ID   CYANR_KRIFD             Reviewed;         402 AA.
AC   D2PPN2;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Cyclobis-(1-6)-alpha-nigerosyl repressor {ECO:0000305|PubMed:27302067};
GN   OrderedLocusNames=Kfla_1900 {ECO:0000312|EMBL:ADB30994.1};
OS   Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC   Bacteria; Actinobacteria; Propionibacteriales; Kribbellaceae; Kribbella.
OX   NCBI_TaxID=479435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000312|Proteomes:UP000007967};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kribbella flavida DSM 17836.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399;
RX   PubMed=27302067; DOI=10.1074/jbc.m116.727305;
RA   Tagami T., Miyano E., Sadahiro J., Okuyama M., Iwasaki T., Kimura A.;
RT   "Two novel glycoside hydrolases responsible for the catabolism of cyclobis-
RT   (1->6)-alpha-nigerosyl.";
RL   J. Biol. Chem. 291:16438-16447(2016).
CC   -!- FUNCTION: Transcriptional repressor of cyclobis-(1-6)-alpha-nigerosyl
CC       (CNN) degrading enzymes. {ECO:0000305|PubMed:27302067}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR   EMBL; CP001736; ADB30994.1; -; Genomic_DNA.
DR   RefSeq; WP_012919550.1; NC_013729.1.
DR   AlphaFoldDB; D2PPN2; -.
DR   SMR; D2PPN2; -.
DR   STRING; 479435.Kfla_1900; -.
DR   EnsemblBacteria; ADB30994; ADB30994; Kfla_1900.
DR   KEGG; kfl:Kfla_1900; -.
DR   eggNOG; COG1846; Bacteria.
DR   eggNOG; COG1940; Bacteria.
DR   HOGENOM; CLU_036604_13_4_11; -.
DR   OMA; INIEHIF; -.
DR   OrthoDB; 1130699at2; -.
DR   Proteomes; UP000007967; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR18964; PTHR18964; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; DNA-binding; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..402
FT                   /note="Cyclobis-(1-6)-alpha-nigerosyl repressor"
FT                   /id="PRO_0000443933"
FT   DNA_BIND        30..49
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  41094 MW;  3C293950066C30E7 CRC64;
     MAHSPGPIPR GDLVPSGIVG LLGTQGPTAR TAIARTLGLS PATVTQVTKD LIARGLIEEL
     ESVPSNGGRP ARLLGLVQDA GVALGAKVTA DHVAIVTVEL DGTVRSSVSH DYDPGADDAL
     PRLGRILAQE VAALDDRLLG VGVGVPGSVD SQASGIVDAP TLSWQAAPVG PSLRAAIGSP
     VLVDNDVNTL AAAERLYGIG RAHSSYLVVT IGRGIGCGIV VDGGIYRGAN GGAGEIGHIP
     VWHDEQDQLP CTCGSTGCLE AHVGAAGLCR TARDRGVIGP RGTLPTLLRA AATGDEAARQ
     VFAAAGAMLG RALAGVIHTI DPEVVVLMGE GVDGWQYWQT GFEPSFRRSL LPARKAVPVV
     VEPWTEDQWA RGAASLVLAS PFDSAGTGGE QSRLVRVRLG AP