ID   KDGR_DICCH              Reviewed;         305 AA.
AC   P37728;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Pectin degradation repressor protein KdgR;
GN   Name=kdgR;
OS   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1840643; DOI=10.1111/j.1365-2958.1991.tb02150.x;
RA   Reverchon S., Nasser W., Robert-Baudouy J.;
RT   "Characterization of kdgR, a gene of Erwinia chrysanthemi that regulates
RT   pectin degradation.";
RL   Mol. Microbiol. 5:2203-2216(1991).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Reverchon S.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=1545709; DOI=10.1111/j.1365-2958.1992.tb02007.x;
RA   Nasser W., Reverchon S., Robert-Baudouy J.;
RT   "Purification and functional characterization of the KdgR protein, a major
RT   repressor of pectinolysis genes of Erwinia chrysanthemi.";
RL   Mol. Microbiol. 6:257-265(1992).
CC   -!- FUNCTION: Transcriptional repressor of genes involved in pectinolysis
CC       and in pectinase secretion. Controls all the genes involved in pectin
CC       catabolism, including the pel genes encoding pectate lyases, KdgT which
CC       encodes the 2-keto-3-deoxygluconate transport system and KdgK which
CC       encodes the kdg kinase.
CC   -!- SUBUNIT: Homodimer.
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DR   EMBL; X62072; CAA43986.1; -; Genomic_DNA.
DR   PIR; S17713; S17713.
DR   AlphaFoldDB; P37728; -.
DR   SMR; P37728; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00090; HTH_ARSR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   InterPro; IPR011991; ArsR-like_HTH.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR014757; Tscrpt_reg_IclR_C.
DR   InterPro; IPR005471; Tscrpt_reg_IclR_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF09339; HTH_IclR; 1.
DR   Pfam; PF01614; IclR; 1.
DR   SMART; SM00346; HTH_ICLR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS51077; HTH_ICLR; 1.
DR   PROSITE; PS51078; ICLR_ED; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..305
FT                   /note="Pectin degradation repressor protein KdgR"
FT                   /id="PRO_0000201761"
FT   DOMAIN          55..116
FT                   /note="HTH iclR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
FT   DOMAIN          131..300
FT                   /note="IclR-ED"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00394"
FT   DNA_BIND        76..95
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00393"
SQ   SEQUENCE   305 AA;  34960 MW;  A3C2E27E7A36C5A3 CRC64;
     MIFNRSVTYS NARLPYSKRS LYTKTRVLFF LKQKILSRVT TKMAIADLDK QPDSVSSVLK
     VFGILQALGE EREIGITELS QRVMMSKSTV YRFLQTMKSL GYVAQEGESE KYSLTLKLFE
     LGAKALQNVD LIRSADIQMR ELSALTRETI HLGALDEDSI VYIHKIDSMY NLRMYSRIGR
     RNPLHSTAIG KVLLAWRDRE EVKEILSQVE FKRTTVHTIG STEELLPQLD LVRQQGYGED
     NEEQEEGLRC IAVPVFDRFG VVIAGLSISF PTIRFSEDNK HEYVAMLHTA ARNISDQMGY
     HDYPF