GenomeNet

Database: UniProt
Entry: R7WWT8_9NOCA
LinkDB: R7WWT8_9NOCA
Original site: R7WWT8_9NOCA 
ID   R7WWT8_9NOCA            Unreviewed;        91 AA.
AC   R7WWT8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Transcriptional regulator WhiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN   Name=whiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN   ORFNames=Rrhod_0003 {ECO:0000313|EMBL:EOM78614.1};
OS   Rhodococcus rhodnii LMG 5362.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM78614.1, ECO:0000313|Proteomes:UP000013525};
RN   [1] {ECO:0000313|EMBL:EOM78614.1, ECO:0000313|Proteomes:UP000013525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM78614.1,
RC   ECO:0000313|Proteomes:UP000013525};
RX   PubMed=23788540;
RA   Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA   Dyson P.J., Facey P.D.;
RT   "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT   Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT   Vector of Trypanosoma cruzi.";
RL   Genome Announc. 1:e00329-13(2013).
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:EOM78614.1}.
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; APMY01000001; EOM78614.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7WWT8; -.
DR   PATRIC; fig|1273125.3.peg.3; -.
DR   eggNOG; ENOG5032S23; Bacteria.
DR   Proteomes; UP000013525; 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: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:UP000013525};
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          16..80
FT                   /note="4Fe-4S Wbl-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51674"
FT   BINDING         17
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         47
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         50
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"
SQ   SEQUENCE   91 AA;  10452 MW;  88E220409D062D62 CRC64;
     MPGPNADVWD WQMHGLCRGV DSAMFFHPDG ERGRARAQRE SRAKEMCRQC PVLTQCRTHA
     LAVAEPYGIW GGMSETEREM YARQRRSRIA V
//
DBGET integrated database retrieval system