RARC_BPP22
ID RARC_BPP22 Reviewed; 53 AA.
AC P03050; Q77D84; Q7PCJ3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 124.
DE RecName: Full=Transcriptional repressor arc;
GN Name=arc;
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 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=8107872; DOI=10.1038/367754a0;
RA Raumann B.E., Rould M.A., Pabo C.O., Sauer R.T.;
RT "DNA recognition by beta-sheets in the Arc repressor-operator crystal
RT structure.";
RL Nature 367:754-757(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT LEU-8.
RX PubMed=7827088; DOI=10.1021/bi00004a035;
RA Schildbach J.F., Milla M.E., Jeffrey P.D., Raumann B.E., Sauer R.T.;
RT "Crystal structure, folding, and operator binding of the hyperstable Arc
RT repressor mutant PL8.";
RL Biochemistry 34:1405-1412(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=9927650; DOI=10.1073/pnas.96.3.811;
RA Schildbach J.F., Karzai A.W., Raumann B.E., Sauer R.T.;
RT "Origins of DNA-binding specificity: role of protein contacts with the DNA
RT backbone.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:811-817(1999).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=2611267; DOI=10.1021/bi00451a041;
RA Zagorski M.G., Bowie J.U., Vershon A.K., Sauer R.T., Patel D.J.;
RT "NMR studies of Arc repressor mutants: proton assignments, secondary
RT structure, and long-range contacts for the thermostable proline-8-->
RT leucine variant of Arc.";
RL Biochemistry 28:9813-9825(1989).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=2611268; DOI=10.1021/bi00451a042;
RA Breg J.N., Boelens R., George A.V.E., Kaptein R.;
RT "Sequence-specific 1H NMR assignment and secondary structure of the Arc
RT repressor of bacteriophage P22, as determined by two-dimensional 1H NMR
RT spectroscopy.";
RL Biochemistry 28:9826-9833(1989).
RN [9]
RP STRUCTURE BY NMR.
RX PubMed=2377232; DOI=10.1038/346586a0;
RA Breg J.N., Vsn Opheusden J.H.J., Burgering M.J.M., Boelens R., Kaptein R.;
RT "Structure of Arc repressor in solution: evidence for a family of beta-
RT sheet DNA-binding proteins.";
RL Nature 346:586-589(1990).
CC -!- FUNCTION: This protein acts as a transcriptional repressor of its own
CC gene arc and of gene ant.
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; CAA25990.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75058.1; -; Genomic_DNA.
DR EMBL; AF527608; AAM81381.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA00979.1; -; Genomic_DNA.
DR PIR; A03586; RGBPA2.
DR RefSeq; NP_059642.1; NC_002371.2.
DR PDB; 1ARQ; NMR; -; A/B=1-53.
DR PDB; 1ARR; NMR; -; A/B=1-53.
DR PDB; 1B28; NMR; -; A/B=1-53.
DR PDB; 1BAZ; X-ray; 1.90 A; A/B/C/D=1-53.
DR PDB; 1BDT; X-ray; 2.50 A; A/B/C/D=1-53.
DR PDB; 1BDV; X-ray; 2.80 A; A/B/C/D=1-53.
DR PDB; 1MYK; X-ray; 2.40 A; A/B=1-53.
DR PDB; 1MYL; X-ray; 2.40 A; A/B/C/D/E/F=1-53.
DR PDB; 1NLA; NMR; -; A/B=1-53.
DR PDB; 1PAR; X-ray; 2.60 A; A/B/C/D=1-53.
DR PDB; 1QTG; NMR; -; A/B=1-53.
DR PDB; 1U9P; X-ray; 1.90 A; A=1-52.
DR PDBsum; 1ARQ; -.
DR PDBsum; 1ARR; -.
DR PDBsum; 1B28; -.
DR PDBsum; 1BAZ; -.
DR PDBsum; 1BDT; -.
DR PDBsum; 1BDV; -.
DR PDBsum; 1MYK; -.
DR PDBsum; 1MYL; -.
DR PDBsum; 1NLA; -.
DR PDBsum; 1PAR; -.
DR PDBsum; 1QTG; -.
DR PDBsum; 1U9P; -.
DR BMRB; P03050; -.
DR SMR; P03050; -.
DR GeneID; 1262795; -.
DR KEGG; vg:1262795; -.
DR EvolutionaryTrace; P03050; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000001796; 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 DisProt; DP01512; -.
DR Gene3D; 1.10.1220.10; -; 1.
DR InterPro; IPR005569; Arc_DNA-bd_dom.
DR InterPro; IPR013321; Arc_rbn_hlx_hlx.
DR InterPro; IPR010985; Ribbon_hlx_hlx.
DR Pfam; PF03869; Arc; 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 CHAIN 1..53
FT /note="Transcriptional repressor arc"
FT /id="PRO_0000077735"
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:1BDT"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1BAZ"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:1BAZ"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:1BAZ"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1ARQ"
SQ SEQUENCE 53 AA; 6227 MW; 06ADFA7BD31B26EB CRC64;
MKGMSKMPQF NLRWPREVLD LVRKVAEENG RSVNSEIYQR VMESFKKEGR IGA
