ID A0A1I2HHA2_9MICO Unreviewed; 107 AA.
AC A0A1I2HHA2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Transcriptional regulator WhiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN Name=whiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN ORFNames=SAMN04488035_2328 {ECO:0000313|EMBL:SFF28803.1};
OS Flavimobilis marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC Flavimobilis.
OX NCBI_TaxID=285351 {ECO:0000313|EMBL:SFF28803.1, ECO:0000313|Proteomes:UP000198520};
RN [1] {ECO:0000313|Proteomes:UP000198520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19083 {ECO:0000313|Proteomes:UP000198520};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FONZ01000004; SFF28803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2HHA2; -.
DR STRING; 285351.SAMN04488035_2328; -.
DR OrthoDB; 5192305at2; -.
DR Proteomes; UP000198520; Unassembled WGS sequence.
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:SF4; TRANSCRIPTIONAL REGULATOR WHIB; 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:UP000198520};
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 44..101
FT /note="4Fe-4S Wbl-type"
FT /evidence="ECO:0000259|PROSITE:PS51674"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
SQ SEQUENCE 107 AA; 11928 MW; 3BFA5CB72D20939D CRC64;
MWNLLDDDGA FPSDVSRPVD GVAAVLPLFG EDAETAMSWQ ERALCAQTDP EAFFPEKGGS
TREAKKVCTS CDVRSECLEY ALANDERFGI WGGLSERERR KLKRQVV
//
