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DMD_BPT4
ID   DMD_BPT4                Reviewed;          60 AA.
AC   P39232;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   23-FEB-2022, entry version 72.
DE   RecName: Full=Antitoxin Dmd;
GN   Name=dmd; Synonyms=61.5, y02B;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8383243; DOI=10.1128/jvi.67.4.2305-2316.1993;
RA   Selick H.E., Stormo G.D., Dyson R.L., Alberts B.M.;
RT   "Analysis of five presumptive protein-coding sequences clustered between
RT   the primosome genes, 41 and 61, of bacteriophages T4, T2, and T6.";
RL   J. Virol. 67:2305-2316(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=8878669; DOI=10.1093/genetics/144.1.7;
RA   Kai T., Selick H.E., Yonesaki T.;
RT   "Destabilization of bacteriophage T4 mRNAs by a mutation of gene 61.5.";
RL   Genetics 144:7-14(1996).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20421606; DOI=10.1534/genetics.110.114462;
RA   Otsuka Y., Miki K., Koga M., Katayama N., Morimoto W., Takahashi Y.,
RA   Yonesaki T.;
RT   "IscR regulates RNase LS activity by repressing rnlA transcription.";
RL   Genetics 185:823-830(2010).
RN   [5]
RP   FUNCTION AS AN ANTITOXIN, INTERACTION WITH HOST TOXINS LSOB AND RNLA, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=22403819; DOI=10.1111/j.1365-2958.2012.07975.x;
RA   Otsuka Y., Yonesaki T.;
RT   "Dmd of bacteriophage T4 functions as an antitoxin against Escherichia coli
RT   LsoA and RnlA toxins.";
RL   Mol. Microbiol. 83:669-681(2012).
RN   [6]
RP   SUBUNIT.
RX   PubMed=24112600; DOI=10.1111/mmi.12409;
RA   Wei Y., Gao Z.Q., Otsuka Y., Naka K., Yonesaki T., Zhang H., Dong Y.H.;
RT   "Structure-function studies of Escherichia coli RnlA reveal a novel toxin
RT   structure involved in bacteriophage resistance.";
RL   Mol. Microbiol. 90:956-965(2013).
CC   -!- FUNCTION: Antitoxin component of a potential type II toxin-antitoxin
CC       (TA) system. Acts as an antitoxin against host toxins RnlA and LsoA,
CC       preventing them from degrading T4 bacteriophage-derived mRNA and thus
CC       permitting successful virus infection. Stabilizes middle (8-10 minutes)
CC       and late (18 to 28 minutes) T4 gene transcripts.
CC       {ECO:0000269|PubMed:22403819}.
CC   -!- SUBUNIT: Can form a complex with non-cognate host toxins LsoA and RnlA.
CC       {ECO:0000269|PubMed:22403819, ECO:0000269|PubMed:24112600}.
CC   -!- DISRUPTION PHENOTYPE: Phage grows very poorly in wild-type E.coli K12
CC       or in cells expressing plasmid-derived toxin-antitoxin system LsoA-
CC       LsoB; if the host has a deletion in rnlA-rnlB no effect is seen.
CC       Absence of full-length transcripts of late (18 to 28 minutes) T4 genes,
CC       and thus loss of synthesis of late proteins. Partially suppressed by
CC       overexpression of host IscR. {ECO:0000269|PubMed:20421606,
CC       ECO:0000269|PubMed:22403819, ECO:0000269|PubMed:8878669}.
CC   -!- CAUTION: Enterobacteria phage T4 probably has no corresponding toxin
CC       gene. {ECO:0000305}.
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DR   EMBL; S57514; AAB25708.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42512.1; -; Genomic_DNA.
DR   PIR; A45681; A45681.
DR   RefSeq; NP_049653.1; NC_000866.4.
DR   PDB; 5HY3; X-ray; 3.10 A; B=1-60.
DR   PDBsum; 5HY3; -.
DR   SMR; P39232; -.
DR   GeneID; 1258668; -.
DR   KEGG; vg:1258668; -.
DR   Proteomes; UP000009087; Genome.
DR   InterPro; IPR035137; Dmd.
DR   Pfam; PF17587; Dmd; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Evasion of bacteria-mediated translation shutoff by virus;
KW   Host-virus interaction; Reference proteome; Toxin-antitoxin system.
FT   CHAIN           1..60
FT                   /note="Antitoxin Dmd"
FT                   /id="PRO_0000165095"
FT   STRAND          4..11
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   STRAND          17..24
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           26..28
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   HELIX           29..40
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   STRAND          43..48
FT                   /evidence="ECO:0007829|PDB:5HY3"
FT   STRAND          51..57
FT                   /evidence="ECO:0007829|PDB:5HY3"
SQ   SEQUENCE   60 AA;  7027 MW;  A726546EE9AC74B2 CRC64;
     MELVKVVFMG WFKNESMFTK EITMMKDDVQ WATTQYAEVN KALVKAFIDD KKVCEVDCRG
 
 
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