ID D2TQ29_CITRI Unreviewed; 257 AA.
AC D2TQ29;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Galactitol utilisation operon repressor {ECO:0000313|EMBL:CBG91381.1};
GN Name=gatR {ECO:0000313|EMBL:CBG91381.1};
GN OrderedLocusNames=ROD_46881 {ECO:0000313|EMBL:CBG91381.1};
OS Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91381.1, ECO:0000313|Proteomes:UP000001889};
RN [1] {ECO:0000313|EMBL:CBG91381.1, ECO:0000313|Proteomes:UP000001889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC168 {ECO:0000313|EMBL:CBG91381.1,
RC ECO:0000313|Proteomes:UP000001889};
RX PubMed=19897651; DOI=10.1128/JB.01144-09;
RA Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT "The Citrobacter rodentium genome sequence reveals convergent evolution
RT with human pathogenic Escherichia coli.";
RL J. Bacteriol. 192:525-538(2010).
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DR EMBL; FN543502; CBG91381.1; -; Genomic_DNA.
DR RefSeq; WP_012908576.1; NC_013716.1.
DR AlphaFoldDB; D2TQ29; -.
DR STRING; 637910.ROD_46881; -.
DR KEGG; cro:ROD_46881; -.
DR eggNOG; COG1349; Bacteria.
DR HOGENOM; CLU_060699_0_1_6; -.
DR OMA; LATVDHW; -.
DR OrthoDB; 5685843at2; -.
DR Proteomes; UP000001889; Chromosome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1360; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR014036; DeoR_C.
DR InterPro; IPR001034; DeoR_HTH.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR018356; Tscrpt_reg_HTH_DeoR_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR30363:SF57; GLUCITOL OPERON REPRESSOR; 1.
DR PANTHER; PTHR30363; HTH-TYPE TRANSCRIPTIONAL REGULATOR SRLR-RELATED; 1.
DR Pfam; PF00455; DeoRC; 1.
DR Pfam; PF08220; HTH_DeoR; 1.
DR PRINTS; PR00037; HTHLACR.
DR SMART; SM01134; DeoRC; 1.
DR SMART; SM00420; HTH_DEOR; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS00894; HTH_DEOR_1; 1.
DR PROSITE; PS51000; HTH_DEOR_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 3..58
FT /note="HTH deoR-type"
FT /evidence="ECO:0000259|PROSITE:PS51000"
SQ SEQUENCE 257 AA; 27503 MW; 11E7B04FC66F1C7E CRC64;
MNSFERRNKI VDLINTQGSV LVLDLSNIFG ISEVTIRADL RLLEEKGLVT RFHGGAAKPG
SHLAEGDNQE VILEDRYQLA SDPKKRIAQA AAAMVNEGMT VILDSGSTTL LIAEALNRKS
NITVITNSLP AAFTLSDNKD LTLVVCGGTV RHKTHSMHGT IAERSLHGIS ADLMFVGADG
IDATNGITTF NEGYSISGVM AAAAHKVVAV LDATKFNRRG FNQVLSMDKI NCVITDDGIS
KQDKAALEKT GVELLIV
//