WHIB1_BIFLO
ID WHIB1_BIFLO Reviewed; 92 AA.
AC Q8G5J9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Transcriptional regulator WhiB1;
GN Name=whiB1; Synonyms=wblE; OrderedLocusNames=BL1011;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
RN [2]
RP INDUCTION.
RC STRAIN=B 397M;
RX PubMed=22609519; DOI=10.1016/j.anaerobe.2012.04.011;
RA Averina O.V., Zakharevich N.V., Danilenko V.N.;
RT "Identification and characterization of WhiB-like family proteins of the
RT Bifidobacterium genus.";
RL Anaerobe 18:421-429(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 -!- 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: Low level expression in exponential phase it increases about
CC 8-fold by late stationary phase. Induced by heat (45 degrees Celsius)
CC osmotic and oxidative stress, nutrient starvation, tetracycline, and
CC bile salts. {ECO:0000269|PubMed:22609519}.
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 -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
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DR EMBL; AE014295; AAN24819.1; -; Genomic_DNA.
DR RefSeq; NP_696183.1; NC_004307.2.
DR RefSeq; WP_003835265.1; NC_004307.2.
DR AlphaFoldDB; Q8G5J9; -.
DR SMR; Q8G5J9; -.
DR STRING; 206672.BL1011; -.
DR PRIDE; Q8G5J9; -.
DR EnsemblBacteria; AAN24819; AAN24819; BL1011.
DR GeneID; 66504851; -.
DR KEGG; blo:BL1011; -.
DR PATRIC; fig|206672.9.peg.715; -.
DR HOGENOM; CLU_106245_6_2_11; -.
DR OMA; DTCLKWA; -.
DR PhylomeDB; Q8G5J9; -.
DR PRO; PR:Q8G5J9; -.
DR Proteomes; UP000000439; 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 2: Evidence at transcript level;
KW 4Fe-4S; Cytoplasm; Disulfide bond; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..92
FT /note="Transcriptional regulator WhiB1"
FT /id="PRO_0000420389"
FT DOMAIN 12..74
FT /note="4Fe-4S Wbl-type"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 44
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"
SQ SEQUENCE 92 AA; 10406 MW; 4A0D27B07B495131 CRC64;
MSSAFDWRAK AACRDKDPEL FFPVGNTGAA YQQIEEAKAV CRTCKVIDAC LKCALDTNQD
YGVWGGLSED ERRALKRRAM RARRSQAMQM QI