ID   VS_BPT4                 Reviewed;         115 AA.
AC   P13310;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Valyl--tRNA ligase modifier;
DE   AltName: Full=Phage factor tau;
DE   AltName: Full=Tau peptide;
GN   Name=vs;
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=3024113; DOI=10.1093/nar/14.21.8637;
RA   Valerie K., Stevens J., Lynch M., Henderson E.E., de Riel J.K.;
RT   "Nucleotide sequence and analysis of the 58.3 to 65.5-kb early region of
RT   bacteriophage T4.";
RL   Nucleic Acids Res. 14:8637-8654(1986).
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   FUNCTION.
RX   PubMed=163351; DOI=10.1128/jvi.15.2.238-243.1975;
RA   Muller U.R., Marchin G.L.;
RT   "Temporal appearance of bacteriophage T4-modified valyl tRNA synthetase in
RT   Escherichia coli.";
RL   J. Virol. 15:238-243(1975).
RN   [4]
RP   FUNCTION.
RX   PubMed=1103442; DOI=10.1016/0042-6822(75)90440-7;
RA   McClain W.H., Marchin G.L., Neidhardt F.C.;
RT   "A gene of bacteriophage T4 controlling the modification of host valyl-tRNA
RT   synthetase.";
RL   Virology 67:385-394(1975).
RN   [5]
RP   FUNCTION, AND CHARACTERIZATION.
RX   PubMed=19475; DOI=10.1016/s0021-9258(17)39895-2;
RA   Muller U.R., Marchin G.L.;
RT   "Purification and properties of a T4 bacteriophage factor that modifies
RT   valyl-tRNA synthetase of Escherichia coli.";
RL   J. Biol. Chem. 252:6640-6645(1977).
CC   -!- FUNCTION: Binds to the host (E.coli) valyl--tRNA ligase and thereby
CC       changes several of its physicochemical properties.
CC       {ECO:0000269|PubMed:1103442, ECO:0000269|PubMed:163351,
CC       ECO:0000269|PubMed:19475}.
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DR   EMBL; X04567; CAA28229.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42671.1; -; Genomic_DNA.
DR   RefSeq; NP_049724.1; NC_000866.4.
DR   PRIDE; P13310; -.
DR   GeneID; 1258658; -.
DR   KEGG; vg:1258658; -.
DR   Proteomes; UP000009087; Genome.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..115
FT                   /note="Valyl--tRNA ligase modifier"
FT                   /id="PRO_0000165073"
SQ   SEQUENCE   115 AA;  13056 MW;  0B6903F580A53FB0 CRC64;
     MTKILVLCIG LISFSASASA DTSYTEIREY VNRTAADYCG KNKACQAEFA QKLIYAYKDG
     ERDKSSRYKN DTLLKRYAKK WNTLECSVAE EKDKAACHSM VDRLVDSYNR GLSTR