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Database: UniProt
Entry: G9PHL4_9ACTO
LinkDB: G9PHL4_9ACTO
Original site: G9PHL4_9ACTO 
ID   G9PHL4_9ACTO            Unreviewed;        84 AA.
AC   G9PHL4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Transcriptional regulator WhiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN   Name=whiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN   ORFNames=HMPREF0045_01742 {ECO:0000313|EMBL:EHM87363.1};
OS   Actinomyces graevenitzii C83.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=435830 {ECO:0000313|EMBL:EHM87363.1, ECO:0000313|Proteomes:UP000003822};
RN   [1] {ECO:0000313|EMBL:EHM87363.1, ECO:0000313|Proteomes:UP000003822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C83 {ECO:0000313|EMBL:EHM87363.1,
RC   ECO:0000313|Proteomes:UP000003822};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA   Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Actinomyces graevenitzii C83.";
RL   Submitted (OCT-2011) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHM87363.1}.
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DR   EMBL; ACRN01000015; EHM87363.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9PHL4; -.
DR   STRING; 435830.HMPREF0045_01742; -.
DR   PATRIC; fig|435830.3.peg.1676; -.
DR   eggNOG; ENOG5032RSG; Bacteria.
DR   HOGENOM; CLU_106245_6_2_11; -.
DR   Proteomes; UP000003822; 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:SF6; TRANSCRIPTIONAL REGULATOR WHIB1; 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:UP000003822};
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          10..72
FT                   /note="4Fe-4S Wbl-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51674"
FT   REGION          64..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         39
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         42
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
SQ   SEQUENCE   84 AA;  9227 MW;  E0C9384A62A9FA46 CRC64;
     MSMDWRERAA CLNADPELFF PVGNTGPAIA QIAEAKTVCR SCSVVDVCLK WALDNGQDAG
     VWGGMSEDER RSLKRRAARA RRSA
//
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