RP54_ACIFI
ID RP54_ACIFI Reviewed; 475 AA.
AC P24695;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=RNA polymerase sigma-54 factor;
GN Name=rpoN; Synonyms=ntrA;
OS Acidithiobacillus ferridurans.
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1232575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX PubMed=2198257; DOI=10.1128/jb.172.8.4399-4406.1990;
RA Berger D.K., Woods D.R., Rawlings D.E.;
RT "Complementation of Escherichia coli sigma 54 (NtrA)-dependent formate
RT hydrogenlyase activity by a cloned Thiobacillus ferrooxidans ntrA gene.";
RL J. Bacteriol. 172:4399-4406(1990).
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; M58480; AAA27379.1; -; Genomic_DNA.
DR PIR; B37761; B37761.
DR RefSeq; WP_012537552.1; NZ_QKQP01000005.1.
DR AlphaFoldDB; P24695; -.
DR SMR; P24695; -.
DR STRING; 380394.Lferr_2633; -.
DR OMA; VTTQKFM; -.
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..475
FT /note="RNA polymerase sigma-54 factor"
FT /id="PRO_0000205544"
FT DNA_BIND 365..384
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 453..461
FT /note="RPON box"
SQ SEQUENCE 475 AA; 52928 MW; B7B000DB08696305 CRC64;
MKQGLELKLG QHLAMTPQLQ QAIRLLQLST VDLQQEVQGM LESNPLLDEE TGDEGGGGPI
PETVELPSEE RQLDLAAENI LPDELPVDSQ WDDIFDMGTS GSGNGSDEDL PDFESRNSRT
QSLQDYLRWQ ADMTHFTADE RNMAELIIDA IDERGYLADS LEDLAATMNV QEDALLAVLL
RVQDFDPPGV GARNLSECLL LQLKQMVEKD DAHVLLAQRI VKDHLQALGR HDYPRLCTVL
GVDEAALRAA MALISALNPK PGEDVGTEST EYVIPDVIVR WAGSRLRTDL NPEAMPKLRI
NRHYADMAGG KDAAHKYIQD QLNEARWFIK SLQSRQDTIL KVARAIVERQ KDFFANGPES
MRPMVLRHIA DAVEMHESTV SRVTNQKYMI TPRGLYEFKY FFSSHVGTDS GGSASATAIR
ALLIKMTQAE DAQHPLSDAE IARVLADQGI QIARRTVAKY REAANVPPAS QRRRL
