ID   NSRR_SALPA              Reviewed;         141 AA.
AC   Q5PL57;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=HTH-type transcriptional repressor NsrR {ECO:0000255|HAMAP-Rule:MF_01177};
GN   Name=nsrR {ECO:0000255|HAMAP-Rule:MF_01177}; OrderedLocusNames=SPA4184;
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: Nitric oxide-sensitive repressor of genes involved in
CC       protecting the cell against nitrosative stress. May require iron for
CC       activity. {ECO:0000255|HAMAP-Rule:MF_01177}.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01177};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01177};
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DR   EMBL; CP000026; AAV79921.1; -; Genomic_DNA.
DR   RefSeq; WP_001177632.1; NC_006511.1.
DR   AlphaFoldDB; Q5PL57; -.
DR   SMR; Q5PL57; -.
DR   EnsemblBacteria; AAV79921; AAV79921; SPA4184.
DR   KEGG; spt:SPA4184; -.
DR   HOGENOM; CLU_107144_2_1_6; -.
DR   OMA; AQEAFYA; -.
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   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_01177; HTH_type_NsrR; 1.
DR   InterPro; IPR000944; Tscrpt_reg_Rrf2.
DR   InterPro; IPR023761; Tscrpt_rep_HTH_NsrR.
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; TIGR00738; rrf2_super; 1.
DR   PROSITE; PS51197; HTH_RRF2_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; DNA-binding; Iron; Iron-sulfur; Metal-binding; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..141
FT                   /note="HTH-type transcriptional repressor NsrR"
FT                   /id="PRO_0000268945"
FT   DOMAIN          2..129
FT                   /note="HTH rrf2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01177"
FT   DNA_BIND        28..51
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01177"
FT   BINDING         91
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01177"
FT   BINDING         96
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01177"
FT   BINDING         102
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01177"
SQ   SEQUENCE   141 AA;  15608 MW;  ABC9A219C1E81BCC CRC64;
     MQLTSFTDYG LRALIYMASL PDGRMTSISE VTEVYGVSRN HMVKIINQLS RAGFVTAVRG
     KNGGIRLGKP ANTICIGDVV RELEPLSLVN CSSEFCHITP ACRLKQALSK AVQSFLKELD
     NYTLADLVEE NQPLYKLLLV E