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Database: UniProt
Entry: A0A0M4R1U5_9PSEU
LinkDB: A0A0M4R1U5_9PSEU
Original site: A0A0M4R1U5_9PSEU 
ID   A0A0M4R1U5_9PSEU        Unreviewed;       108 AA.
AC   A0A0M4R1U5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Transcriptional regulator WhiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN   Name=whiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN   ORFNames=WY02_22545 {ECO:0000313|EMBL:ALE80726.1};
OS   Pseudonocardia sp. AL041005-10.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE80726.1, ECO:0000313|Proteomes:UP000067245};
RN   [1] {ECO:0000313|EMBL:ALE80726.1, ECO:0000313|Proteomes:UP000067245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE80726.1,
RC   ECO:0000313|Proteomes:UP000067245};
RX   PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA   Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT   "Variable genetic architectures produce virtually identical molecules in
RT   bacterial symbionts of fungus-growing ants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
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 of
CC       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|ARBA:ARBA00004496,
CC       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|ARBA:ARBA00006597,
CC       ECO:0000256|HAMAP-Rule:MF_01479}.
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DR   EMBL; CP011862; ALE80726.1; -; Genomic_DNA.
DR   RefSeq; WP_060710891.1; NZ_CP011862.1.
DR   AlphaFoldDB; A0A0M4R1U5; -.
DR   STRING; 445576.WY02_22545; -.
DR   KEGG; psea:WY02_22545; -.
DR   PATRIC; fig|445576.3.peg.4930; -.
DR   OrthoDB; 4954884at2; -.
DR   Proteomes; UP000067245; 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 DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01479; WhiB; 1.
DR   InterPro; IPR034768; 4FE4S_WBL.
DR   InterPro; IPR003482; Whib.
DR   PANTHER; PTHR38839:SF5; TRANSCRIPTIONAL REGULATOR WHID; 1.
DR   PANTHER; PTHR38839; TRANSCRIPTIONAL REGULATOR WHID-RELATED; 1.
DR   Pfam; PF02467; Whib; 1.
DR   PROSITE; PS51674; 4FE4S_WBL; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01479};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01479};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_01479};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01479};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01479};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_01479};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01479};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01479};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01479}.
FT   DOMAIN          22..86
FT                   /note="4Fe-4S Wbl-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51674"
FT   BINDING         23
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         56
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         62
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
SQ   SEQUENCE   108 AA;  12139 MW;  B784ECF7914E1695 CRC64;
     MSDVSRLPGP MDDVWQWQRL GACRGMDSAV FFHPDGERNP SRSRRTERAK QVCRGCPVLQ
     ECRRFALASR EPFGVWGGLG ESERRAIIER RDAERIVAEQ GPGLAAVV
//
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