NSRR_VIBPA
ID NSRR_VIBPA Reviewed; 141 AA.
AC P40610;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=HTH-type transcriptional repressor NsrR {ECO:0000255|HAMAP-Rule:MF_01177};
GN Name=nsrR {ECO:0000255|HAMAP-Rule:MF_01177}; Synonyms=yjeB;
GN OrderedLocusNames=VP2808;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB22;
RA McCarter L.L.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; U09005; AAA62191.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC61071.1; -; Genomic_DNA.
DR RefSeq; NP_799187.1; NC_004603.1.
DR RefSeq; WP_005460673.1; NC_004603.1.
DR AlphaFoldDB; P40610; -.
DR SMR; P40610; -.
DR STRING; 223926.28807818; -.
DR EnsemblBacteria; BAC61071; BAC61071; BAC61071.
DR GeneID; 1190358; -.
DR KEGG; vpa:VP2808; -.
DR PATRIC; fig|223926.6.peg.2700; -.
DR eggNOG; COG1959; Bacteria.
DR HOGENOM; CLU_107144_2_0_6; -.
DR OMA; AQEAFYA; -.
DR Proteomes; UP000002493; Chromosome 1.
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; IPR030489; TR_Rrf2-type_CS.
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; PS01332; HTH_RRF2_1; 1.
DR PROSITE; PS51197; HTH_RRF2_2; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; DNA-binding; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..141
FT /note="HTH-type transcriptional repressor NsrR"
FT /id="PRO_0000109559"
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; 15557 MW; B6E43A88E07DE053 CRC64;
MQLTSFTDYA LRTLIYLASL PKDELTNITE VTDLFGVSRN HMVKVINRLG QLGYVHTVRG
KNGGIRLMKP ASEITVGGVV RDLEPLDLVN CGVEFCHITP ACRLKDKLAK AKSAFLAELD
ECTIESLLSD NSELLILLAR P