ID C4LLG3_CORK4 Unreviewed; 498 AA.
AC C4LLG3;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Transcriptional regulator, HTH_3 family {ECO:0000313|EMBL:ACR18668.1};
GN Name=ramB {ECO:0000313|EMBL:ACR18668.1};
GN OrderedLocusNames=ckrop_1959 {ECO:0000313|EMBL:ACR18668.1};
OS Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS CCUG 35717).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR18668.1, ECO:0000313|Proteomes:UP000001473};
RN [1] {ECO:0000313|EMBL:ACR18668.1, ECO:0000313|Proteomes:UP000001473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC {ECO:0000313|Proteomes:UP000001473};
RX PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT revealed insights into the physiology of a lipophilic corynebacterium that
RT lacks mycolic acids.";
RL J. Biotechnol. 136:22-30(2008).
CC -!- SIMILARITY: Belongs to the short-chain fatty acyl-CoA assimilation
CC regulator (ScfR) family. {ECO:0000256|ARBA:ARBA00007227}.
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DR EMBL; CP001620; ACR18668.1; -; Genomic_DNA.
DR RefSeq; WP_012732555.1; NC_012704.1.
DR AlphaFoldDB; C4LLG3; -.
DR STRING; 645127.ckrop_1959; -.
DR GeneID; 78092140; -.
DR KEGG; ckp:ckrop_1959; -.
DR eggNOG; COG1396; Bacteria.
DR eggNOG; COG3800; Bacteria.
DR HOGENOM; CLU_046383_0_0_11; -.
DR OMA; FHFVDNY; -.
DR OrthoDB; 9810578at2; -.
DR Proteomes; UP000001473; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR026281; HTH_RamB.
DR InterPro; IPR010359; IrrE_HExxH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR018653; ScfR_C.
DR NCBIfam; NF038139; Reg_Aceta_RamB; 1.
DR PANTHER; PTHR46797; HTH-TYPE TRANSCRIPTIONAL REGULATOR; 1.
DR PANTHER; PTHR46797:SF1; METHYLPHOSPHONATE SYNTHASE; 1.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF06114; Peptidase_M78; 1.
DR Pfam; PF09856; ScfRs; 1.
DR PIRSF; PIRSF019251; Rv0465c; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000001473};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 20..74
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
SQ SEQUENCE 498 AA; 55709 MW; BA9950DCCD23DA9C CRC64;
MTTGAEKEGP SSRVFVGTRL KQLRKERELS QATLAHALGL SASYVNQIEN DSRPLTSSVL
RKITHVFGID EAFFSREDDS RLVAEVHDVT LDREVCPTSI DVQEVADLVH THPELARALV
DIHRRYRNVS DKLSLVTEER NRSDVEDSST GSDALTMPHE EVRDFFYARQ NYIDSLDVAA
EELAGTLGLG VPNINHVEDC VATRLTSKYG VEVRYISHLD SGGNEHPDTA EHMVQHRFFP
DTGVLTIDAH LTSGQKAFRM ATELAYLEVG DQLHSLVDED PRFTSDESRQ LAVRGAATYY
AAALVLPYTN FHAQAERAGY DIEYLSTAYG MGYETICHRL STLQRPKLRG IPWTFVRVDR
AGNVSKRQSA TGFHFTHSGG TCPLWNVYET FSYPGKVMRQ LAQMPDGRTY MWVARTVKHY
RRRFGQPGKV FAIGLGCEAR HAERTVYAEG LDLSDLAAAT PIGPGCRVCS RTECPQRAFP
SILHDIRINT HSSSVNPY
//