ISCR_SALPA
ID ISCR_SALPA Reviewed; 164 AA.
AC Q5PNG2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=HTH-type transcriptional regulator IscR {ECO:0000255|HAMAP-Rule:MF_01176};
GN Name=iscR {ECO:0000255|HAMAP-Rule:MF_01176}; OrderedLocusNames=SPA0322;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
CC -!- FUNCTION: Regulates the transcription of several operons and genes
CC involved in the biogenesis of Fe-S clusters and Fe-S-containing
CC proteins. {ECO:0000255|HAMAP-Rule:MF_01176}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01176};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_01176};
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DR EMBL; CP000026; AAV76341.1; -; Genomic_DNA.
DR RefSeq; WP_001241346.1; NC_006511.1.
DR AlphaFoldDB; Q5PNG2; -.
DR SMR; Q5PNG2; -.
DR EnsemblBacteria; AAV76341; AAV76341; SPA0322.
DR KEGG; spt:SPA0322; -.
DR HOGENOM; CLU_107144_0_0_6; -.
DR OMA; YGLTIMM; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_01176; HTH_type_IscR; 1.
DR InterPro; IPR010242; TF_HTH_IscR.
DR InterPro; IPR030489; TR_Rrf2-type_CS.
DR InterPro; IPR000944; Tscrpt_reg_Rrf2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR33221; PTHR33221; 1.
DR Pfam; PF02082; Rrf2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR TIGRFAMs; TIGR02010; IscR; 1.
DR TIGRFAMs; TIGR00738; rrf2_super; 1.
DR PROSITE; PS01332; HTH_RRF2_1; 1.
DR PROSITE; PS51197; HTH_RRF2_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Activator; DNA-binding; Iron; Iron-sulfur; Metal-binding;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..164
FT /note="HTH-type transcriptional regulator IscR"
FT /id="PRO_0000268923"
FT DOMAIN 2..131
FT /note="HTH rrf2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01176"
FT DNA_BIND 28..51
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01176"
FT BINDING 92
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01176"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01176"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01176"
SQ SEQUENCE 164 AA; 17391 MW; D35A11F77F5FF5A3 CRC64;
MRLTSKGRYA VTAMLDVALN SEAGPVPLAD ISERQGISLS YLEQLFSRLR KNGLVSSVRG
PGGGYLLGKD AGSIAVGEVI SAVDESVDAT RCQGKGGCQG GDKCLTHALW RDLSDRLTGF
LNNITLGELV NNQEVLDVSG RQHTHDAPRA SGRAQDAIDV KLRA
