WHIB3_MYCTO
ID WHIB3_MYCTO Reviewed; 102 AA.
AC P9WF40; F2GEG1; L0TCG8; Q50710; Q7D5K3;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Redox- and pH-responsive transcriptional regulator WhiB3;
GN Name=whiB3; OrderedLocusNames=MT3525;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP INDUCTION.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=16870781; DOI=10.1128/aac.00295-06;
RA Geiman D.E., Raghunand T.R., Agarwal N., Bishai W.R.;
RT "Differential gene expression in response to exposure to antimycobacterial
RT agents and other stress conditions among seven Mycobacterium tuberculosis
RT whiB-like genes.";
RL Antimicrob. Agents Chemother. 50:2836-2841(2006).
RN [3]
RP INDUCTION.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=22829866; DOI=10.1371/journal.pone.0037516;
RA Larsson C., Luna B., Ammerman N.C., Maiga M., Agarwal N., Bishai W.R.;
RT "Gene expression of Mycobacterium tuberculosis putative transcription
RT factors whiB1-7 in redox environments.";
RL PLoS ONE 7:E37516-E37516(2012).
CC -!- FUNCTION: A redox-sensitive transcriptional regulator. Maintains
CC intracellular redox homeostasis by regulating catabolic metabolism and
CC polyketide biosynthesis. Regulates expression of the redox buffer
CC ergothioneine (ERG). In concert with myothiol (MSH), another redox
CC buffer, responds to low pH leading to acid resistance. Senses changes
CC in the intracellular redox state and helps mediate a metabolic
CC switchover to preferred in vivo carbon sources (fatty acids). The
CC apo- but not holo-form probably binds DNA (By similarity).
CC {ECO:0000250|UniProtKB:P9WF41}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P9WF41};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of
CC the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
CC {ECO:0000250|UniProtKB:P9WF41};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9S426}.
CC -!- INDUCTION: Strongly expressed upon entry into stationary phase, 12-fold
CC induced at pH 4.5, 10-fold induced by streptomycin, 2-fold by
CC starvation and by ethanol (PubMed:16870781). Repressed during iron-
CC starvation (PubMed:16870781). Slightly induced by hypoxia and cAMP, 9-
CC fold by NO (PubMed:22829866). Only slightly induced in macrophage and
CC mouse infection (PubMed:22829866). {ECO:0000269|PubMed:16870781,
CC ECO:0000269|PubMed:22829866}.
CC -!- PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
CC {ECO:0000250|UniProtKB:P9WF41}.
CC -!- PTM: Upon Fe-S cluster removal intramolecular disulfide bonds are
CC formed. {ECO:0000250|UniProtKB:P9WF41}.
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
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DR EMBL; AE000516; AAK47863.1; -; Genomic_DNA.
DR PIR; E70737; E70737.
DR RefSeq; WP_003418017.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WF40; -.
DR SMR; P9WF40; -.
DR EnsemblBacteria; AAK47863; AAK47863; MT3525.
DR GeneID; 45427412; -.
DR KEGG; mtc:MT3525; -.
DR PATRIC; fig|83331.31.peg.3782; -.
DR HOGENOM; CLU_106245_6_0_11; -.
DR Proteomes; UP000001020; 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 PANTHER; PTHR38839; PTHR38839; 1.
DR Pfam; PF02467; Whib; 1.
DR PROSITE; PS51674; 4FE4S_WBL; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Cytoplasm; Disulfide bond; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Transcription; Transcription regulation; Virulence.
FT CHAIN 1..102
FT /note="Redox- and pH-responsive transcriptional regulator
FT WhiB3"
FT /id="PRO_0000428605"
FT DOMAIN 22..86
FT /note="4Fe-4S Wbl-type"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P9WF41"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P9WF41"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P9WF41"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P9WF41"
SQ SEQUENCE 102 AA; 11612 MW; C38A6774457F71BA CRC64;
MPQPEQLPGP NADIWNWQLQ GLCRGMDSSM FFHPDGERGR ARTQREQRAK EMCRRCPVIE
ACRSHALEVG EPYGVWGGLS ESERDLLLKG TMGRTRGIRR TA
