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 27-MAR-2024, entry version 63.
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; Actinomycetota; Actinomycetes; Propionibacteriales;
OC 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 KEGG; kfl:Kfla_1900; -.
DR eggNOG; COG1846; Bacteria.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_13_4_11; -.
DR OrthoDB; 3464494at2; -.
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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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:SF149; BIFUNCTIONAL UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE_N-ACETYLMANNOSAMINE KINASE; 1.
DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//
