WHIB3_MYCBO
ID WHIB3_MYCBO Reviewed; 102 AA.
AC Q7TWJ2; A0A1R3Y4A3; X2BPI5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Redox-responsive transcriptional regulator WhiB3;
GN Name=whiB3; OrderedLocusNames=BQ2027_MB3450;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 35723 / TMC 405;
RX PubMed=11880648; DOI=10.1073/pnas.052705399;
RA Steyn A.J., Collins D.M., Hondalus M.K., Jacobs W.R. Jr., Kawakami R.P.,
RA Bloom B.R.;
RT "Mycobacterium tuberculosis WhiB3 interacts with RpoV to affect host
RT survival but is dispensable for in vivo growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3147-3152(2002).
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). Plays a role
CC in virulence (PubMed:11880648). {ECO:0000250|UniProtKB:P9WF41,
CC ECO:0000269|PubMed:11880648}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9S426}.
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 -!- DISRUPTION PHENOTYPE: Not essential for growth in culture, however
CC required for growth in vivo in guinea pig infections. Note strain ATCC
CC 35723 is virulent whereas ATCC BAA-935 is not.
CC {ECO:0000269|PubMed:11880648}.
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
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DR EMBL; LT708304; SIU02078.1; -; Genomic_DNA.
DR RefSeq; NP_857090.1; NC_002945.3.
DR RefSeq; WP_003418017.1; NC_002945.4.
DR AlphaFoldDB; Q7TWJ2; -.
DR SMR; Q7TWJ2; -.
DR EnsemblBacteria; SIU02078; SIU02078; BQ2027_MB3450.
DR GeneID; 45427412; -.
DR PATRIC; fig|233413.5.peg.3785; -.
DR OMA; WQLHGAC; -.
DR Proteomes; UP000001419; 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 3: Inferred from homology;
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-responsive transcriptional regulator WhiB3"
FT /id="PRO_0000420391"
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
