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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
 
 
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