ID   RAMB_MYCTO              Reviewed;         474 AA.
AC   P9WMI0; L0T6J8; O53750; Q7D9R8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=HTH-type transcriptional regulator RamB {ECO:0000250|UniProtKB:P9WMI1};
GN   Name=ramB {ECO:0000250|UniProtKB:P9WMI1}; OrderedLocusNames=MT0481;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Involved in the control of the glyoxylate cycle. RamB
CC       negatively controls the expression of icl expression during growth on
CC       acetate as the sole carbon source. {ECO:0000250|UniProtKB:P9WMI1}.
CC   -!- INDUCTION: RamB represses its own expression (independently of the
CC       available carbon source) and is negatively regulated by PrpR.
CC       {ECO:0000250|UniProtKB:P9WMI1}.
CC   -!- SIMILARITY: Belongs to the short-chain fatty acyl-CoA assimilation
CC       regulator (ScfR) family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44705.1; -; Genomic_DNA.
DR   PIR; E70828; E70828.
DR   RefSeq; WP_003898467.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMI0; -.
DR   SMR; P9WMI0; -.
DR   EnsemblBacteria; AAK44705; AAK44705; MT0481.
DR   KEGG; mtc:MT0481; -.
DR   PATRIC; fig|83331.31.peg.511; -.
DR   HOGENOM; CLU_046383_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 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   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; SSF47413; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Lipid metabolism; Repressor; Steroid metabolism;
KW   Sterol metabolism; Transcription; Transcription regulation.
FT   CHAIN           1..474
FT                   /note="HTH-type transcriptional regulator RamB"
FT                   /id="PRO_0000427300"
FT   DOMAIN          10..64
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DNA_BIND        21..40
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
SQ   SEQUENCE   474 AA;  53072 MW;  F715A9362A860644 CRC64;
     MSKTYVGSRV RQLRNERGFS QAALAQMLEI SPSYLNQIEH DVRPLTVAVL LRITEVFGVD
     ATFFASQDDT RLVAELREVT LDRDLDIAID PHEVAEMVSA HPGLACAVVN LHRRYRITTA
     QLAAATEERF SDGSGRGSIT MPHEEVRDYF YQRQNYLHAL DTAAEDLTAQ MRMHHGDLAR
     ELTRRLTEVH GVRINKRIDL GDTVLHRYDP ATNTLEISSH LSPGQQVFKM AAELAYLEFG
     DLIDAMVTDG KFTSAESRTL ARLGLANYFA AATVLPYRQF HDVAENFRYD VERLSAFYSV
     SYETIAHRLS TLQRPSMRGV PFTFVRVDRA GNMSKRQSAT GFHFSSSGGT CPLWNVYETF
     ANPGKILVQI AQMPDGRNYL WVARTVELRA ARYGQPGKTF AIGLGCELRH AHRLVYSEGL
     DLSGDPNTAA TPIGAGCRVC ERDNCPQRAF PALGRALDLD EHRSTVSPYL VKQL