WHIB7_MYCS2
ID WHIB7_MYCS2 Reviewed; 103 AA.
AC A0QTT1; I7FZ62;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Transcriptional regulator WhiB7;
GN Name=whiB7; OrderedLocusNames=MSMEG_1953, MSMEI_1910;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=22069311; DOI=10.1074/jbc.m111.302588;
RA Burian J., Ramon-Garcia S., Sweet G., Gomez-Velasco A., Av-Gay Y.,
RA Thompson C.J.;
RT "The mycobacterial transcriptional regulator whiB7 gene links redox
RT homeostasis and intrinsic antibiotic resistance.";
RL J. Biol. Chem. 287:299-310(2012).
CC -!- FUNCTION: Acts as a transcriptional regulator. Probably redox-
CC responsive. The apo- but not holo-form probably binds DNA (By
CC similarity). Participates in maintaining a reduced cytoplasmic
CC (MSH/MSSM) environment under normal growth conditions and directly or
CC indirectly controls the concentration of mycothiol (MSH + MSSM).
CC {ECO:0000250, ECO:0000269|PubMed:22069311}.
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: By a considerable number of antibiotics many of which
CC perturb respiration, redox balance, or transmembrane ion flux,
CC including erythromycin. Much stronger induction by erythromycin plus
CC the reducing agent DTT but not erythromycin plus the oxidizing agent
CC diamide. Positively regulates its own expression.
CC {ECO:0000269|PubMed:22069311}.
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: Not essential. Cells have a 5-X decrease in
CC mycothiol reduced form (MSH)/ mycothiol oxidized disulfide form (MSSM),
CC an indicator of a more oxidzed cytoplasm.
CC {ECO:0000269|PubMed:22069311}.
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP38382.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; CP000480; ABK72788.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38382.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003893333.1; NZ_SIJM01000020.1.
DR RefSeq; YP_886319.1; NC_008596.1.
DR AlphaFoldDB; A0QTT1; -.
DR SMR; A0QTT1; -.
DR STRING; 246196.MSMEI_1910; -.
DR EnsemblBacteria; ABK72788; ABK72788; MSMEG_1953.
DR EnsemblBacteria; AFP38382; AFP38382; MSMEI_1910.
DR GeneID; 66733384; -.
DR KEGG; msg:MSMEI_1910; -.
DR KEGG; msm:MSMEG_1953; -.
DR PATRIC; fig|246196.19.peg.1931; -.
DR eggNOG; ENOG5032RVG; Bacteria.
DR OMA; CHVEDPD; -.
DR OrthoDB; 1974660at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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; Antibiotic resistance; Cytoplasm; Disulfide bond; DNA-binding;
KW Iron; Iron-sulfur; Metal-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..103
FT /note="Transcriptional regulator WhiB7"
FT /id="PRO_0000420395"
FT DOMAIN 25..82
FT /note="4Fe-4S Wbl-type"
FT REGION 82..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 103 AA; 10950 MW; E671ACB3F894C22C CRC64;
MSIAMTAPTT GVAPMTCETR LPAVPCHVGD PDLWFAENPG DLERAKALCA GCPIRVQCLT
AALERQEPWG VWGGEILDRG SIVARKRPRG RPRKDSGGNP AAA
