WHIB_STRCO
ID WHIB_STRCO Reviewed; 87 AA.
AC Q7AKN0; Q53963;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Transcriptional regulator WhiB;
GN Name=whiB; Synonyms=whiB2; OrderedLocusNames=SCO3034;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RA Bruton C.J.;
RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=1316997; DOI=10.1007/bf00266237;
RA Davis N.K., Chater K.F.;
RT "The Streptomyces coelicolor whiB gene encodes a small transcription
RT factor-like protein dispensable for growth but essential for sporulation.";
RL Mol. Gen. Genet. 232:351-358(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [4]
RP INDUCTION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=1400171; DOI=10.1128/jb.174.19.6215-6220.1992;
RA Soliveri J., Brown K.L., Buttner M.J., Chater K.F.;
RT "Two promoters for the whiB sporulation gene of Streptomyces coelicolor
RT A3(2) and their activities in relation to development.";
RL J. Bacteriol. 174:6215-6220(1992).
RN [5]
RP FUNCTION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
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). Complements a whiB2 disruption mutant in M.smegmatis (AC
CC Q9S426). {ECO:0000250, ECO:0000269|PubMed:16980499}.
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: Transcribed from 2 promoters; expression from the stronger
CC promoter is induced when aerial hyphae became visible and then
CC declines. Expressed during exponential growth but decreases during
CC stationary phase in liquid culture. {ECO:0000269|PubMed:1400171}.
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: A white non-sporulating phenotype. Spore
CC septation does not occur. {ECO:0000269|PubMed:1316997}.
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000305}.
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DR EMBL; X62287; CAA44175.1; -; Genomic_DNA.
DR EMBL; AL939114; CAB88918.1; -; Genomic_DNA.
DR PIR; S20912; S20912.
DR RefSeq; NP_627256.1; NC_003888.3.
DR RefSeq; WP_003975777.1; NZ_VNID01000013.1.
DR AlphaFoldDB; Q7AKN0; -.
DR SMR; Q7AKN0; -.
DR STRING; 100226.SCO3034; -.
DR GeneID; 1098467; -.
DR GeneID; 24313836; -.
DR GeneID; 67400763; -.
DR KEGG; sco:SCO3034; -.
DR PATRIC; fig|100226.15.peg.3094; -.
DR eggNOG; ENOG5032RUK; Bacteria.
DR HOGENOM; CLU_106245_6_1_11; -.
DR InParanoid; Q7AKN0; -.
DR OMA; KRICGRC; -.
DR PhylomeDB; Q7AKN0; -.
DR PRO; PR:Q7AKN0; -.
DR Proteomes; UP000001973; 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 GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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; Cytoplasm; Disulfide bond; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..87
FT /note="Transcriptional regulator WhiB"
FT /id="PRO_0000420397"
FT DOMAIN 24..81
FT /note="4Fe-4S Wbl-type"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 87 AA; 9878 MW; DDF71B4AE6259B95 CRC64;
MTELVQQLLV DDADEELGWQ ERALCAQTDP ESFFPEKGGS TREAKKVCLA CEVRSECLEY
ALANDERFGI WGGLSERERR RLKKAAV