WHIB4_MYCMM
ID WHIB4_MYCMM Reviewed; 116 AA.
AC B2HK79;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Transcriptional regulator WhiB4;
GN Name=whiB4; OrderedLocusNames=MMAR_5170;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=E11;
RX PubMed=22505711; DOI=10.1074/jbc.m111.336461;
RA van der Woude A.D., Sarkar D., Bhatt A., Sparrius M., Raadsen S.A.,
RA Boon L., Geurtsen J., van der Sar A.M., Luirink J., Houben E.N.,
RA Besra G.S., Bitter W.;
RT "Unexpected link between lipooligosaccharide biosynthesis and surface
RT protein release in Mycobacterium marinum.";
RL J. Biol. Chem. 287:20417-20429(2012).
CC -!- FUNCTION: Acts as a transcriptional regulator. Probably redox-
CC responsive. The apo- but not holo-form probably binds DNA (By
CC similarity). Plays a role in lipooligosaccharide (LOS) biosynthesis by
CC regulating LOS gene expression. {ECO:0000250,
CC ECO:0000269|PubMed:22505711}.
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 -!- 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: Has a rough-dry colony morphology. About 50%
CC lipooligosaccharide (LOS) biosynthesis, with LOS-III and LOS-IV being
CC most affected. Decreased expression of a number of genes involved in
CC LOS synthesis, such as mmar_2326, mmar_2327, mmar_2354 and papA3
CC (mmar_2355). {ECO:0000269|PubMed:22505711}.
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; CP000854; ACC43576.1; -; Genomic_DNA.
DR RefSeq; WP_012396686.1; NC_010612.1.
DR AlphaFoldDB; B2HK79; -.
DR SMR; B2HK79; -.
DR STRING; 216594.MMAR_5170; -.
DR EnsemblBacteria; ACC43576; ACC43576; MMAR_5170.
DR GeneID; 64258450; -.
DR KEGG; mmi:MMAR_5170; -.
DR eggNOG; ENOG5032TCV; Bacteria.
DR HOGENOM; CLU_106245_2_2_11; -.
DR OMA; FAAQRKH; -.
DR OrthoDB; 1929976at2; -.
DR PHI-base; PHI:7189; -.
DR Proteomes; UP000001190; 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; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..116
FT /note="Transcriptional regulator WhiB4"
FT /id="PRO_0000420392"
FT DOMAIN 36..92
FT /note="4Fe-4S Wbl-type"
FT BINDING 37
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 BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 116 AA; 13016 MW; 6C91CB9F4DA85E77 CRC64;
MSGIRPVDGR ANLTSAQNLL STGEAEERIN WVSKALCRAT DPDELFVRGA AQRKAAVICR
HCPVMQECGA DALDNKVEFG VWGGMTERQR RALLKQHPEV VSWSDYFEKR KRRSVG
