ID RAMB_CORGL Reviewed; 474 AA.
AC Q8NTD8; Q6M7Z3;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=HTH-type transcriptional regulator RamB {ECO:0000303|PubMed:15090522};
DE AltName: Full=Regulator of acetate metabolism B {ECO:0000303|PubMed:15090522};
DE Short=RamB {ECO:0000303|PubMed:15090522};
GN Name=ramB {ECO:0000303|PubMed:15090522}; OrderedLocusNames=cg0444, Cgl0369;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nakagawa S.;
RT "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=15090522; DOI=10.1128/jb.186.9.2798-2809.2004;
RA Gerstmeir R., Cramer A., Dangel P., Schaffer S., Eikmanns B.J.;
RT "RamB, a novel transcriptional regulator of genes involved in acetate
RT metabolism of Corynebacterium glutamicum.";
RL J. Bacteriol. 186:2798-2809(2004).
RN [5]
RP FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=17114251; DOI=10.1128/jb.01061-06;
RA Cramer A., Auchter M., Frunzke J., Bott M., Eikmanns B.J.;
RT "RamB, the transcriptional regulator of acetate metabolism in
RT Corynebacterium glutamicum, is subject to regulation by RamA and RamB.";
RL J. Bacteriol. 189:1145-1149(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=18355281; DOI=10.1111/j.1574-6968.2008.01098.x;
RA Jungwirth B., Emer D., Brune I., Hansmeier N., Puehler A., Eikmanns B.J.,
RA Tauch A.;
RT "Triple transcriptional control of the resuscitation promoting factor 2
RT (rpf2) gene of Corynebacterium glutamicum by the regulators of acetate
RT metabolism RamA and RamB and the cAMP-dependent regulator GlxR.";
RL FEMS Microbiol. Lett. 281:190-197(2008).
CC -!- FUNCTION: During growth on glucose, RamB negatively controls the
CC expression of aceA, aceB, ack and pta genes which are involved in
CC acetate metabolism (PubMed:15090522, PubMed:17114251). RamB is also a
CC negative regulator of rpf2 gene expression during growth on acetate as
CC the sole carbon source (PubMed:18355281). {ECO:0000269|PubMed:15090522,
CC ECO:0000269|PubMed:17114251, ECO:0000269|PubMed:18355281}.
CC -!- INDUCTION: RamB represses its own expression. Additionally, ramB
CC expression is subject to carbon source-dependent positive control by
CC RamA. {ECO:0000269|PubMed:17114251}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show high-level specific
CC activities of acetate kinase (Ack), phosphotransacetylase (Pta),
CC isocitrate lyase (AceA) and malate synthase (AceB) irrespective of the
CC substrate (PubMed:15090522). The transcription level of the rpf2 gene
CC is increased 20-fold in the ramB deletion mutant during growth on
CC acetate as the sole carbon source (PubMed:18355281).
CC {ECO:0000269|PubMed:15090522, ECO:0000269|PubMed:18355281}.
CC -!- MISCELLANEOUS: C.glutamicum shows high-level specific activities of
CC acetate kinase (Ack), phosphotransacetylase (Pta), isocitrate lyase
CC (AceA) and malate synthase (AceB) when grown on acetate as sole carbon
CC and energy sources. It shows low-level specific activities with all
CC four enzymes when grown on glucose as sole carbon and energy sources.
CC {ECO:0000269|PubMed:15090522}.
CC -!- SIMILARITY: Belongs to the short-chain fatty acyl-CoA assimilation
CC regulator (ScfR) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000036; BAB97762.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19083.1; -; Genomic_DNA.
DR RefSeq; NP_599617.1; NC_003450.3.
DR RefSeq; WP_003859703.1; NC_006958.1.
DR AlphaFoldDB; Q8NTD8; -.
DR SMR; Q8NTD8; -.
DR STRING; 196627.cg0444; -.
DR KEGG; cgb:cg0444; -.
DR KEGG; cgl:Cgl0369; -.
DR PATRIC; fig|196627.13.peg.369; -.
DR eggNOG; COG1396; Bacteria.
DR eggNOG; COG3800; Bacteria.
DR HOGENOM; CLU_046383_0_0_11; -.
DR OrthoDB; 9810578at2; -.
DR BioCyc; CORYNE:G18NG-9926-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB.
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:SF23; HTH-TYPE TRANSCRIPTIONAL REGULATOR PRPR; 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 2: Evidence at transcript 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_0000433053"
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; 53866 MW; 29B6840EFD81BA9A CRC64;
MGKTYVGSRL RQLRRERDLS QASLAATLGL SASYVNQIEH DVRPLTVPVL LRITEAFGVD
ATFFSRDDDS RLLAEVQDVM LDREINPANV ELQELSEMVY NHPQLARAMV EMHQRYRNVR
DKFSIAVDNR TNTPEERRPI AEAVSMPHEE VRDFIYARQN YFDALDRRAE AIAAQLGWQP
YDSRAMEDSI ARRLQMDHDV TITSSKEESG TLHHFDPETR LLTIHARLNP GQRAFRMATE
LGYLEANDLI EGIVDDGIWS TPEARTLAIR GVASYFAAAV MLPYKIFHSE AEKSGYDIEY
LGQLFGVGYE TTAHRLSTLQ RPNLRGIPFT FVRVDRAGNM SKRQSATGFH FTHYGGTCPL
WNVFETFTNP GQVLRQFAQM PDGRNYLWIS RTVRHHEARF GEVDKMFAIG LGCEARHADR
TVYSRGFNLQ DLSTATPIGS GCRVCTRENC AQRAFPSVHG RINIDAHEST IAPY
//
