GenomeNet

Database: UniProt
Entry: Q8NSD3_CORGL
LinkDB: Q8NSD3_CORGL
Original site: Q8NSD3_CORGL 
ID   Q8NSD3_CORGL            Unreviewed;       136 AA.
AC   Q8NSD3;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=Transcriptional regulator WhiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN   Name=whiB {ECO:0000256|HAMAP-Rule:MF_01479};
GN   OrderedLocusNames=Cgl0743 {ECO:0000313|EMBL:BAB98136.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB98136.1, ECO:0000313|Proteomes:UP000000582};
RN   [1] {ECO:0000313|Proteomes:UP000000582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
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; BA000036; BAB98136.1; -; Genomic_DNA.
DR   RefSeq; NP_599973.1; NC_003450.3.
DR   AlphaFoldDB; Q8NSD3; -.
DR   STRING; 196627.cg0850; -.
DR   KEGG; cgl:Cgl0743; -.
DR   PATRIC; fig|196627.13.peg.729; -.
DR   eggNOG; ENOG5032RUK; Bacteria.
DR   HOGENOM; CLU_106245_4_1_11; -.
DR   OrthoDB; 5192305at2; -.
DR   BioCyc; CORYNE:G18NG-10305-MONOMER; -.
DR   Proteomes; UP000000582; 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: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:UP000000582};
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          73..130
FT                   /note="4Fe-4S Wbl-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51674"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         97
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         100
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
FT   BINDING         106
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01479"
SQ   SEQUENCE   136 AA;  15221 MW;  10168DA204190FF9 CRC64;
     MGEGKIFQTC SGTNIPDENR LKVALKVRGG RVMEDSAGDV SAKLKAGQTR TALEMTLDDL
     FGAVEQEWQE QALCAQTDPE AFFPEKGGST REAKRICQGC PVRDECLEFA LEHDERFGIW
     GGLSERERRR LKREIS
//
DBGET integrated database retrieval system