CYNR_ECOLI
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 25-MAY-2022, entry version 158.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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_SSZK01000061.1.
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 PDBsum; 2HXR; -.
DR PDBsum; 3HFU; -.
DR AlphaFoldDB; P27111; -.
DR SMR; P27111; -.
DR BioGRID; 4259814; 4.
DR DIP; DIP-9364N; -.
DR STRING; 511145.b0338; -.
DR PaxDb; P27111; -.
DR PRIDE; P27111; -.
DR EnsemblBacteria; AAC73441; AAC73441; b0338.
DR EnsemblBacteria; BAE76120; BAE76120; BAE76120.
DR GeneID; 945001; -.
DR KEGG; ecj:JW5894; -.
DR KEGG; eco:b0338; -.
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; EQCIAGV; -.
DR PhylomeDB; P27111; -.
DR BioCyc; EcoCyc:PD00291; -.
DR EvolutionaryTrace; P27111; -.
DR PRO; PR:P27111; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd08425; PBP2_CynR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR037403; CynR_PBP2.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
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 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
