ID   REGB_BPT4               Reviewed;         153 AA.
AC   P13312;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   02-JUN-2021, entry version 85.
DE   RecName: Full=Endoribonuclease RegB;
DE            EC=3.1.-.-;
DE   AltName: Full=Gp61.9;
GN   Name=regB; Synonyms=61.9;
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   IDENTIFICATION OF PROTEIN, AND FUNCTION.
RX   PubMed=2488272;
RA   Ruckman J., Parma D., Tuerk C., Hall D.H., Gold L.;
RT   "Identification of a T4 gene required for bacteriophage mRNA processing.";
RL   New Biol. 1:54-65(1989).
RN   [4]
RP   FUNCTION, SUBSTRATE SPECIFICITY, AND ACTIVITY REGULATION.
RX   PubMed=17130171; DOI=10.1093/nar/gkl911;
RA   Durand S., Richard G., Bisaglia M., Laalami S., Bontems F., Uzan M.;
RT   "Activation of RegB endoribonuclease by S1 ribosomal protein requires an 11
RT   nt conserved sequence.";
RL   Nucleic Acids Res. 34:6549-6560(2006).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=17046813; DOI=10.1074/jbc.m608271200;
RA   Odaert B., Saida F., Aliprandi P., Durand S., Crechet J.B., Guerois R.,
RA   Laalami S., Uzan M., Bontems F.;
RT   "Structural and functional studies of RegB, a new member of a family of
RT   sequence-specific ribonucleases involved in mRNA inactivation on the
RT   ribosome.";
RL   J. Biol. Chem. 282:2019-2028(2007).
CC   -!- FUNCTION: Essential to the early nucleolytic processing of a number of
CC       T4 messenger RNAs. Specifically cleaves after the GG dinucleotide GGAG
CC       within consensus 5'-GGAGRAYARAA-3' (R is a purine and Y is a
CC       pyrimidine) sequences found mainly in translation initiation sites.
CC       {ECO:0000269|PubMed:17130171, ECO:0000269|PubMed:2488272}.
CC   -!- ACTIVITY REGULATION: Activity is stimulated 10- to 100-fold by host
CC       ribosomal protein S1, which also helps confer substrate choice.
CC       {ECO:0000269|PubMed:17130171}.
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DR   EMBL; X04567; CAA28227.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42652.1; -; Genomic_DNA.
DR   RefSeq; NP_049726.1; NC_000866.4.
DR   PDB; 2HX6; NMR; -; A=1-153.
DR   PDBsum; 2HX6; -.
DR   BMRB; P13312; -.
DR   SMR; P13312; -.
DR   GeneID; 1258703; -.
DR   KEGG; vg:1258703; -.
DR   BRENDA; 4.6.1.25; 732.
DR   EvolutionaryTrace; P13312; -.
DR   Proteomes; UP000009087; Genome.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   InterPro; IPR019653; T4_endoribonuclease_RegB.
DR   Pfam; PF10715; REGB_T4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..153
FT                   /note="Endoribonuclease RegB"
FT                   /id="PRO_0000164973"
FT   HELIX           4..36
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   HELIX           47..55
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   HELIX           62..69
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   HELIX           70..73
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   HELIX           74..81
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   STRAND          82..84
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   STRAND          88..92
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   STRAND          102..108
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   STRAND          111..117
FT                   /evidence="ECO:0007829|PDB:2HX6"
FT   STRAND          125..136
FT                   /evidence="ECO:0007829|PDB:2HX6"
SQ   SEQUENCE   153 AA;  17977 MW;  D61494E883F4C9D5 CRC64;
     MTINTEVFIR RNKLRRHFES EFRQINNEIR EASKAAGVSS FHLKYSQHLL DRAIQREIDE
     TYVFELFHKI KDHVLEVNEF LSMPPRPDID EDFIDGVEYR PGRLEITDGN LWLGFTVCKP
     NEKFKDPSLQ CRMAIINSRR LPGKASKAVI KTQ