WHIB2_MYCSM
ID WHIB2_MYCSM Reviewed; 129 AA.
AC Q9S426;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Transcriptional regulator WhiB2;
GN Name=whmD; Synonyms=whiB2;
OS Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1772;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=mc(2)6 1-2c;
RX PubMed=10880571; DOI=10.1073/pnas.140225297;
RA Gomez J.E., Bishai W.R.;
RT "whmD is an essential mycobacterial gene required for proper septation and
RT cell division.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:8554-8559(2000).
RN [2]
RP SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=mc(2)6 1-2c;
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 [3]
RP FUNCTION, COFACTOR, SUBUNIT, AND MUTAGENESIS OF CYS-67; ASP-71; CYS-90;
RP CYS-93; CYS-99; GLY-111 AND LEU-116.
RC STRAIN=mc(2)6 1-2c;
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).
CC -!- FUNCTION: Acts as a transcriptional regulator. Probably redox-
CC responsive. The apo- but not holo-form probably binds DNA (By
CC similarity). Affects the localization or efficiency of septum
CC formation. Complemented by whiB2 of M.tuberculosis and whiB of
CC S.coelicolor. {ECO:0000250, ECO:0000269|PubMed:10880571,
CC ECO:0000269|PubMed:16980499}.
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. Following nitrosylation of
CC the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
CC {ECO:0000250, ECO:0000305};
CC -!- SUBUNIT: Oligomeric in native gel electrophoresis.
CC {ECO:0000269|PubMed:16980499}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16946268}.
CC -!- INDUCTION: In exponential phase (at protein level).
CC {ECO:0000269|PubMed:16946268}.
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: Essential. In depletion experiments, individual
CC cells are elongated and/or filamented, with diminished septum formation
CC and aberrant septal placement. The septa that do form may be immature
CC as cytokinesis does not occur. Has no effect on FtsZ accumulation.
CC Cells are less viable, colonies are smaller and the mutant is non-acid-
CC fast under conditions of acetamide withdrawal.
CC {ECO:0000269|PubMed:10880571, ECO:0000269|PubMed:16946268}.
CC -!- MISCELLANEOUS: In this protein one of the ligands for the Fe-S cluster
CC may be provided by Asp-71 rather than Cys-67.
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF164439; AAD47079.1; -; Genomic_DNA.
DR RefSeq; WP_003893222.1; NZ_SIUA01000021.1.
DR AlphaFoldDB; Q9S426; -.
DR SMR; Q9S426; -.
DR OMA; CQGCEVR; -.
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; Cytoplasm; Disulfide bond; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Transcription; Transcription regulation.
FT CHAIN 1..129
FT /note="Transcriptional regulator WhiB2"
FT /id="PRO_0000420396"
FT DOMAIN 66..123
FT /note="4Fe-4S Wbl-type"
FT REGION 23..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT MUTAGEN 67
FT /note="C->A: Not required to complement filamentous
FT phenotype in depletion experiments."
FT /evidence="ECO:0000269|PubMed:16980499"
FT MUTAGEN 71
FT /note="D->A: Required to complement filamentous phenotype
FT in depletion experiments."
FT /evidence="ECO:0000269|PubMed:16980499"
FT MUTAGEN 90
FT /note="C->A: Required to complement filamentous phenotype
FT in depletion experiments."
FT /evidence="ECO:0000269|PubMed:16980499"
FT MUTAGEN 93
FT /note="C->A: Required to complement filamentous phenotype
FT in depletion experiments."
FT /evidence="ECO:0000269|PubMed:16980499"
FT MUTAGEN 99
FT /note="C->A: Required to complement filamentous phenotype
FT in depletion experiments."
FT /evidence="ECO:0000269|PubMed:16980499"
FT MUTAGEN 111
FT /note="G->P: Required to complement filamentous phenotype
FT in depletion experiments."
FT /evidence="ECO:0000269|PubMed:16980499"
FT MUTAGEN 116
FT /note="L->P: Partial complementation of filamentous
FT phenotype in depletion experiments."
FT /evidence="ECO:0000269|PubMed:16980499"
SQ SEQUENCE 129 AA; 14396 MW; 953A5C10E00CC16C CRC64;
MSYESGDFDR VVRFDNRLLG SVSHAPHIDT GSTPTGAAGR PQLSLVPDSF DVAPEAEEDQ
WQERALCAQT DPEAFFPEKG GSTREAKRIC QGCEVRDACL EYALAHDERF GIWGGLSERE
RRRLKRGII
