CDDTR_MYCTU
ID CDDTR_MYCTU Reviewed; 107 AA.
AC I6X7F9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Transcriptional regulator Rv3488 {ECO:0000303|PubMed:30266832};
GN OrderedLocusNames=Rv3488 {ECO:0000312|EMBL:CCP46310.1};
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3] {ECO:0007744|PDB:5ZHC, ECO:0007744|PDB:5ZHV, ECO:0007744|PDB:5ZI8}
RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH
RP CADMIUM AND ZINC, FUNCTION, DNA-BINDING, SUBUNIT, DOMAIN, AND MUTAGENESIS
RP OF HIS-16 AND HIS-34.
RX PubMed=30266832; DOI=10.1042/bcj20180356;
RA Kumari M., Pal R.K., Mishra A.K., Tripathi S., Biswal B.K.,
RA Srivastava K.K., Arora A.;
RT "Structural and functional characterization of the transcriptional
RT regulator Rv3488 of Mycobacterium tuberculosis H37Rv.";
RL Biochem. J. 475:3393-3416(2018).
CC -!- FUNCTION: May have transcription regulation and metal-detoxifying
CC functions through which it may enhance intracellular survival of
CC mycobacteria. Binds to its own promoter region and to the Rv1999c
CC promoter region. It displays strong affinity for cadmium ions, but can
CC also bind zinc, manganese and nickel. Expression increases the
CC intracellular survival of recombinant M. smegmatis in murine macrophage
CC cell line and increases its tolerance to cadmium ions.
CC {ECO:0000269|PubMed:30266832}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30266832}.
CC -!- DOMAIN: Contains an N-terminal winged-helix-turn-helix (wHTH) DNA-
CC binding domain and a C-terminal alpha helix, which is mainly involved
CC in dimerization (PubMed:30266832). Binding of cadmium causes subtle
CC conformational changes in all key metal-binding residues and conserved
CC DNA-binding residues (PubMed:30266832). {ECO:0000269|PubMed:30266832}.
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DR EMBL; AL123456; CCP46310.1; -; Genomic_DNA.
DR RefSeq; NP_218005.1; NC_000962.3.
DR RefSeq; WP_003418948.1; NZ_NVQJ01000042.1.
DR PDB; 5ZHC; X-ray; 1.97 A; A/B=1-107.
DR PDB; 5ZHV; X-ray; 2.40 A; A/B=1-107.
DR PDB; 5ZI8; X-ray; 2.20 A; A/B=1-107.
DR PDB; 7WH4; X-ray; 2.80 A; A/B=1-107.
DR PDBsum; 5ZHC; -.
DR PDBsum; 5ZHV; -.
DR PDBsum; 5ZI8; -.
DR PDBsum; 7WH4; -.
DR AlphaFoldDB; I6X7F9; -.
DR SMR; I6X7F9; -.
DR STRING; 83332.Rv3488; -.
DR PaxDb; I6X7F9; -.
DR PRIDE; I6X7F9; -.
DR DNASU; 888417; -.
DR GeneID; 45427474; -.
DR GeneID; 888417; -.
DR KEGG; mtu:Rv3488; -.
DR PATRIC; fig|83332.111.peg.3886; -.
DR TubercuList; Rv3488; -.
DR eggNOG; COG1695; Bacteria.
DR OMA; IQIHILH; -.
DR PhylomeDB; I6X7F9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005149; Tscrpt_reg_PadR_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF03551; PadR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cadmium; DNA-binding; Metal-binding; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..107
FT /note="Transcriptional regulator Rv3488"
FT /id="PRO_0000447364"
FT BINDING 16
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000269|PubMed:30266832"
FT BINDING 30
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000269|PubMed:30266832"
FT BINDING 34
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000269|PubMed:30266832"
FT BINDING 101
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000269|PubMed:30266832"
FT MUTAGEN 16
FT /note="H->A: Abolishes cadmium and zinc binding."
FT /evidence="ECO:0000269|PubMed:30266832"
FT MUTAGEN 34
FT /note="H->A: Abolishes cadmium and zinc binding."
FT /evidence="ECO:0000269|PubMed:30266832"
FT HELIX 1..19
FT /evidence="ECO:0007829|PDB:5ZHC"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:5ZHC"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:5ZHC"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:5ZHC"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:5ZHC"
FT HELIX 75..95
FT /evidence="ECO:0007829|PDB:5ZHC"
SQ SEQUENCE 107 AA; 11928 MW; CCE62597646F6D94 CRC64;
MREFQRAAVR LHILHHAADN EVHGAWLTQE LSRHGYRVSP GTLYPTLHRL EADGLLVSEQ
RVVDGRARRV YRATPAGRAA LTEDRRALEE LAREVLGGQS HTAGNGT
