RMNT_BPP22
ID RMNT_BPP22 Reviewed; 83 AA.
AC P03049; Q7PCJ4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 02-JUN-2021, entry version 124.
DE RecName: Full=Regulatory protein mnt;
GN Name=mnt;
OS Salmonella phage P22 (Bacteriophage P22).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10754;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6350606; DOI=10.1016/s0022-2836(83)80070-9;
RA Sauer R.T., Krovatin W., Deanda J., Youderian P., Susskind M.M.;
RT "Primary structure of the immI immunity region of bacteriophage P22.";
RL J. Mol. Biol. 168:699-713(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA Vander Byl C.S., Kropinski A.M.B.;
RT "Sequence of the genome of Salmonella bacteriophage P22.";
RL J. Bacteriol. 182:6472-6481(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA Casjens S.R.;
RT "Corrected sequence of the bacteriophage P22 genome.";
RL J. Bacteriol. 185:1475-1477(2003).
RN [4]
RP STRUCTURE BY NMR OF 1-77.
RX PubMed=7999761; DOI=10.1021/bi00254a012;
RA Burgering M.J.M., Boelens R., Gilbert D.E., Breg J.N., Knight K.L.,
RA Sauer R.T., Kaptein R.;
RT "Solution structure of dimeric Mnt repressor (1-76).";
RL Biochemistry 33:15036-15045(1994).
RN [5]
RP STRUCTURE BY NMR OF 53-83.
RX PubMed=10426954; DOI=10.1038/11531;
RA Nooren I.M., Kaptein R., Sauer R.T., Boelens R.;
RT "The tetramerization domain of the Mnt repressor consists of two right-
RT handed coiled coils.";
RL Nat. Struct. Biol. 6:755-759(1999).
CC -!- FUNCTION: Mnt acts as a transcriptional repressor of genes ant and arc.
CC -!- SUBUNIT: Binds DNA as a homotetramer.
CC -!- SIMILARITY: Belongs to the p22 arc/mnt family. {ECO:0000305}.
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DR EMBL; X01916; CAA25989.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75057.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA00978.1; -; Genomic_DNA.
DR PIR; A03585; RGBPM2.
DR RefSeq; NP_059641.1; NC_002371.2.
DR PDB; 1MNT; NMR; -; A/B=2-77.
DR PDB; 1QEY; NMR; -; A/B/C/D=53-83.
DR PDBsum; 1MNT; -.
DR PDBsum; 1QEY; -.
DR BMRB; P03049; -.
DR SMR; P03049; -.
DR PRIDE; P03049; -.
DR GeneID; 1262808; -.
DR KEGG; vg:1262808; -.
DR EvolutionaryTrace; P03049; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.1220.10; -; 1.
DR InterPro; IPR005569; Arc_DNA-bd_dom.
DR InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR InterPro; IPR024421; Phage_P22_Mnt.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
DR Pfam; PF03869; Arc; 1.
DR Pfam; PF11423; Repressor_Mnt; 1.
DR SUPFAM; SSF47598; SSF47598; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..83
FT /note="Regulatory protein mnt"
FT /id="PRO_0000077736"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:1MNT"
FT HELIX 14..22
FT /evidence="ECO:0007829|PDB:1MNT"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:1MNT"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:1MNT"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1MNT"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:1MNT"
SQ SEQUENCE 83 AA; 9678 MW; 992188ECC78DBBAE CRC64;
MARDDPHFNF RMPMEVREKL KFRAEANGRS MNSELLQIVQ DALSKPSPVT GYRNDAERLA
DEQSELVKKM VFDTLKDLYK KTT
