MNTA_HAEIN
ID MNTA_HAEIN Reviewed; 114 AA.
AC P43933;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable protein adenylyltransferase MntA;
DE EC=2.7.7.n1 {ECO:0000250|UniProtKB:A0A0B0QJN8};
DE AltName: Full=Probable antitoxin MntA;
GN Name=mntA; OrderedLocusNames=HI_0073;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP SUBUNIT.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=12486719; DOI=10.1002/prot.10260;
RA Lehmann C., Lim K., Chalamasetty V.R., Krajewski W., Melamud E., Galkin A.,
RA Howard A., Kelman Z., Reddy P.T., Murzin A.G., Herzberg O.;
RT "The HI0073/HI0074 protein pair from Haemophilus influenzae is a member of
RT a new nucleotidyltransferase family: structure, sequence analyses, and
RT solution studies.";
RL Proteins 50:249-260(2003).
RN [3]
RP POSSIBLE FUNCTION.
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:1NO5}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC, POSSIBLE
RP NUCLEOTIDE-BINDING, AND COFACTOR.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=16028221; DOI=10.1002/prot.20586;
RA Lehmann C., Pullalarevu S., Krajewski W., Willis M.A., Galkin A.,
RA Howard A., Herzberg O.;
RT "Structure of HI0073 from Haemophilus influenzae, the nucleotide-binding
RT domain of a two-protein nucleotidyl transferase.";
RL Proteins 60:807-811(2005).
CC -!- FUNCTION: Probable antitoxin component of a type VII toxin-antitoxin
CC (TA) system. Neutralizes cognate toxic HEPN probably by di-AMPylation
CC (Probable). A mixture of HepT and MntA binds nucleotides; the highest
CC affinity is for TTP, ATP binds more tightly than ADP or AMP
CC (PubMed:16028221). {ECO:0000269|PubMed:16028221,
CC ECO:0000305|PubMed:29555683}.
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:0000250|UniProtKB:A0A0B0QJN8};
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:0000250|UniProtKB:A0A0B0QJN8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:16028221};
CC Note=Binds 2 divalent metal cations, probably Mg(2+) in vivo, Zn(2+)
CC ions are found in the crystal structure. {ECO:0000305|PubMed:16028221};
CC -!- SUBUNIT: Forms a complex with HepT, probably with a stoichiometry of
CC 2:2. {ECO:0000269|PubMed:12486719}.
CC -!- SIMILARITY: Belongs to the MntA antitoxin family. {ECO:0000305}.
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DR EMBL; L42023; AAC21758.1; -; Genomic_DNA.
DR PIR; E64000; E64000.
DR RefSeq; NP_438246.1; NC_000907.1.
DR RefSeq; WP_005693849.1; NC_000907.1.
DR PDB; 1NO5; X-ray; 1.80 A; A/B=1-114.
DR PDBsum; 1NO5; -.
DR AlphaFoldDB; P43933; -.
DR SMR; P43933; -.
DR STRING; 71421.HI_0073; -.
DR REBASE; 191853; S1.Apa1447ORF2799P.
DR REBASE; 191857; S1.Apa1447ORF3031P.
DR REBASE; 191869; S1.Apa1342ORF2943P.
DR REBASE; 191874; S2.Apa1342ORF3157P.
DR EnsemblBacteria; AAC21758; AAC21758; HI_0073.
DR KEGG; hin:HI_0073; -.
DR PATRIC; fig|71421.8.peg.74; -.
DR eggNOG; COG1708; Bacteria.
DR HOGENOM; CLU_130257_5_2_6; -.
DR OMA; WVFGSRI; -.
DR PhylomeDB; P43933; -.
DR BioCyc; HINF71421:G1GJ1-74-MON; -.
DR EvolutionaryTrace; P43933; -.
DR Proteomes; UP000000579; Chromosome.
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; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Toxin-antitoxin system;
KW Transferase.
FT CHAIN 1..114
FT /note="Probable protein adenylyltransferase MntA"
FT /id="PRO_0000077881"
FT MOTIF 34..48
FT /note="GSX(10)DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q8ECH7"
FT ACT_SITE 46
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJN8"
FT ACT_SITE 48
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJN8"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000305|PubMed:16028221,
FT ECO:0007744|PDB:1NO5"
FT BINDING 46
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000305|PubMed:16028221,
FT ECO:0007744|PDB:1NO5"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000305|PubMed:16028221,
FT ECO:0007744|PDB:1NO5"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000305|PubMed:16028221,
FT ECO:0007744|PDB:1NO5"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000305|PubMed:16028221,
FT ECO:0007744|PDB:1NO5"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000305|PubMed:16028221,
FT ECO:0007744|PDB:1NO5"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain A"
FT /evidence="ECO:0000305|PubMed:16028221,
FT ECO:0007744|PDB:1NO5"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in chain B"
FT /evidence="ECO:0000305|PubMed:16028221,
FT ECO:0007744|PDB:1NO5"
FT HELIX 11..24
FT /evidence="ECO:0007829|PDB:1NO5"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1NO5"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1NO5"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1NO5"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1NO5"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:1NO5"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1NO5"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1NO5"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:1NO5"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1NO5"
SQ SEQUENCE 114 AA; 13179 MW; B1367D6644F61DF6 CRC64;
MTSFAQLDIK SEELAIVKTI LQQLVPDYTV WAFGSRVKGK AKKYSDLDLA IISEEPLDFL
ARDRLKEAFS ESDLPWRVDL LDWATTSEDF REIIRKVYVV IQEKEKTVEK PTAL
