RPC1_BP434
ID RPC1_BP434 Reviewed; 95 AA.
AC P16117;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 120.
DE RecName: Full=Repressor protein CI;
DE Flags: Fragment;
GN Name=CI;
OS Enterobacteria phage 434 (Bacteriophage 434).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10712;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3031621; DOI=10.1093/nar/15.7.3181;
RA Kuziel W.A., Tucker P.W.;
RT "Determination of vector: insert junctions in lambda gt10 cDNAs that do not
RT recut with EcoRI. Nucleotide sequence of the lambda imm434 HindIII-EcoRI
RT DNA fragment encoding part of the cI protein.";
RL Nucleic Acids Res. 15:3181-3181(1987).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-67.
RX PubMed=2926803; DOI=10.1016/0022-2836(89)90375-6;
RA Mondragon A., Subbiah S., Almo S.C., Drottar M., Harrison S.C.;
RT "Structure of the amino-terminal domain of phage 434 repressor at 2.0-A
RT resolution.";
RL J. Mol. Biol. 205:189-200(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-67.
RX PubMed=3187531; DOI=10.1126/science.3187531;
RA Aggarwal A.K., Rodgers D.W., Drottar M., Ptashne M., Harrison S.C.;
RT "Recognition of a DNA operator by the repressor of phage 434: a view at
RT high resolution.";
RL Science 242:899-907(1988).
RN [4]
RP STRUCTURE BY NMR OF 1-67.
RX PubMed=1311771; DOI=10.1016/0022-2836(92)90987-u;
RA Neri D., Billeter M., Wuethrich K.;
RT "Determination of the nuclear magnetic resonance solution structure of the
RT DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison
RT with the X-ray crystal structure.";
RL J. Mol. Biol. 223:743-767(1992).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=9000626; DOI=10.1006/jmbi.1996.0692;
RA Pervushin K., Billeter M., Siegal G., Wuethrich K.;
RT "Structural role of a buried salt bridge in the 434 repressor DNA-binding
RT domain.";
RL J. Mol. Biol. 264:1002-1012(1996).
CC -!- FUNCTION: Binds to two sets of three contiguous operator sites in the
CC phage genome.
CC -!- SUBUNIT: Homodimer, when bound to an operator.
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DR EMBL; Y00118; CAA68301.1; -; Genomic_DNA.
DR PDB; 1PER; X-ray; 2.50 A; L/R=2-70.
DR PDB; 1PRA; NMR; -; A=2-70.
DR PDB; 1R63; NMR; -; A=2-64.
DR PDB; 1R69; X-ray; 2.00 A; A=2-70.
DR PDB; 1RPE; X-ray; 2.50 A; L/R=2-70.
DR PDB; 1SQ8; NMR; -; A=11-63.
DR PDB; 2OR1; X-ray; 2.50 A; L/R=2-70.
DR PDB; 2R63; NMR; -; A=2-64.
DR PDBsum; 1PER; -.
DR PDBsum; 1PRA; -.
DR PDBsum; 1R63; -.
DR PDBsum; 1R69; -.
DR PDBsum; 1RPE; -.
DR PDBsum; 1SQ8; -.
DR PDBsum; 2OR1; -.
DR PDBsum; 2R63; -.
DR BMRB; P16117; -.
DR SMR; P16117; -.
DR EvolutionaryTrace; P16117; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR Pfam; PF01381; HTH_3; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..>95
FT /note="Repressor protein CI"
FT /id="PRO_0000149714"
FT DOMAIN 7..60
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 18..37
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT NON_TER 95
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1R69"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:1R69"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1R69"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:2OR1"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:1R69"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1R69"
SQ SEQUENCE 95 AA; 10426 MW; 6229D2DD66EA7EFC CRC64;
MSISSRVKSK RIQLGLNQAE LAQKVGTTQQ SIEQLENGKT KRPRFLPELA SALGVSVDWL
LNGTSDSNVR FVGHVEPKGK YPLISMVRAG SWCEA