ID   RP54_CERSP              Reviewed;         434 AA.
AC   Q01194;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=RNA polymerase sigma-54 factor;
GN   Name=rpoN;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1317839; DOI=10.1128/jb.174.12.3855-3866.1992;
RA   Meijer W.G., Tabita F.R.;
RT   "Isolation and characterization of the nifUSVW-rpoN gene cluster from
RT   Rhodobacter sphaeroides.";
RL   J. Bacteriol. 174:3855-3866(1992).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released. This sigma factor is responsible for the expression of the
CC       nitrogen fixation genes. The open complex (sigma-54 and core RNA
CC       polymerase) serves as the receptor for receipt of the melting signal
CC       from the remotely bound activator protein NifA for the expression of
CC       the nitrogen fixation proteins.
CC   -!- SIMILARITY: Belongs to the sigma-54 factor family. {ECO:0000305}.
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DR   EMBL; M86823; AAA26134.1; -; Genomic_DNA.
DR   PIR; F41880; F41880.
DR   RefSeq; WP_011338295.1; NZ_WSNV01000150.1.
DR   AlphaFoldDB; Q01194; -.
DR   SMR; Q01194; -.
DR   OrthoDB; 1906842at2; -.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; IEA:InterPro.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016987; F:sigma factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1330; -; 1.
DR   InterPro; IPR000394; RNA_pol_sigma_54.
DR   InterPro; IPR007046; RNA_pol_sigma_54_core-bd.
DR   InterPro; IPR007634; RNA_pol_sigma_54_DNA-bd.
DR   InterPro; IPR038709; RpoN_core-bd_sf.
DR   PANTHER; PTHR32248; PTHR32248; 1.
DR   Pfam; PF00309; Sigma54_AID; 1.
DR   Pfam; PF04963; Sigma54_CBD; 1.
DR   Pfam; PF04552; Sigma54_DBD; 1.
DR   PIRSF; PIRSF000774; RpoN; 1.
DR   PRINTS; PR00045; SIGMA54FCT.
DR   TIGRFAMs; TIGR02395; rpoN_sigma; 1.
DR   PROSITE; PS00717; SIGMA54_1; 1.
DR   PROSITE; PS00718; SIGMA54_2; 1.
DR   PROSITE; PS50044; SIGMA54_3; 1.
PE   3: Inferred from homology;
KW   DNA-binding; DNA-directed RNA polymerase; Nitrogen fixation;
KW   Nucleotidyltransferase; Sigma factor; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..434
FT                   /note="RNA polymerase sigma-54 factor"
FT                   /id="PRO_0000205542"
FT   DNA_BIND        319..338
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   MOTIF           408..416
FT                   /note="RPON box"
SQ   SEQUENCE   434 AA;  47871 MW;  B6346BD3E3513F66 CRC64;
     MDMMQFQRQT TQLAMTQRMQ ESLRILQMSN ADLADYLTAQ ALENPCLEVR VPEGASVAPA
     LPSRGIQAGL DRDAFATVEG QPPSLLAHVE AQIDLAFFDP GDRRTALAFA EALEPSGWLG
     QPVSEVAAAA EVEEEEALVI LERLQALEPA GLFARSLAEC LALQLEDLGL LTWELRTMLD
     HLPLLAEGRI ADLARRCDCE PEHIRENLAL IRSLSPKPGE AFAADRTPIQ PPDVRVLRGP
     EGWEVELTRA QLPRIRVSEA GDTGDRQADA WLARARSQAR WLERAVERRQ ATLLRTAVCL
     VRHQADFLDQ GPRALRPLSM EEVALELDLH PSTISRATAT RLIETPRGLI PLRAFFSRSV
     SSDGPEAPQS QDALMALVRE IIAREDRTKP FSDDAIVKQA KLAGAVLARR TVTKYRETLG
     IPSSYDRKRA AAAA