STP_BPT4
ID STP_BPT4 Reviewed; 26 AA.
AC P62765; P18788;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=T4 Suppressor of prr;
DE Short=Stp;
GN Name=stp;
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=3280805; DOI=10.1016/0022-2836(88)90320-8;
RA Chapman D., Morad I., Kaufmann G., Gait M.J., Jorissen L., Snyder L.;
RT "Nucleotide and deduced amino acid sequence of stp: the bacteriophage T4
RT anticodon nuclease gene.";
RL J. Mol. Biol. 199:373-377(1988).
RN [2]
RP SEQUENCE REVISION.
RA Kaufmann G.;
RL Unpublished observations (DEC-1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DOMAIN.
RX PubMed=7791212; DOI=10.1006/jmbi.1995.0343;
RA Penner M., Morad I., Snyder L., Kaufmann G.;
RT "Phage T4-coded Stp: double-edged effector of coupled DNA and tRNA-
RT restriction systems.";
RL J. Mol. Biol. 249:857-868(1995).
RN [4]
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 [5]
RP FUNCTION, AND SYNTHESIS OF ORIGINAL SEQUENCE.
RX PubMed=1639077; DOI=10.1002/j.1460-2075.1992.tb05385.x;
RA Amitsur M., Morad I., Chapman-Shimshoni D., Kaufmann G.;
RT "HSD restriction-modification proteins partake in latent anticodon
RT nuclease.";
RL EMBO J. 11:3129-3134(1992).
RN [6]
RP FUNCTION.
RX PubMed=14507369; DOI=10.1046/j.1365-2958.2003.03691.x;
RA Amitsur M., Benjamin S., Rosner R., Chapman-Shimshoni D., Meidler R.,
RA Blanga S., Kaufmann G.;
RT "Bacteriophage T4-encoded Stp can be replaced as activator of anticodon
RT nuclease by a normal host cell metabolite.";
RL Mol. Microbiol. 50:129-143(2003).
CC -!- FUNCTION: Plays a role in the inactivation of several host DNA
CC restriction systems including EcoprrI or EcoR124I. As a consequence, it
CC activates the host anticodon nuclease PrrC. However, the phage-encoded
CC RNA repair enzymes normally offset the damage.
CC {ECO:0000269|PubMed:14507369, ECO:0000269|PubMed:1639077,
CC ECO:0000269|PubMed:7791212}.
CC -!- DOMAIN: The conserved N-proximal 18 residue region of Stp is critical
CC both for its anti-DNA restriction and ACNase activating functions.
CC {ECO:0000269|PubMed:7791212}.
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; Z46884; CAA86982.1; -; Genomic_DNA.
DR EMBL; Z46874; CAA86954.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42660.1; -; Genomic_DNA.
DR PIR; S55796; STBPT4.
DR RefSeq; NP_049878.1; NC_000866.4.
DR GeneID; 1258673; -.
DR KEGG; vg:1258673; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:0050792; P:regulation of viral process; IEA:InterPro.
DR InterPro; IPR012585; Stp.
DR Pfam; PF08133; Nuclease_act; 1.
PE 4: Predicted;
KW Host-virus interaction; Reference proteome;
KW Restriction-modification system evasion by virus.
FT PEPTIDE 1..26
FT /note="T4 Suppressor of prr"
FT /id="PRO_0000164985"
SQ SEQUENCE 26 AA; 3184 MW; 50416719F5088D40 CRC64;
MSNFHNEHVM QFYRNNLKTK GVFGRQ