HEPT_HAEIN
ID HEPT_HAEIN Reviewed; 146 AA.
AC P43934;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Probable ribonuclease HepT;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8ECH6};
DE AltName: Full=Probable toxin HepT;
GN Name=hepT; OrderedLocusNames=HI_0074;
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 POSSIBLE NUCLEOTIDE-BINDING.
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).
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:1JOG}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND 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).
CC -!- FUNCTION: Probable toxic component of a type VII toxin-antitoxin (TA)
CC system, probably an RNase. Neutralized by cognate antitoxin MntA.
CC Neutralization is probably due to AMPylation by MntA (Probable). A
CC mixture of HepT and MntA binds nucleotides; the highest affinity is for
CC TTP, ATP binds more tightly than ADP or AMP (PubMed:16028221).
CC {ECO:0000269|PubMed:16028221, ECO:0000305|PubMed:29555683}.
CC -!- SUBUNIT: Homodimer. Forms a complex with MntA, probably with a
CC stoichiometry of 2:2. {ECO:0000269|PubMed:12486719}.
CC -!- PTM: Modified by cognate antitoxin MntA; probably at least 2 successive
CC AMPylation events occur on Tyr-113. {ECO:0000250|UniProtKB:A0A0B0QJR1}.
CC -!- SIMILARITY: Belongs to the HepT RNase toxin 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; AAC21759.1; -; Genomic_DNA.
DR PIR; F64000; F64000.
DR RefSeq; NP_438247.1; NC_000907.1.
DR RefSeq; WP_005693848.1; NC_000907.1.
DR PDB; 1JOG; X-ray; 2.40 A; A/B/C/D=1-146.
DR PDBsum; 1JOG; -.
DR AlphaFoldDB; P43934; -.
DR SMR; P43934; -.
DR STRING; 71421.HI_0074; -.
DR EnsemblBacteria; AAC21759; AAC21759; HI_0074.
DR KEGG; hin:HI_0074; -.
DR PATRIC; fig|71421.8.peg.75; -.
DR eggNOG; COG1708; Bacteria.
DR HOGENOM; CLU_118479_0_0_6; -.
DR OMA; QISDRNW; -.
DR PhylomeDB; P43934; -.
DR BioCyc; HINF71421:G1GJ1-75-MON; -.
DR EvolutionaryTrace; P43934; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR InterPro; IPR010235; HepT.
DR Pfam; PF08780; NTase_sub_bind; 1.
DR TIGRFAMs; TIGR01987; HI0074; 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..146
FT /note="Probable ribonuclease HepT"
FT /id="PRO_0000077882"
FT MOTIF 106..113
FT /note="RX(4)HXY motif"
FT /evidence="ECO:0000305|PubMed:29555683"
FT ACT_SITE 106
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT ACT_SITE 111
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT MOD_RES 113
FT /note="O-di-AMP-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:A0A0B0QJR1"
FT HELIX 8..26
FT /evidence="ECO:0007829|PDB:1JOG"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1JOG"
FT HELIX 36..68
FT /evidence="ECO:0007829|PDB:1JOG"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1JOG"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:1JOG"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1JOG"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:1JOG"
FT HELIX 125..140
FT /evidence="ECO:0007829|PDB:1JOG"
SQ SEQUENCE 146 AA; 17128 MW; 1DF7C7C199701999 CRC64;
MMTDKLNLNV LDAAFYSLEQ TVVQISDRNW FDMQPSIVQD TLIAGAIQKF EFVYELSLKM
MKRQLQQDAI NTDDIGAYGF KDILREALRF GLIGDMSKWV AYRDMRNITS HTYDQEKAMA
VYAQIDDFLI ESSFLLEQLR QRNQYD
