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 27-MAR-2024, entry version 111. DE RecName: Full=Probable protein adenylyltransferase MntA; DE EC=2.7.7.108 {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; Pseudomonadota; 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=2.7.7.108; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L42023; AAC21758.1; -; Genomic_DNA. DR PIR; E64000; E64000. DR RefSeq; NP_438246.1; 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 OrthoDB; 9808659at2; -. DR PhylomeDB; P43933; -. DR BioCyc; HINF71421:G1GJ1-74-MONOMER; -. 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 CDD; cd05403; NT_KNTase_like; 1. DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1. DR InterPro; IPR043519; NT_sf. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR PANTHER; PTHR33933; NUCLEOTIDYLTRANSFERASE; 1. DR PANTHER; PTHR33933:SF1; PROTEIN ADENYLYLTRANSFERASE MNTA-RELATED; 1. DR Pfam; PF01909; NTP_transf_2; 1. DR SUPFAM; SSF81301; Nucleotidyltransferase; 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 //