RAMB_MYCTU
ID RAMB_MYCTU Reviewed; 474 AA.
AC P9WMI1; 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 42.
DE RecName: Full=HTH-type transcriptional regulator RamB {ECO:0000303|PubMed:19767422};
DE AltName: Full=icl1 and ramB operon repressor protein {ECO:0000305};
GN Name=ramB {ECO:0000303|PubMed:19767422}; OrderedLocusNames=Rv0465c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP FUNCTION, DNA-BINDING, INDUCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19767422; DOI=10.1128/jb.01009-09;
RA Micklinghoff J.C., Breitinger K.J., Schmidt M., Geffers R., Eikmanns B.J.,
RA Bange F.C.;
RT "Role of the transcriptional regulator RamB (Rv0465c) in the control of the
RT glyoxylate cycle in Mycobacterium tuberculosis.";
RL J. Bacteriol. 191:7260-7269(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22916289; DOI=10.1371/journal.pone.0043651;
RA Masiewicz P., Brzostek A., Wolanski M., Dziadek J.,
RA Zakrzewska-Czerwinska J.;
RT "A novel role of the PrpR as a transcription factor involved in the
RT regulation of methylcitrate pathway in Mycobacterium tuberculosis.";
RL PLoS ONE 7:E43651-E43651(2012).
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. Does not regulate the expression of
CC other genes involved in acetate metabolism.
CC {ECO:0000269|PubMed:19767422}.
CC -!- INDUCTION: RamB represses its own expression (independently of the
CC available carbon source) and is negatively regulated by PrpR.
CC {ECO:0000269|PubMed:19767422, ECO:0000269|PubMed:22916289}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an expression level
CC of icl higher than wild-type during incubation with glucose while
CC remaining approximately at the same level than wild-type during
CC incubation with acetate. ramB expression levels are found to be higher
CC in the deletion mutant than in the wild-type during incubation with
CC acetate or glucose. {ECO:0000269|PubMed:19767422}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the short-chain fatty acyl-CoA assimilation
CC regulator (ScfR) family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43198.1; -; Genomic_DNA.
DR PIR; E70828; E70828.
DR RefSeq; NP_214979.1; NC_000962.3.
DR RefSeq; WP_003898467.1; NZ_NVQJ01000002.1.
DR AlphaFoldDB; P9WMI1; -.
DR SMR; P9WMI1; -.
DR STRING; 83332.Rv0465c; -.
DR PaxDb; P9WMI1; -.
DR DNASU; 886320; -.
DR GeneID; 886320; -.
DR KEGG; mtu:Rv0465c; -.
DR TubercuList; Rv0465c; -.
DR eggNOG; COG1396; Bacteria.
DR eggNOG; COG3800; Bacteria.
DR OMA; QRAFPPI; -.
DR PhylomeDB; P9WMI1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:MTBBASE.
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 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..474
FT /note="HTH-type transcriptional regulator RamB"
FT /id="PRO_0000382634"
FT DOMAIN 10..64
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257,
FT ECO:0000269|PubMed:19767422"
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