ID D7AZU6_NOCDD Unreviewed; 99 AA.
AC D7AZU6;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Transcriptional regulator WhiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN Name=whiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN OrderedLocusNames=Ndas_2805 {ECO:0000313|EMBL:ADH68217.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH68217.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH68217.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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}.
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; CP002040; ADH68217.1; -; Genomic_DNA.
DR AlphaFoldDB; D7AZU6; -.
DR STRING; 446468.Ndas_2805; -.
DR KEGG; nda:Ndas_2805; -.
DR eggNOG; ENOG5032S23; Bacteria.
DR HOGENOM; CLU_106245_6_1_11; -.
DR Proteomes; UP000002219; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002219};
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 23..87
FT /note="4Fe-4S Wbl-type"
FT /evidence="ECO:0000259|PROSITE:PS51674"
FT REGION 77..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
SQ SEQUENCE 99 AA; 11513 MW; 88DB4BFC2F217F9E CRC64;
MSQVRRQAAL RPRPHWGWQD AAACRGEDLV LFFGPDGERQ PEREIRERKA KEICAACPVR
NDCLDYAISR PEKYGTWGGL NEDERASERR RRMRRANAA
//