WHB7A_MYCTU
ID WHB7A_MYCTU Reviewed; 92 AA.
AC Q6MX01; F2GK66; L0TDF5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable transcriptional regulator WhiB7;
GN Name=whiB7; Synonyms=Rv3197A; OrderedLocusNames=Rv3197.1;
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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=1254, and ATCC 25618 / H37Rv;
RX PubMed=16103351; DOI=10.1073/pnas.0505446102;
RA Morris R.P., Nguyen L., Gatfield J., Visconti K., Nguyen K.,
RA Schnappinger D., Ehrt S., Liu Y., Heifets L., Pieters J., Schoolnik G.,
RA Thompson C.J.;
RT "Ancestral antibiotic resistance in Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12200-12205(2005).
RN [3]
RP FUNCTION AS A PROTEIN DISULFIDE REDUCTASE, COFACTOR, MASS SPECTROMETRY, AND
RP DISULFIDE BOND.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19016840; DOI=10.1111/j.1742-4658.2008.06755.x;
RA Alam M.S., Garg S.K., Agrawal P.;
RT "Studies on structural and functional divergence among seven WhiB proteins
RT of Mycobacterium tuberculosis H37Rv.";
RL FEBS J. 276:76-93(2009).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22069311; DOI=10.1074/jbc.m111.302588;
RA Burian J., Ramon-Garcia S., Sweet G., Gomez-Velasco A., Av-Gay Y.,
RA Thompson C.J.;
RT "The mycobacterial transcriptional regulator whiB7 gene links redox
RT homeostasis and intrinsic antibiotic resistance.";
RL J. Biol. Chem. 287:299-310(2012).
CC -!- FUNCTION: The apo- but not holo-form probably binds DNA (By
CC similarity). Acts as a transcriptional regulator. Probably redox-
CC responsive. Upon overproduction at least 10 other genes are up-
CC regulated, among them are Rv1258c, Rv1988, Rv2301, Rv2416c, Rv2725c and
CC whiB7 itself. Probably redox-responsive. The apo-form has been shown to
CC act as a protein disulfide reductase. {ECO:0000250,
CC ECO:0000269|PubMed:16103351, ECO:0000269|PubMed:19016840}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250, ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. Contains 1 [2Fe-2S] cluster
CC after reconstitution of overexpressed protein from E.coli. Following
CC nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per
CC subunit. {ECO:0000250, ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: By sublethal doses of antibiotics such as erythromycin,
CC streptomycin and tetracycline as well as the fatty acids palmitic and
CC oleic acid (in clinical strain 1254). By the antibiotic erythromycin.
CC Positively regulates its own expression (in strain H37Rv).
CC {ECO:0000269|PubMed:16103351, ECO:0000269|PubMed:22069311}.
CC -!- PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
CC {ECO:0000250}.
CC -!- PTM: Upon Fe-S cluster removal intramolecular disulfide bonds are
CC formed. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=15697.81; Method=MALDI; Note=Fully oxidized
CC recombinant protein tagged at both termini.;
CC Evidence={ECO:0000269|PubMed:19016840};
CC -!- MASS SPECTROMETRY: Mass=15924.16; Method=MALDI; Note=Fully reduced
CC recombinant protein tagged at both termini.;
CC Evidence={ECO:0000269|PubMed:19016840};
CC -!- DISRUPTION PHENOTYPE: Decreased resistance to macrolides, a
CC lincosamide, and an aminoglycoside antibiotic.
CC {ECO:0000269|PubMed:16103351}.
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46011.1; -; Genomic_DNA.
DR RefSeq; WP_003899963.1; NZ_NVQJ01000003.1.
DR RefSeq; YP_177940.1; NC_000962.3.
DR PDB; 7KIF; EM; 2.94 A; Z=1-92.
DR PDB; 7KIM; EM; 3.38 A; Z=1-92.
DR PDB; 7KUF; X-ray; 2.60 A; A=1-92.
DR PDB; 7KUG; X-ray; 1.55 A; A/C=1-79.
DR PDBsum; 7KIF; -.
DR PDBsum; 7KIM; -.
DR PDBsum; 7KUF; -.
DR PDBsum; 7KUG; -.
DR AlphaFoldDB; Q6MX01; -.
DR SMR; Q6MX01; -.
DR STRING; 83332.Rv3197A; -.
DR PaxDb; Q6MX01; -.
DR DNASU; 3205083; -.
DR GeneID; 3205083; -.
DR GeneID; 45427187; -.
DR KEGG; mtu:Rv3197A; -.
DR TubercuList; Rv3197.1; -.
DR eggNOG; ENOG5032RVG; Bacteria.
DR InParanoid; Q6MX01; -.
DR OMA; CHVEDPD; -.
DR PhylomeDB; Q6MX01; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0035731; F:dinitrosyl-iron complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IMP:MTBBASE.
DR GO; GO:0070542; P:response to fatty acid; IMP:MTBBASE.
DR HAMAP; MF_01479; WhiB; 1.
DR InterPro; IPR034768; 4FE4S_WBL.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR003482; Whib.
DR PANTHER; PTHR38839; PTHR38839; 1.
DR Pfam; PF02178; AT_hook; 1.
DR Pfam; PF02467; Whib; 1.
DR PROSITE; PS51674; 4FE4S_WBL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Antibiotic resistance; Cytoplasm; Disulfide bond;
KW DNA-binding; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..92
FT /note="Probable transcriptional regulator WhiB7"
FT /id="PRO_0000420387"
FT DOMAIN 19..76
FT /note="4Fe-4S Wbl-type"
FT DNA_BIND 80..91
FT /note="A.T hook"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:7KIM"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:7KUG"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:7KUG"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:7KUG"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:7KUG"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:7KUG"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:7KUG"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:7KIF"
SQ SEQUENCE 92 AA; 10139 MW; 18EA51941235B9E8 CRC64;
MSVLTVPRQT PRQRLPVLPC HVGDPDLWFA DTPAGLEVAK TLCVSCPIRR QCLAAALQRA
EPWGVWGGEI FDQGSIVSHK RPRGRPRKDA VA
