ID CMR_MYCTU Reviewed; 244 AA.
AC P9WMH5; F2GK61; L0T8Y5; O53922; Q7D864;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=HTH-type transcriptional regulator Cmr;
GN Name=cmr; OrderedLocusNames=Rv1675c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
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 [3]
RP FUNCTION IN TRANSCRIPTION, AND DNA-BINDING.
RX PubMed=22464736; DOI=10.1016/j.tube.2012.03.001;
RA Stapleton M.R., Smith L.J., Hunt D.M., Buxton R.S., Green J.;
RT "Mycobacterium tuberculosis WhiB1 represses transcription of the essential
RT chaperonin GroEL2.";
RL Tuberculosis 92:328-332(2012).
CC -!- FUNCTION: Positively regulates the expression of at least groEL2.
CC Cyclic AMP does not affect transcription in vitro.
CC {ECO:0000269|PubMed:22464736}.
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DR EMBL; AL123456; CCP44440.1; -; Genomic_DNA.
DR PIR; F70818; F70818.
DR RefSeq; NP_216191.1; NC_000962.3.
DR RefSeq; WP_003898967.1; NZ_NVQJ01000010.1.
DR PDB; 5W5A; X-ray; 1.85 A; A/B=2-244.
DR PDB; 5W5B; X-ray; 1.80 A; A=13-244.
DR PDBsum; 5W5A; -.
DR PDBsum; 5W5B; -.
DR AlphaFoldDB; P9WMH5; -.
DR SMR; P9WMH5; -.
DR STRING; 83332.Rv1675c; -.
DR PaxDb; 83332-Rv1675c; -.
DR DNASU; 885693; -.
DR GeneID; 885693; -.
DR KEGG; mtu:Rv1675c; -.
DR TubercuList; Rv1675c; -.
DR eggNOG; COG0664; Bacteria.
DR InParanoid; P9WMH5; -.
DR OrthoDB; 272447at2; -.
DR PhylomeDB; P9WMH5; -.
DR PHI-base; PHI:7359; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MTBBASE.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR24567:SF79; CAMP-ACTIVATED GLOBAL TRANSCRIPTIONAL REGULATOR CRP; 1.
DR PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF13545; HTH_Crp_2; 1.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..244
FT /note="HTH-type transcriptional regulator Cmr"
FT /id="PRO_0000420401"
FT DOMAIN 174..237
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 197..216
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT BINDING 41..160
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:5W5B"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 110..115
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 120..135
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 147..171
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 208..220
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:5W5B"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:5W5B"
FT HELIX 236..242
FT /evidence="ECO:0007829|PDB:5W5B"
SQ SEQUENCE 244 AA; 26793 MW; D1B3CD2894CD5B69 CRC64;
MADRSVRPLR HLVHAVTGGQ PPSEAQVRQA AWIARCVGRG GSAPLHRDDV SALAETLQVK
EFAPGAVVFH ADQTADGVWI VRHGLIELAV GSRRRRAVVN ILHPGDVDGD IPLLLEMPMV
YTGRALTQAT CLFLDRQAFE RLLATHPAIA RRWLSSVAQR VSTAQIRLMG MLGRPLPAQV
AQLLLDEAID ARIELAQRTL AAMLGAQRPS INKILKEFER DRLITVGYAV IEITDQHGLR
ARAQ
//
