MCE2R_MYCTU
ID MCE2R_MYCTU Reviewed; 240 AA.
AC P9WMG5; L0T5T5; O07792; P67741;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=HTH-type transcriptional regulator Mce2R;
GN Name=mce2R; OrderedLocusNames=Rv0586; ORFNames=MTCY19H5.36c;
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 DNA-BINDING.
RX PubMed=18329386; DOI=10.1016/j.febslet.2008.02.074;
RA Vindal V., Ashwantha Kumar E., Ranjan A.;
RT "Identification of operator sites within the upstream region of the
RT putative mce2R gene from mycobacteria.";
RL FEBS Lett. 582:1117-1122(2008).
RN [4]
RP FUNCTION, DNA-BINDING, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19027363; DOI=10.1016/j.tube.2008.09.002;
RA Santangelo Mde L., Blanco F., Campos E., Soria M., Bianco M.V., Klepp L.,
RA Alito A., Zabal O., Cataldi A., Bigi F.;
RT "Mce2R from Mycobacterium tuberculosis represses the expression of the mce2
RT operon.";
RL Tuberculosis 89:22-28(2009).
RN [5]
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).
CC -!- FUNCTION: Negatively regulates the expression of its operon as well as
CC expression of end (endonuclease 4). {ECO:0000269|PubMed:19027363}.
CC -!- INDUCTION: Expressed in mid-log phase cells and in gamma-interferon
CC stimulated, mouse macrophage-like cell line J774.
CC {ECO:0000269|PubMed:19027363}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- MISCELLANEOUS: Part of an operon comprising at least mce2R and yrbE2A
CC and probably extending to at least mce2A.
CC {ECO:0000305|PubMed:19027363}.
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DR EMBL; AL123456; CCP43324.1; -; Genomic_DNA.
DR PIR; E70907; E70907.
DR RefSeq; NP_215100.1; NC_000962.3.
DR RefSeq; WP_003403065.1; NZ_NVQJ01000033.1.
DR AlphaFoldDB; P9WMG5; -.
DR SMR; P9WMG5; -.
DR STRING; 83332.Rv0586; -.
DR PaxDb; P9WMG5; -.
DR DNASU; 887754; -.
DR GeneID; 887754; -.
DR KEGG; mtu:Rv0586; -.
DR TubercuList; Rv0586; -.
DR eggNOG; COG2186; Bacteria.
DR OMA; FWDHIVD; -.
DR PhylomeDB; P9WMG5; -.
DR Proteomes; UP000001584; Chromosome.
DR CollecTF; EXPREG_00000c40; -.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MTBBASE.
DR GO; GO:0052572; P:response to host immune response; IDA:MTBBASE.
DR CDD; cd07377; WHTH_GntR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.20.120.530; -; 1.
DR InterPro; IPR011711; GntR_C.
DR InterPro; IPR008920; TF_FadR/GntR_C.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF07729; FCD; 1.
DR Pfam; PF00392; GntR; 1.
DR PRINTS; PR00035; HTHGNTR.
DR SMART; SM00895; FCD; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48008; SSF48008; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..240
FT /note="HTH-type transcriptional regulator Mce2R"
FT /id="PRO_0000050699"
FT DOMAIN 9..77
FT /note="HTH gntR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT DNA_BIND 37..56
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
SQ SEQUENCE 240 AA; 26509 MW; A0AA26FD6BFF8FB8 CRC64;
MALQPVTRRS VPEEVFEQIA TDVLTGEMPP GEALPSERRL AELLGVSRPA VREALKRLSA
AGLVEVRQGD VTTVRDFRRH AGLDLLPRLL FRNGELDISV VRSILEARLR NFPKVAELAA
ERNEPELAEL LQDSLRALDT EEDPIVWQRH TLDFWDHVVD SAGSIVDRLM YNAFRAAYEP
TLAALTTTMT AAAKRPSDYR KLADAICSGD PTGAKKAAQD LLELANTSLM AVLVSQASRQ
