ECH7, ECO:0000269|PubMed:33290744};
CC -!- SUBUNIT: Forms a complex with HepT, probably MntA(1):HepT(2) in vivo;
CC can only be purified when both 'Arg-102' and 'Tyr-109' (or 'His-107'
CC and 'Tyr-109') of HepThave been mutated. The fully di-AMPylated HepT
CC homodimer is not found in a complex with MntA.
CC {ECO:0000269|PubMed:33290744}.
CC -!- MISCELLANEOUS: Part of a locus that includes subtype I-D CRISPR-Cas
CC genes. {ECO:0000269|PubMed:25593252}.
CC -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR EMBL; JSDP01000312; KHG38970.1; -; Genomic_DNA.
DR RefSeq; WP_039205097.1; NZ_JSDP01000312.1.
DR PDB; 7AE2; X-ray; 2.00 A; B=1-150.
DR PDB; 7AE9; X-ray; 2.90 A; E/F/G/H=1-147.
DR PDBsum; 7AE2; -.
DR PDBsum; 7AE9; -.
DR AlphaFoldDB; A0A0B0QJN8; -.
DR SMR; A0A0B0QJN8; -.
DR EnsemblBacteria; KHG38970; KHG38970; OA07_26450.
DR GO; GO:0005524; F:ATP 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; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Toxin-antitoxin system; Transferase; Virulence.
FT CHAIN 1..150
FT /note="Protein adenylyltransferase MntA"
FT /id="PRO_0000452435"
FT MOTIF 32..46
FT /note="GSX(10)DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT ACT_SITE 44
FT /evidence="ECO:0000305|PubMed:33290744"
FT ACT_SITE 46
FT /evidence="ECO:0000305|PubMed:33290744"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT MUTAGEN 31
FT /note="F->A: Very small amounts of HepT are di-AMPylated."
FT /evidence="ECO:0000269|PubMed:33290744"
FT MUTAGEN 44..46
FT /note="DWD->AWA: No longer neutralizes HepT, no di-
FT AMPylation of HepT."
FT /evidence="ECO:0000269|PubMed:33290744"
FT MUTAGEN 44
FT /note="D->A: No longer neutralizes HepT, no di-AMPylation
FT of HepT."
FT /evidence="ECO:0000269|PubMed:33290744"
FT MUTAGEN 127..150
FT /note="Missing: No di-AMPylation of HepT."
FT /evidence="ECO:0000269|PubMed:33290744"
FT HELIX 8..14
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:7AE2"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:7AE2"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:7AE2"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:7AE2"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:7AE2"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:7AE2"
FT HELIX 127..148
FT /evidence="ECO:0007829|PDB:7AE2"
SQ SEQUENCE 150 AA; 17359 MW; E5FBA0D4762FB635 CRC64;
MQDKIPTIAE LRELSLRLLT KIPYLKMLVL FGSRATGNIN ANSDWDFAVL YDEEKYNLYI
QNNPLAAFVI PGILGEIFKI NSDKIDIVEL NHCSKLIAHF VARDGKVLYE EPGDEFDKFQ
QRVLLSNTEI KKIEKTKLEN IENFLQRWGV
