ID   NODD2_SINFN             Reviewed;         312 AA.
AC   P55700;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Nodulation protein D 2;
GN   Name=nodD2; OrderedLocusNames=NGR_a00810; ORFNames=y4xH;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=9535093; DOI=10.1046/j.1365-2958.1998.00761.x;
RA   Fellay R., Hanin M., Montorzi G., Frey J., Freiberg C., Golinowski W.,
RA   Staehelin C., Broughton W.J., Jabbouri S.;
RT   "nodD2 of Rhizobium sp. NGR234 is involved in the repression of the nodABC
RT   operon.";
RL   Mol. Microbiol. 27:1039-1050(1998).
CC   -!- FUNCTION: Represses the expression of the nodABCIJ-nolO-noeI operon.
CC   -!- INDUCTION: By flavonoids.
CC   -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC       {ECO:0000305}.
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DR   EMBL; U00090; AAB91931.1; -; Genomic_DNA.
DR   PIR; T10836; T10836.
DR   RefSeq; NP_444144.1; NC_000914.2.
DR   RefSeq; WP_010875122.1; NC_000914.2.
DR   AlphaFoldDB; P55700; -.
DR   SMR; P55700; -.
DR   STRING; 394.NGR_a00810; -.
DR   EnsemblBacteria; AAB91931; AAB91931; NGR_a00810.
DR   KEGG; rhi:NGR_a00810; -.
DR   PATRIC; fig|394.7.peg.71; -.
DR   eggNOG; COG0583; Bacteria.
DR   HOGENOM; CLU_039613_39_0_5; -.
DR   OMA; CVMRQGH; -.
DR   OrthoDB; 1591366at2; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd08462; PBP2_NodD; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR005119; LysR_subst-bd.
DR   InterPro; IPR037416; NodD_PBP2.
DR   InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00126; HTH_1; 1.
DR   Pfam; PF03466; LysR_substrate; 1.
DR   PRINTS; PR00039; HTHLYSR.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50931; HTH_LYSR; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nodulation; Plasmid; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..312
FT                   /note="Nodulation protein D 2"
FT                   /id="PRO_0000105722"
FT   DOMAIN          6..63
FT                   /note="HTH lysR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT   DNA_BIND        23..42
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
SQ   SEQUENCE   312 AA;  35283 MW;  2AB326A3B042789F CRC64;
     MRFKGLDLNL LVALDALMTK RSVTAAARSI NLSQPAMSAA IARLRTYFGD DLFTMRGREL
     IPTPRAIALA PAVRDALLHI QFSIISWDMF NPVQSERRFR IRLSDVMMLV FFERVVKRLA
     REAPGIGFEL LPLTEDPDEL LRYGDVDFVI LPELFASSDH PKAKLLDDTL VCVGCPTNKQ
     LKRQLSFENY GSMGHIAAKF GRTLKPSIEN WLLLEHGLKR RIEVVVPGFS LIPPLLSGTD
     RIATMPLRLV EHFAKTTPLR VAELPLALPP FAQAVQWPSL HNRDQASIWM RQVLLQEALH
     MTAPRDSVEY RP