WHB2A_MYCTU
ID WHB2A_MYCTU Reviewed; 89 AA.
AC O53353; L0TF37;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Transcriptional regulator WhiB2;
DE AltName: Full=Probable chaperone WhiB2;
GN Name=whiB2; OrderedLocusNames=Rv3260c;
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, COFACTOR, MASS SPECTROMETRY, AND 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 COFACTOR, AND DNA-BINDING.
RX PubMed=20545868; DOI=10.1111/j.1365-2958.2010.07235.x;
RA Rybniker J., Nowag A., van Gumpel E., Nissen N., Robinson N., Plum G.,
RA Hartmann P.;
RT "Insights into the function of the WhiB-like protein of mycobacteriophage
RT TM4--a transcriptional inhibitor of WhiB2.";
RL Mol. Microbiol. 77:642-657(2010).
RN [4]
RP FUNCTION AS A CHAPERONE, PHOSPHORYLATION AT SER-42, AND MUTAGENESIS OF
RP CYS-27; SER-42; CYS-50; CYS-53 AND CYS-59.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22686939; DOI=10.1111/j.1742-4658.2012.08662.x;
RA Konar M., Alam M.S., Arora C., Agrawal P.;
RT "WhiB2/Rv3260c, a cell division-associated protein of Mycobacterium
RT tuberculosis H37Rv, has properties of a chaperone.";
RL FEBS J. 279:2781-2792(2012).
CC -!- FUNCTION: Acts as a transcriptional regulator. Probably redox-
CC responsive. The apo- but not holo-form probably binds DNA (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: The apo-form functions as a chaperone, preventing aggregation
CC or helping in correct refolding of a number of substrates; this
CC activity does not require ATP or the ability to bind a Fe-S cluster.
CC Chaperone activity is insensitive to the redox state of its cysteine
CC residues. The apo-form has no protein disulfide reductase activity. The
CC apo-form binds to its own promoter. {ECO:0000269|PubMed:19016840,
CC ECO:0000269|PubMed:22686939}.
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 -!- PTM: May be phosphorylated, possibly on Ser-42.
CC {ECO:0000269|PubMed:22686939}.
CC -!- PTM: The cluster is degraded quickly in the presence of air. Upon
CC cluster removal intramolecular disulfide bonds are formed.
CC -!- PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
CC {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=15041.115; Method=MALDI; Note=Fully oxidized
CC recombinant protein tagged at both termini.;
CC Evidence={ECO:0000269|PubMed:19016840};
CC -!- MASS SPECTROMETRY: Mass=15276.807; 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; CCP46079.1; -; Genomic_DNA.
DR PIR; C70847; C70847.
DR RefSeq; NP_217777.1; NC_000962.3.
DR RefSeq; WP_003417079.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; O53353; -.
DR SMR; O53353; -.
DR STRING; 83332.Rv3260c; -.
DR iPTMnet; O53353; -.
DR PaxDb; O53353; -.
DR DNASU; 888687; -.
DR GeneID; 888687; -.
DR KEGG; mtu:Rv3260c; -.
DR PATRIC; fig|83332.111.peg.3639; -.
DR TubercuList; Rv3260c; -.
DR eggNOG; ENOG5032RUK; Bacteria.
DR InParanoid; O53353; -.
DR OMA; KRICGRC; -.
DR PhylomeDB; O53353; -.
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 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; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..89
FT /note="Transcriptional regulator WhiB2"
FT /id="PRO_0000420380"
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"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:22686939"
FT MUTAGEN 27
FT /note="C->A: Retains chaperone activity; when associated
FT with A-50, A-53 and A-59."
FT /evidence="ECO:0000269|PubMed:22686939"
FT MUTAGEN 42
FT /note="S->A: Considerable loss of chaperone activity."
FT /evidence="ECO:0000269|PubMed:22686939"
FT MUTAGEN 50
FT /note="C->A: Retains chaperone activity; when associated
FT with A-27, A-53 and A-59."
FT /evidence="ECO:0000269|PubMed:22686939"
FT MUTAGEN 53
FT /note="C->A: Retains chaperone activity; when associated
FT with A-27, A-50 and A-59."
FT /evidence="ECO:0000269|PubMed:22686939"
FT MUTAGEN 59
FT /note="C->A: Retains chaperone activity; when associated
FT with A-27, A-50 and A-53."
FT /evidence="ECO:0000269|PubMed:22686939"
SQ SEQUENCE 89 AA; 10157 MW; 04D4D99C01D6D9BD CRC64;
MVPEAPAPFE EPLPPEATDQ WQDRALCAQT DPEAFFPEKG GSTREAKKIC MGCEVRHECL
EYALAHDERF GIWGGLSERE RRRLKRGII
