REPC_BPMU
ID REPC_BPMU Reviewed; 196 AA.
AC P06019;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 02-JUN-2021, entry version 108.
DE RecName: Full=Repressor protein c;
DE Short=Repc;
DE AltName: Full=CI;
DE AltName: Full=Gene product 1;
DE Short=gp1;
DE AltName: Full=Mu repressor;
DE Short=MuR;
GN Name=repc; Synonyms=c; OrderedLocusNames=Mup01;
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 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 [5]
RP DNA-BINDING.
RX PubMed=1833382; DOI=10.1128/jb.173.20.6568-6577.1991;
RA Vogel J.L., Li Z.J., Howe M.M., Toussaint A., Higgins N.P.;
RT "Temperature-sensitive mutations in the bacteriophage Mu c repressor locate
RT a 63-amino-acid DNA-binding domain.";
RL J. Bacteriol. 173:6568-6577(1991).
RN [6]
RP FUNCTION.
RX PubMed=8626285; DOI=10.1128/jb.178.6.1585-1592.1996;
RA Kahmeyer-Gabbe M., Howe M.M.;
RT "Regulatory factors acting at the bacteriophage Mu middle promoter.";
RL J. Bacteriol. 178:1585-1592(1996).
RN [7]
RP SUBUNIT.
RX PubMed=9546656; DOI=10.1046/j.1432-1327.1998.2520408.x;
RA Alazard R., Ebel C., Venien-Bryan V., Mourey L., Samama J.P., Chandler M.;
RT "Oligomeric structure of the repressor of the bacteriophage Mu early
RT operon.";
RL Eur. J. Biochem. 252:408-415(1998).
RN [8]
RP FUNCTION.
RX PubMed=11517307; DOI=10.1073/pnas.171620598;
RA Ranquet C., Geiselmann J., Toussaint A.;
RT "The tRNA function of SsrA contributes to controlling repression of
RT bacteriophage Mu prophage.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10220-10225(2001).
RN [9]
RP FUNCTION.
RX PubMed=12217693; DOI=10.1016/s0022-2836(02)00755-6;
RA O'Handley D., Nakai H.;
RT "Derepression of bacteriophage mu transposition functions by truncated
RT forms of the immunity repressor.";
RL J. Mol. Biol. 322:311-324(2002).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=16154589; DOI=10.1016/j.jmb.2005.08.015;
RA Ranquet C., Toussaint A., de Jong H., Maenhaut-Michel G., Geiselmann J.;
RT "Control of bacteriophage mu lysogenic repression.";
RL J. Mol. Biol. 353:186-195(2005).
RN [11]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF VAL-183; LYS-193 AND VAL-196.
RX PubMed=18230617; DOI=10.1074/jbc.m705508200;
RA Marshall-Batty K.R., Nakai H.;
RT "Activation of a dormant ClpX recognition motif of bacteriophage Mu
RT repressor by inducing high local flexibility.";
RL J. Biol. Chem. 283:9060-9070(2008).
RN [12]
RP STRUCTURE BY NMR OF 1-59, AND DNA-BINDING.
RX PubMed=11135677; DOI=10.1038/83103;
RA Wojciak J.M., Iwahara J., Clubb R.T.;
RT "The Mu repressor-DNA complex contains an immobilized 'wing' within the
RT minor groove.";
RL Nat. Struct. Biol. 8:84-90(2001).
CC -!- FUNCTION: Promotes latency by binding operators O1 and O2 in the
CC enhancer/operator region, thereby repressing the transcription from the
CC Pe (early) promoter and blocking the expression of the genes required
CC for replication (lytic growth). Competes with DDE-recombinase A for
CC binding to the internal activation sequence (IAS), which overlaps O1
CC and O2. The outcome of this competition determines if the virus enters
CC latency or starts replication. Makes the cell immune to superinfection
CC by repressing genes expression of any subsequent incoming viral genome.
CC {ECO:0000269|PubMed:11517307, ECO:0000269|PubMed:12217693,
CC ECO:0000269|PubMed:16154589, ECO:0000269|PubMed:18230617,
CC ECO:0000269|PubMed:8626285}.
