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ID Q9FCJ8_STRCO Unreviewed; 122 AA.
AC Q9FCJ8; Q8GHG1;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 16-JAN-2019, entry version 90.
DE RecName: Full=Transcriptional regulator WhiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN Name=whiB7 {ECO:0000313|EMBL:AAO15313.1};
GN Synonyms=whiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN OrderedLocusNames=SCO5190 {ECO:0000313|EMBL:CAC01320.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAC01320.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3 {ECO:0000313|EMBL:CAC01320.1}, and ATCC BAA-471 / A3(2) /
RC M145 {ECO:0000313|Proteomes:UP000001973};
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.,
RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA Huang C.H., Kieser T., Larke L., Murphy L., Oliver K., O'Neil S.,
RA Rabbinowitsch E., Rajandream M.A., Rutherford K., Rutter S.,
RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA Warren T., Wietzorrek A., Woodward J., Barrell B.G., Parkhill J.,
RA Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces
RT coelicolor A3(2).";
RL Nature 417:141-147(2002).
RN [2] {ECO:0000313|EMBL:AAO15313.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M145 {ECO:0000313|EMBL:AAO15313.1};
RX PubMed=16103351; DOI=10.1073/pnas.0505446102;
RA Morris R.P., Nguyen L., Gatfield J., Visconti K., Nguyen K.,
RA Schnappinger D., Ehrt S., Liu Y., Heifets L., Pieters J.,
RA Schoolnik G., Thompson C.J.;
RT "Ancestral antibiotic resistance in Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12200-12205(2005).
CC -!- FUNCTION: Acts as a transcriptional regulator. Probably redox-
CC responsive. The apo- but not holo-form probably binds DNA.
CC {ECO:0000256|HAMAP-Rule:MF_01479}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01479};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation
CC of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01479};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01479}.
CC -!- PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
CC {ECO:0000256|HAMAP-Rule:MF_01479}.
CC -!- PTM: Upon Fe-S cluster removal intramolecular disulfide bonds are
CC formed. {ECO:0000256|HAMAP-Rule:MF_01479}.
CC -!- SIMILARITY: Belongs to the WhiB family. {ECO:0000256|HAMAP-
CC Rule:MF_01479}.
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DR EMBL; AF205848; AAO15313.1; -; Genomic_DNA.
DR EMBL; AL939122; CAC01320.1; -; Genomic_DNA.
DR RefSeq; NP_629338.1; NC_003888.3.
DR RefSeq; WP_003973786.1; NC_003888.3.
DR STRING; 100226.SCO5190; -.
DR EnsemblBacteria; CAC01320; CAC01320; CAC01320.
DR GeneID; 1100631; -.
DR KEGG; sco:SCO5190; -.
DR PATRIC; fig|100226.15.peg.5273; -.
DR eggNOG; ENOG4105WBQ; Bacteria.
DR eggNOG; ENOG4112352; LUCA.
DR HOGENOM; HOG000247631; -.
DR KO; K18958; -.
DR OMA; RTCPLVE; -.
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:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0047134; F:protein-disulfide reductase 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 HAMAP; MF_01479; WhiB; 1.
DR InterPro; IPR034768; 4FE4S_WBL.
DR InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
DR InterPro; IPR003482; Whib.
DR PANTHER; PTHR38839; PTHR38839; 1.
DR Pfam; PF02467; Whib; 1.
DR PROSITE; PS51674; 4FE4S_WBL; 1.
DR PROSITE; PS00354; HMGI_Y; 1.
PE 3: Inferred from homology;
DR PRODOM; Q9FCJ8.
DR SWISS-2DPAGE; Q9FCJ8.
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01479};
KW Complete proteome {ECO:0000313|Proteomes:UP000001973};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01479};
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01479};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01479,
KW ECO:0000313|EMBL:CAC01320.1}; Iron {ECO:0000256|HAMAP-Rule:MF_01479};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01479};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01479};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_01479};
KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01479}.
FT DOMAIN 48 105 4Fe-4S Wbl-type. {ECO:0000259|PROSITE:
FT PS51674}.
FT METAL 49 49 Dinitrosyliron [4Fe-8(NO)]; alternate.
FT {ECO:0000256|HAMAP-Rule:MF_01479}.
FT METAL 49 49 Iron-sulfur (4Fe-4S); alternate.
FT {ECO:0000256|HAMAP-Rule:MF_01479}.
FT METAL 72 72 Dinitrosyliron [4Fe-8(NO)]; alternate.
FT {ECO:0000256|HAMAP-Rule:MF_01479}.
FT METAL 72 72 Iron-sulfur (4Fe-4S); alternate.
FT {ECO:0000256|HAMAP-Rule:MF_01479}.
FT METAL 75 75 Dinitrosyliron [4Fe-8(NO)]; alternate.
FT {ECO:0000256|HAMAP-Rule:MF_01479}.
FT METAL 75 75 Iron-sulfur (4Fe-4S); alternate.
FT {ECO:0000256|HAMAP-Rule:MF_01479}.
FT METAL 81 81 Dinitrosyliron [4Fe-8(NO)]; alternate.
FT {ECO:0000256|HAMAP-Rule:MF_01479}.
FT METAL 81 81 Iron-sulfur (4Fe-4S); alternate.
FT {ECO:0000256|HAMAP-Rule:MF_01479}.
SQ SEQUENCE 122 AA; 13201 MW; 41063B4F0DA45CB3 CRC64;
MQLEAHAPSV PPSDTIPKPC STEDSTLTPL TALTALDDAI ENLGVPVPCR SYDPEVFFAE
SPADVEYAKS LCRTCPLIEA CLAGAKERRE PWGVWGGELF VQGVVVARKR PRGRPRKNPV
SA
//
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