ID CYNR_ECOLI Reviewed; 299 AA. AC P27111; Q2MC86; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 5. DT 02-SEP-2026, entry version 173. DE RecName: Full=HTH-type transcriptional regulator CynR; DE AltName: Full=Cyn operon transcriptional activator; GN Name=cynR; OrderedLocusNames=b0338, JW5894; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS TRANSCRIPTIONAL REGULATOR, RP AND INDUCTION. RC STRAIN=K12; RX PubMed=1592818; DOI=10.1128/jb.174.11.3645-3650.1992; RA Sung Y.-C., Fuchs J.A.; RT "The Escherichia coli K-12 cyn operon is positively regulated by a member RT of the lysR family."; RL J. Bacteriol. 174:3645-3650(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP IDENTIFICATION OF START CODON, AND DNA-BINDING. RX PubMed=8253686; DOI=10.1128/jb.175.24.7990-7999.1993; RA Lamblin A.-F.J., Fuchs J.A.; RT "Expression and purification of the cynR regulatory gene product: CynR is a RT DNA-binding protein."; RL J. Bacteriol. 175:7990-7999(1993). CC -!- FUNCTION: Positively regulates the cynTSX operon, and negatively CC regulates its own transcription. Binds specifically to the cynR-cynTSX CC intergenic region. {ECO:0000269|PubMed:1592818}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:1592818}. CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB18062.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M93053; AAA23628.1; -; Genomic_DNA. DR EMBL; U73857; AAB18062.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC73441.3; -; Genomic_DNA. DR EMBL; AP009048; BAE76120.1; -; Genomic_DNA. DR PIR; A41900; A41900. DR RefSeq; NP_414872.3; NC_000913.3. DR RefSeq; WP_000952503.1; NZ_CP009789.1. DR PDB; 2HXR; X-ray; 2.05 A; A/B=63-299. DR PDB; 3HFU; X-ray; 2.60 A; A/B/C/D=63-299. DR AlphaFoldDB; P27111; -. DR SMR; P27111; -. DR BioGRID; 4259814; 127. DR DIP; DIP-9364N; -. DR FunCoup; P27111; 108. DR STRING; 511145.b0338; -. DR PaxDb; 511145-b0338; -. DR EnsemblBacteria; AAC73441; AAC73441; b0338. DR GeneID; 945001; -. DR KEGG; ecj:JW5894; -. DR KEGG; eco:b0338; -. DR KEGG; ecoc:C3026_01655; -. DR KEGG; ecoc:C3026_24825; -. DR PATRIC; fig|511145.12.peg.346; -. DR EchoBASE; EB1391; -. DR eggNOG; COG0583; Bacteria. DR HOGENOM; CLU_039613_6_0_6; -. DR InParanoid; P27111; -. DR OMA; ECGSLDW; -. DR OrthoDB; 646694at2; -. DR PhylomeDB; P27111; -. DR BioCyc; EcoCyc:PD00291; -. DR EvolutionaryTrace; P27111; -. DR PRO; PR:P27111; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P27111; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR CDD; cd08425; PBP2_CynR; 1. DR FunFam; 1.10.10.10:FF:000001; LysR family transcriptional regulator; 1. DR Gene3D; 3.40.190.290; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR037403; CynR_PBP2. DR InterPro; IPR050950; HTH-type_LysR_regulators. DR InterPro; IPR000847; LysR_HTH_N. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR NCBIfam; NF008416; PRK11242.1; 1. DR PANTHER; PTHR30419; HTH-TYPE TRANSCRIPTIONAL REGULATOR YBHD; 1. DR PANTHER; PTHR30419:SF8; NITROGEN ASSIMILATION TRANSCRIPTIONAL ACTIVATOR-RELATED; 1. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50931; HTH_LYSR; 1. DR PDBsum; 2HXR; -. DR PDBsum; 3HFU; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; Cytoplasm; DNA-binding; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1..299 FT /note="HTH-type transcriptional regulator CynR" FT /id="PRO_0000105612" FT DOMAIN 1..58 FT /note="HTH lysR-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253" FT DNA_BIND 18..37 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 99..102 FT /evidence="ECO:0007829|PDB:2HXR" FT TURN 103..105 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 106..116 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 122..126 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 129..137 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 142..149 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 155..170 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 174..177 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 179..181 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 183..188 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 199..210 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 216..222 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 224..233 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 243..247 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 251..258 FT /evidence="ECO:0007829|PDB:2HXR" FT STRAND 262..270 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:2HXR" FT HELIX 277..290 FT /evidence="ECO:0007829|PDB:2HXR" SQ SEQUENCE 299 AA; 32961 MW; 5649F6FF2437624A CRC64; MLSRHINYFL AVAEHGSFTR AASALHVSQP ALSQQIRQLE ESLGVPLFDR SGRTIRLTDA GEVWRQYASR ALQELGAGKR AIHDVADLTR GSLRIAVTPT FTSYFIGPLM ADFYARYPSI TLQLQEMSQE KIEDMLCRDE LDVGIAFAPV HSPELEAIPL LTESLALVVA QHHPLAVHEQ VALSRLHDEK LVLLSAEFAT REQIDHYCEK AGLHPQVVIE ANSISAVLEL IRRTSLSTLL PAAIATQHDG LKAISLAPPL LERTAVLLRR KNSWQTAAAK AFLHMALDKC AVVGGNESR //