ID   REPC_BPD10              Reviewed;         174 AA.
AC   P07040; C9DGK9;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   23-FEB-2022, entry version 91.
DE   RecName: Full=Repressor c protein;
DE            Short=Repc;
DE   AltName: Full=CI;
GN   Name=repc; Synonyms=c;
OS   Escherichia phage D108 (Bacteriophage D108).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Muvirus; unclassified Muvirus.
OX   NCBI_TaxID=665033;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3012481; DOI=10.1093/nar/14.9.3813;
RA   Mizuuchi M., Weisberg R.A., Mizuuchi K.;
RT   "DNA sequence of the control region of phage D108: the N-terminal amino
RT   acid sequences of repressor and transposase are similar both in phage D108
RT   and in its relative, phage Mu.";
RL   Nucleic Acids Res. 14:3813-3825(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kropinski A.M., Villegas A., Lingohr E.J.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Three homodimers assemble as a homohexamer (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
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 Repc, the Lon protease, and the stationary phase-specific
CC       sigma factor RpoS are all influencing viral repression in response to
CC       either temperature or stationary growth phase. Decreased availability
CC       of host SsrA in growing cells would favor latency, whereas starvation
CC       would favor Repc degradation and hence induction.
CC   -!- DOMAIN: The winged HTH N-terminal domain cooperatively binds to the
CC       enhancer/operator region of the Pe promoter. The C-terminal domain
CC       (CTD) regulates DNA binding by the N-terminal domain and degradation by
CC       ClpX-ClpP protease.
CC   -!- SIMILARITY: Belongs to the mulikevirus repressor c protein family.
CC       {ECO:0000305}.
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DR   EMBL; X03847; CAA27474.1; -; Genomic_DNA.
DR   EMBL; GQ357916; ACV50260.1; -; Genomic_DNA.
DR   PIR; S07370; S07370.
DR   RefSeq; YP_003335749.1; NC_013594.1.
DR   SMR; P07040; -.
DR   GeneID; 8658869; -.
DR   KEGG; vg:8658869; -.
DR   Proteomes; UP000000320; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0098689; P:latency-replication decision; 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   2: Evidence at transcript level;
KW   DNA-binding; Early protein; Host cytoplasm; Host-virus interaction;
KW   Latency-replication decision; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..174
FT                   /note="Repressor c protein"
FT                   /id="PRO_0000077588"
FT   DOMAIN          6..73
FT                   /note="HTH Mu-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01039"
FT   REGION          170..174
FT                   /note="Recognition by host ClpX-ClpP"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        50
FT                   /note="Y -> N (in Ref. 2; ACV50260)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   174 AA;  19518 MW;  2DA5D6CCDCB4C585 CRC64;
     MMSFEIKEWF NAKELEGMPG VPKLATNITR KAVAEDWVKR QRHGGKGVAY EYHINSLPEE
     TRRAIKGASL SDKPVHTSIV HTVDERLIYA MSFLTPDEQA AAVEIIRVAG IKGLMPTIVS
     KDKALEALGI TVEQQKTLQT LQALPPEKVR EILSQYEGKE HNFPVRENDV KKAV