WHIB6_MYCTU
ID WHIB6_MYCTU Reviewed; 116 AA.
AC P9WF37; F2GDM3; L0TGU1; P96215; Q7D4Q1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Probable transcriptional regulator WhiB6;
GN Name=whiB6; OrderedLocusNames=Rv3862c;
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 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 [3]
RP INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22780904; DOI=10.1111/j.1365-2958.2012.08165.x;
RA Chawla M., Parikh P., Saxena A., Munshi M., Mehta M., Mai D.,
RA Srivastava A.K., Narasimhulu K.V., Redding K.E., Vashi N., Kumar D.,
RA Steyn A.J., Singh A.;
RT "Mycobacterium tuberculosis WhiB4 regulates oxidative stress response to
RT modulate survival and dissemination in vivo.";
RL Mol. Microbiol. 85:1148-1165(2012).
CC -!- FUNCTION: Acts as a transcriptional regulator. Probably redox-
CC responsive. The apo- but not holo-form probably binds DNA (By
CC similarity). The apo-form has been shown to act as a protein disulfide
CC reductase. {ECO:0000250, 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: Weakly expressed in exponential phase, more induced upon
CC entry into stationary phase. 3-fold induced by streptomycin and pH 4.5,
CC 4-fold by ethanol. Slightly induced during entry into hypoxia, by cAMP,
CC in macrophage infection and 5-fold induced by NO. Repressed by WhiB4.
CC {ECO:0000269|PubMed:22780904}.
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.
CC -!- MASS SPECTROMETRY: Mass=17670.02; Method=MALDI; Note=Fully oxidized
CC recombinant protein tagged at both termini.;
CC Evidence={ECO:0000269|PubMed:19016840};
CC -!- MASS SPECTROMETRY: Mass=17902.90; Method=MALDI; Note=Fully reduced
CC recombinant protein tagged at both termini.;
CC Evidence={ECO:0000269|PubMed:19016840};
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46691.1; -; Genomic_DNA.
DR PIR; C70656; C70656.
DR RefSeq; NP_218379.1; NC_000962.3.
DR RefSeq; WP_003899734.1; NZ_NVQJ01000057.1.
DR AlphaFoldDB; P9WF37; -.
DR SMR; P9WF37; -.
DR STRING; 83332.Rv3862c; -.
DR PaxDb; P9WF37; -.
DR DNASU; 886190; -.
DR GeneID; 45427866; -.
DR GeneID; 886190; -.
DR KEGG; mtu:Rv3862c; -.
DR PATRIC; fig|83332.12.peg.4307; -.
DR TubercuList; Rv3862c; -.
DR eggNOG; ENOG5031A0R; Bacteria.
DR OMA; AKAICRA; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0035731; F:dinitrosyl-iron complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01479; WhiB; 1.
DR InterPro; IPR034768; 4FE4S_WBL.
DR InterPro; IPR003482; Whib.
DR Pfam; PF02467; Whib; 1.
DR PROSITE; PS51674; 4FE4S_WBL; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; Disulfide bond; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..116
FT /note="Probable transcriptional regulator WhiB6"
FT /id="PRO_0000420386"
FT DOMAIN 33..86
FT /note="4Fe-4S Wbl-type"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 116 AA; 12792 MW; 7FDD5ABBD7F22A94 CRC64;
MRYAFAAEAT TCNAFWRNVD MTVTALYEVP LGVCTQDPDR WTTTPDDEAK TLCRACPRRW
LCARDAVESA GAEGLWAGVV IPESGRARAF ALGQLRSLAE RNGYPVRDHR VSAQSA
