WHB2B_MYCTO
ID WHB2B_MYCTO Reviewed; 89 AA.
AC Q7D5T7; F2GKT3;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Transcriptional regulator WhiB2;
DE AltName: Full=Probable chaperone WhiB2;
GN Name=whiB2; OrderedLocusNames=MT3358;
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 FUNCTION.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=16980499; DOI=10.1128/jb.00384-06;
RA Raghunand T.R., Bishai W.R.;
RT "Mapping essential domains of Mycobacterium smegmatis WhmD: insights into
RT WhiB structure and function.";
RL J. Bacteriol. 188:6966-6976(2006).
RN [4]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=16946268; DOI=10.1099/mic.0.28911-0;
RA Raghunand T.R., Bishai W.R.;
RT "Mycobacterium smegmatis whmD and its homologue Mycobacterium tuberculosis
RT whiB2 are functionally equivalent.";
RL Microbiology 152:2735-2747(2006).
RN [5]
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: Acts as a transcriptional regulator. Probably redox-
CC responsive. The apo- but not holo-form probably binds DNA (By
CC similarity). Complements a whiB2 disruption mutant in M.smegmatis (AC
CC Q9S426). {ECO:0000250, ECO:0000269|PubMed:16980499}.
CC -!- FUNCTION: The apo-form functions as a chaperone, preventing aggregation
CC or helping in correct refolding of a number of substrates.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Steady during exponential growth (at protein level),
CC decreases as cells age in stationary phase. About 2-fold induced by
CC cell-wall active agents cycloserine, ethambutol and isoniazid, 5-fold
CC by starvation. Repressed by heat shock and SDS. Slightly repressed in
CC hypoxia and in macrophage and mouse infection, slightly induced by NO
CC and cAMP. {ECO:0000269|PubMed:16870781, ECO:0000269|PubMed:16946268,
CC ECO:0000269|PubMed:22829866}.
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 -!- DISRUPTION PHENOTYPE: Probably essential; depletion experiments (by
CC expressing antisense RNA) show smaller colonies are formed, while
CC individual cells are elongated and/or filamented. Colonies are glossy
CC and spherical, cells are less viable. {ECO:0000269|PubMed:16946268}.
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK47700.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK47700.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003417079.1; NZ_KK341227.1.
DR AlphaFoldDB; Q7D5T7; -.
DR SMR; Q7D5T7; -.
DR EnsemblBacteria; AAK47700; AAK47700; MT3358.
DR KEGG; mtc:MT3358; -.
DR PATRIC; fig|83331.31.peg.3614; -.
DR HOGENOM; CLU_106245_4_1_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 1: Evidence at protein level;
KW 4Fe-4S; Chaperone; Cytoplasm; Disulfide bond; DNA-binding; Iron;
KW Iron-sulfur; Metal-binding; Transcription; Transcription regulation.
FT CHAIN 1..89
FT /note="Transcriptional regulator WhiB2"
FT /id="PRO_0000420381"
FT DOMAIN 26..83
FT /note="4Fe-4S Wbl-type"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 50
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 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 89 AA; 10157 MW; 04D4D99C01D6D9BD CRC64;
MVPEAPAPFE EPLPPEATDQ WQDRALCAQT DPEAFFPEKG GSTREAKKIC MGCEVRHECL
EYALAHDERF GIWGGLSERE RRRLKRGII
