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CYTR_ECOL6
ID   CYTR_ECOL6              Reviewed;         341 AA.
AC   P0ACN8; P06964;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=HTH-type transcriptional repressor CytR;
GN   Name=cytR; OrderedLocusNames=c4887;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: This protein negatively controls the transcription initiation
CC       of genes such as deoCABD, udp, and cdd encoding catabolizing enzymes
CC       and nupC, nupG, and tsx encoding transporting and pore-forming
CC       proteins. Binds cytidine and adenosine as effectors (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; AE014075; AAN83315.1; -; Genomic_DNA.
DR   RefSeq; WP_000644904.1; NC_004431.1.
DR   AlphaFoldDB; P0ACN8; -.
DR   BMRB; P0ACN8; -.
DR   SMR; P0ACN8; -.
DR   STRING; 199310.c4887; -.
DR   EnsemblBacteria; AAN83315; AAN83315; c4887.
DR   GeneID; 66672158; -.
DR   KEGG; ecc:c4887; -.
DR   eggNOG; COG1609; Bacteria.
DR   HOGENOM; CLU_037628_6_0_6; -.
DR   OMA; HSEFVFM; -.
DR   BioCyc; ECOL199310:C4887-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd01392; HTH_LacI; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR000843; HTH_LacI.
DR   InterPro; IPR046335; LacI/GalR-like_sensor.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   Pfam; PF00356; LacI; 1.
DR   Pfam; PF13377; Peripla_BP_3; 1.
DR   SMART; SM00354; HTH_LACI; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS00356; HTH_LACI_1; 1.
DR   PROSITE; PS50932; HTH_LACI_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..341
FT                   /note="HTH-type transcriptional repressor CytR"
FT                   /id="PRO_0000107940"
FT   DOMAIN          10..64
FT                   /note="HTH lacI-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT   DNA_BIND        12..31
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
SQ   SEQUENCE   341 AA;  37820 MW;  0C29D8829AE7062C CRC64;
     MKAKKQETAA TMKDVALKAK VSTATVSRAL MNPDKVSQAT RNRVEKAARE VGYLPQPMGR
     NVKRNESRTI LVIVPDICDP FFSEIIRGIE VTAANHGYLV LIGDCAHQNQ QEKTFIDLII
     TKQIDGMLLL GSRLPFDASI EEQRNLPPMV MANEFAPELE LPTVHIDNLT AAFDAVNYLY
     EQGHKRIGCI AGPEEMPLCH YRLQGYVQAL RRCGIMVDPQ YIARGDFTFE AGSKAMQQLL
     DLPQPPTAVF CHSDVMALGA LSQAKRQGLK VPEDLSIIGF DNIDLTQFCD PPLTTIAQPR
     YEIGREAMLL LLDQMQGQHV GSGSRLMDCE LIIRGSTRAL P
 
 
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