CC -!- SUBUNIT: Homodimer. Three homodimers assemble as a homohexamer
CC (Probable). {ECO:0000305|PubMed:9546656}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC When present at high concentration, negatively regulates its own
CC expression by binding to O3 (PcM promoter). PcM promoter, and thus Repc
CC expression, is blocked by Ner. The host SsrA, the ClpXP host protease
CC that degrades Repressor c protein, the Lon protease, and the stationary
CC phase-specific sigma factor RpoS are all influencing Mu repression in
CC response to either temperature or stationary growth phase. Decreased
CC availability of host SsrA in growing cells would favor latency, whereas
CC starvation would favor Repc degradation and hence induction.
CC {ECO:0000269|PubMed:16154589, ECO:0000269|PubMed:2524470}.
CC -!- DOMAIN: The winged HTH N-terminal domain cooperatively binds to three
CC operators O1, O2, and O3 with respectively 3, 4 and 2 binding sites.
CC The C-terminal domain (CTD) regulates DNA binding by the N-terminal
CC domain and degradation by ClpX-ClpP protease.
CC {ECO:0000269|PubMed:18230617}.
CC -!- PTM: C-terminally truncated forms act as exceptionally stable
CC repressors that prevent prophage induction.
CC -!- SIMILARITY: Belongs to the mulikevirus repressor c protein family.
CC {ECO:0000305}.
CC -!- CAUTION: Translation initiates from a non-canonical start codon (UUG).
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32376.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF01132.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA24711.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; V01464; CAA24711.1; ALT_INIT; Genomic_DNA.
DR EMBL; M64097; AAA32376.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF083977; AAF01132.1; ALT_INIT; Genomic_DNA.
DR PIR; S07291; S07291.
DR RefSeq; NP_050605.1; NC_000929.1.
DR PDB; 1G4D; NMR; -; A=13-81.
DR PDB; 1QPM; NMR; -; A=13-81.
DR PDBsum; 1G4D; -.
DR PDBsum; 1QPM; -.
DR SMR; P06019; -.
DR GeneID; 2636266; -.
DR KEGG; vg:2636266; -.
DR EvolutionaryTrace; P06019; -.
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 GO; GO:0098689; P:latency-replication decision; IEA:UniProtKB-KW.
DR GO; GO:0019042; P:viral latency; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR003314; Mu-type_HTH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF02316; HTH_Tnp_Mu_1; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR PROSITE; PS51702; HTH_MU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Early protein; Host cytoplasm;
KW Host-virus interaction; Latency-replication decision; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Viral latency;
KW Viral latency initiation and maintenance.
FT CHAIN 1..196
FT /note="Repressor protein c"
FT /id="PRO_0000077589"
FT DOMAIN 13..81
FT /note="HTH Mu-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01039"
FT REGION 192..196
FT /note="Recognition by host ClpX-ClpP"
FT MUTAGEN 183
FT /note="V->S: Resistant to ClpX-ClpP degradation."
FT /evidence="ECO:0000269|PubMed:18230617"
FT MUTAGEN 193
FT /note="K->S: Resistant to ClpX-ClpP degradation."
FT /evidence="ECO:0000269|PubMed:18230617"
FT MUTAGEN 196
FT /note="V->S: Resistant to ClpX-ClpP degradation."
FT /evidence="ECO:0000269|PubMed:18230617"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:1G4D"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:1G4D"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1G4D"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:1G4D"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1G4D"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1G4D"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:1G4D"
SQ SEQUENCE 196 AA; 21822 MW; 11BFBDF143934E88 CRC64;
MKSNFIEKNN TEKSIWCSPQ EIMAADGMPG SVAGVHYRAN VQGWTKQKKE GVKGGKAVEY
DVMSMPTKER EQVIAHLGLS TPDTGAQANE KQDSSELINK LTTTLINMIE ELEPDEARKA
LKLLSKGGLL ALMPLVFNEQ KLYSFIGFSQ QSIQTLMMLD ALPEEKRKEI LSKYGIHEQE
SVVVPSQEPQ EVKKAV
