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Database: UniProt
Entry: C4LLG3_CORK4
LinkDB: C4LLG3_CORK4
Original site: C4LLG3_CORK4 
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
//
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