WHID_STRCO
ID WHID_STRCO Reviewed; 112 AA.
AC Q7AKI9; O88103;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Transcriptional regulator WhiD;
DE AltName: Full=Transcriptional regulator WhiB3;
GN Name=whiD; Synonyms=wblB, whiB3; OrderedLocusNames=SCO4767;
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 Palframan W.;
RL Thesis (1998), University of East Anglia, United Kingdom.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=10708372; DOI=10.1099/00221287-146-2-333;
RA Soliveri J.A., Gomez J., Bishai W.R., Chater K.F.;
RT "Multiple paralogous genes related to the Streptomyces coelicolor
RT developmental regulatory gene whiB are present in Streptomyces and other
RT actinomycetes.";
RL Microbiology 146:333-343(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=10931278; DOI=10.1046/j.1365-2958.2000.01977.x;
RA Molle V., Buttner M.J.;
RT "Different alleles of the response regulator gene bldM arrest Streptomyces
RT coelicolor development at distinct stages.";
RL Mol. Microbiol. 36:1265-1278(2000).
RN [4]
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 [5]
RP FUNCTION, IDENTIFICATION, INDUCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF ALA-21.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=10671449; DOI=10.1128/jb.182.5.1286-1295.2000;
RA Molle V., Palframan W.J., Findlay K.C., Buttner M.J.;
RT "WhiD and WhiB, homologous proteins required for different stages of
RT sporulation in Streptomyces coelicolor A3(2).";
RL J. Bacteriol. 182:1286-1295(2000).
RN [6]
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF CYS-23; CYS-53; CYS-56 AND CYS-62.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=15615709; DOI=10.1074/jbc.m412622200;
RA Jakimowicz P., Cheesman M.R., Bishai W.R., Chater K.F., Thomson A.J.,
RA Buttner M.J.;
RT "Evidence that the Streptomyces developmental protein WhiD, a member of the
RT WhiB family, binds a [4Fe-4S] cluster.";
RL J. Biol. Chem. 280:8309-8315(2005).
RN [7]
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND LACK OF ACTIVITY AS A
RP DISULFIDE REDUCTASE.
RX PubMed=19954209; DOI=10.1021/bi901498v;
RA Crack J.C., den Hengst C.D., Jakimowicz P., Subramanian S., Johnson M.K.,
RA Buttner M.J., Thomson A.J., Le Brun N.E.;
RT "Characterization of [4Fe-4S]-containing and cluster-free forms of
RT Streptomyces WhiD.";
RL Biochemistry 48:12252-12264(2009).
RN [8]
RP DINITROSYLATION.
RX PubMed=21182249; DOI=10.1021/ja109581t;
RA Crack J.C., Smith L.J., Stapleton M.R., Peck J., Watmough N.J.,
RA Buttner M.J., Buxton R.S., Green J., Oganesyan V.S., Thomson A.J.,
RA Le Brun N.E.;
RT "Mechanistic insight into the nitrosylation of the [4Fe-4S] cluster of
RT WhiB-like proteins.";
RL J. Am. Chem. Soc. 133:1112-1121(2011).
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 positive role in prespore maturation and the
CC initiation of sporulation septation. {ECO:0000250,
CC ECO:0000269|PubMed:10671449}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Anaerobically binds 1 [4Fe-4S] cluster per subunit; cluster is
CC lost on exposure to O(2). Cluster is stabilized in the presence of
CC mycothiol. Following nitrosylation of the [4Fe-4S] cluster binds 1
CC [4Fe-8(NO)] cluster per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0 to 8.0 for 4Fe-4S stability.
CC {ECO:0000269|PubMed:19954209};
CC -!- SUBUNIT: The 4Fe-4S form is a monomer; upon oxidation forms a
CC disulfide-bonded homodimer. {ECO:0000269|PubMed:15615709,
CC ECO:0000269|PubMed:19954209}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- INDUCTION: Expressed in exponential phase (PubMed:10708372). Expressed
CC from 2 promoters at the onset of sporulation, no longer expressed in
CC mature colonies (PubMed:10671449). {ECO:0000269|PubMed:10671449,
CC ECO:0000269|PubMed:10708372}.
CC -!- PTM: Can be nitrosylated by NO, 8 NO react per cluster. These complexes
CC are quite stable under anaerobic conditions, but degrade slowly
CC aerobically.
CC -!- PTM: Upon Fe-S cluster removal intramolecular disulfide bonds are
CC formed. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Forms white aerial mycelium. Sporulation is
CC reduced, spores are heat sensitive, lyse frequently and highly
CC irregular in size. Septum placement and spore cell wall thickness is
CC irregular. {ECO:0000269|PubMed:10671449}.
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; AJ010601; CAA09262.1; -; Genomic_DNA.
DR EMBL; AJ239086; CAB43031.1; -; Genomic_DNA.
DR EMBL; AL939121; CAA20423.1; -; Genomic_DNA.
DR PIR; T35596; T35596.
DR RefSeq; NP_628925.1; NC_003888.3.
DR RefSeq; WP_003974205.1; NZ_VNID01000016.1.
DR AlphaFoldDB; Q7AKI9; -.
DR SMR; Q7AKI9; -.
DR STRING; 100226.SCO4767; -.
DR GeneID; 1100208; -.
DR KEGG; sco:SCO4767; -.
DR PATRIC; fig|100226.15.peg.4839; -.
DR eggNOG; ENOG5032S23; Bacteria.
DR HOGENOM; CLU_106245_6_0_11; -.
DR InParanoid; Q7AKI9; -.
DR OMA; WQLHGAC; -.
DR PhylomeDB; Q7AKI9; -.
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 1: Evidence at protein 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..112
FT /note="Transcriptional regulator WhiD"
FT /id="PRO_0000420398"
FT DOMAIN 22..86
FT /note="4Fe-4S Wbl-type"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000305"
FT MUTAGEN 21
FT /note="A->T: In whiD16; white on sporulation media, forms
FT defective spores killed at 50 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:10671449"
FT MUTAGEN 23
FT /note="C->A: Spores remain white."
FT /evidence="ECO:0000269|PubMed:15615709"
FT MUTAGEN 53
FT /note="C->A: Spores remain white."
FT /evidence="ECO:0000269|PubMed:15615709"
FT MUTAGEN 56
FT /note="C->A: Spores remain white."
FT /evidence="ECO:0000269|PubMed:15615709"
FT MUTAGEN 62
FT /note="C->A: Spores remain white."
FT /evidence="ECO:0000269|PubMed:15615709"
SQ SEQUENCE 112 AA; 11995 MW; 8948745CF2409311 CRC64;
MADFSRLPGP NADLWDWQLL AACRGVDSSL FFHPEGERGA ARSARENSAK EVCMRCPVRA
ECAAHALAVR EPYGVWGGLT EDEREELMGR ARNRLVAATA SASAGGEAAG PH
