NER_BPMU
ID NER_BPMU Reviewed; 75 AA.
AC P06020;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Negative regulator of transcription;
DE Short=Ner;
DE AltName: Full=Gene product 2;
DE Short=gp2;
GN Name=ner; Synonyms=CII; OrderedLocusNames=Mup02;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6214696; DOI=10.1007/bf00729448;
RA Priess H., Kamp D., Kahmann R., Braeuer B., Delius H.;
RT "Nucleotide sequence of the immunity region of bacteriophage Mu.";
RL Mol. Gen. Genet. 186:315-321(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Priess H., Brauer B., Schmidt C., Kamp D.;
RT "Sequence of the left end of Mu.";
RL (In) Symonds N., Toussaint A., van de Putte P., Howe M.M. (eds.);
RL Phage Mu, pp.277-296, Cold Spring Harbor Laboratory Press, New York (1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [4]
RP PROTEIN SEQUENCE OF 2-75.
RX PubMed=2970420; DOI=10.1016/0378-1119(88)90462-3;
RA Allet B., Payton M., Mattaliano R.J., Gronenborn A.M., Clore G.M.,
RA Wingfield P.T.;
RT "Purification and characterization of the DNA-binding protein Ner of
RT bacteriophage Mu.";
RL Gene 65:259-268(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-75.
RX PubMed=6222246; DOI=10.1007/bf00330326;
RA Toussaint A., Faelen M., Desmet L., Allet B.;
RT "The products of gene A of the related phages Mu and D108 differ in their
RT specificities.";
RL Mol. Gen. Genet. 190:70-79(1983).
RN [6]
RP FUNCTION.
RX PubMed=3015876; DOI=10.1128/jb.167.2.503-507.1986;
RA Goosen N., van de Putte P.;
RT "Role of ner protein in bacteriophage Mu transposition.";
RL J. Bacteriol. 167:503-507(1986).
RN [7]
RP CHARACTERIZATION.
RX PubMed=2537762; DOI=10.1016/0014-5793(89)80565-4;
RA Kukolj G., Tolias P.P., DuBow M.S.;
RT "Purification and characterization of the Ner repressor of bacteriophage
RT Mu.";
RL FEBS Lett. 244:369-375(1989).
RN [8]
RP INDUCTION.
RX PubMed=2524470; DOI=10.1128/jb.171.6.3440-3448.1989;
RA Stoddard S.F., Howe M.M.;
RT "Localization and regulation of bacteriophage Mu promoters.";
RL J. Bacteriol. 171:3440-3448(1989).
RN [9]
RP POST-TRANSLATIONAL MODIFICATIONS.
RX PubMed=1388164; DOI=10.1016/s0021-9258(18)41747-4;
RA Rose K., Simona M.G., Savoy L.-A., Regamey P.-O., Green B.N., Clore G.M.,
RA Gronenborn A.M., Wingfield P.T.;
RT "Pyruvic acid is attached through its central carbon atom to the amino
RT terminus of the recombinant DNA-derived DNA-binding protein Ner of
RT bacteriophage Mu.";
RL J. Biol. Chem. 267:19101-19106(1992).
RN [10]
RP DNA-BINDING.
RX PubMed=7893708; DOI=10.1021/bi00009a026;
RA Strzelecka T.E., Hayes J.J., Clore G.M., Gronenborn A.M.;
RT "DNA binding specificity of the Mu Ner protein.";
RL Biochemistry 34:2946-2955(1995).
RN [11]
RP STRUCTURE BY NMR.
RX PubMed=8590003; DOI=10.1016/s0969-2126(01)00244-1;
RA Strzelecka T.E., Clore G.M., Gronenborn A.M.;
RT "The solution structure of the Mu Ner protein reveals a helix-turn-helix
RT DNA recognition motif.";
RL Structure 3:1087-1095(1995).
CC -!- FUNCTION: Switches off the PcM promoter thereby blocking expression of
CC the major repressor Repc (latency factor) and favoring transcription
CC from the early promoter (Pe) and hence viral transposition and lytic
CC development. Negatively regulates the early promoter (Pe) thereby
CC controlling its own expression and keeping the level of early genes
CC expression independent of the viral genome copy number.
CC {ECO:0000269|PubMed:3015876}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC Early gene transcription is repressed by viral Repc (latency) and
CC favored by viral Ner protein (lytic development).
CC {ECO:0000269|PubMed:2524470}.
CC -!- SIMILARITY: Belongs to the ner transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; V01464; CAA24712.1; -; Genomic_DNA.
DR EMBL; M64097; AAA32378.1; -; Genomic_DNA.
DR EMBL; AF083977; AAF01082.1; -; Genomic_DNA.
DR EMBL; V00868; CAA24235.1; -; Genomic_DNA.
DR PIR; S09549; DNBPNU.
DR RefSeq; NP_050606.1; NC_000929.1.
DR PDB; 1NEQ; NMR; -; A=2-75.
DR PDB; 1NER; NMR; -; A=2-75.
DR PDBsum; 1NEQ; -.
DR PDBsum; 1NER; -.
DR BMRB; P06020; -.
DR SMR; P06020; -.
DR GeneID; 2636289; -.
DR KEGG; vg:2636289; -.
DR EvolutionaryTrace; P06020; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR038722; Ner_HTH_dom.
DR Pfam; PF13693; HTH_35; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding; Early protein;
KW Host cytoplasm; Pyruvate; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:2970420"
FT CHAIN 2..75
FT /note="Negative regulator of transcription"
FT /id="PRO_0000062784"
FT DNA_BIND 26..45
FT /note="H-T-H motif"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-pyruvate 2-iminyl-cysteine; by host"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1NEQ"
FT HELIX 12..20
FT /evidence="ECO:0007829|PDB:1NEQ"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1NEQ"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:1NEQ"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1NEQ"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:1NEQ"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:1NEQ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1NEQ"
SQ SEQUENCE 75 AA; 8506 MW; 10195EBFBE103276 CRC64;
MCSNEKARDW HRADVIAGLK KRKLSLSALS RQFGYAPTTL ANALERHWPK GEQIIANALE
TKPEVIWPSR YQAGE
