RP54_KLEOX
ID RP54_KLEOX Reviewed; 477 AA.
AC P06223;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=RNA polymerase sigma-54 factor;
GN Name=rpoN; Synonyms=ntrA;
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2999700; DOI=10.1093/nar/13.21.7607;
RA Merrick M.J., Gibbins J.R.;
RT "The nucleotide sequence of the nitrogen-regulation gene ntrA of Klebsiella
RT pneumoniae and comparison with conserved features in bacterial RNA
RT polymerase sigma factors.";
RL Nucleic Acids Res. 13:7607-7620(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 465-477.
RC STRAIN=M5a1;
RX PubMed=2695747; DOI=10.1111/j.1365-2958.1989.tb00162.x;
RA Merrick M.J., Coppard J.R.;
RT "Mutations in genes downstream of the rpoN gene (encoding sigma 54) of
RT Klebsiella pneumoniae affect expression from sigma 54-dependent
RT promoters.";
RL Mol. Microbiol. 3:1765-1775(1989).
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; X03147; CAA26925.1; -; Genomic_DNA.
DR EMBL; X16335; CAA34390.1; -; Genomic_DNA.
DR PIR; A24115; A24115.
DR RefSeq; WP_049087000.1; NZ_QPKC01000013.1.
DR PDB; 5NSR; EM; 3.80 A; M=1-477.
DR PDB; 5NSS; EM; 5.80 A; M=1-477.
DR PDB; 6GFW; EM; 3.70 A; M=1-477.
DR PDB; 6GH5; EM; 3.40 A; M=1-477.
DR PDB; 6GH6; EM; 4.10 A; M=1-477.
DR PDBsum; 5NSR; -.
DR PDBsum; 5NSS; -.
DR PDBsum; 6GFW; -.
DR PDBsum; 6GH5; -.
DR PDBsum; 6GH6; -.
DR AlphaFoldDB; P06223; -.
DR SMR; P06223; -.
DR STRING; 571.MC52_05295; -.
DR GeneID; 64335458; -.
DR eggNOG; COG1508; Bacteria.
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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; DNA-directed RNA polymerase; Nitrogen fixation;
KW Nucleotidyltransferase; Sigma factor; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..477
FT /note="RNA polymerase sigma-54 factor"
FT /id="PRO_0000205533"
FT DNA_BIND 366..385
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 44..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 454..462
FT /note="RPON box"
FT COMPBIAS 48..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:6GH5"
FT TURN 225..230
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 244..254
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 322..354
FT /evidence="ECO:0007829|PDB:6GH5"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 416..429
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:6GH5"
FT HELIX 457..463
FT /evidence="ECO:0007829|PDB:6GH5"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:6GH5"
SQ SEQUENCE 477 AA; 53927 MW; 481F29B66B3DCF9A CRC64;
MKQGLQLRLS QQLAMTPQLQ QAIRLLQLST LELQQELQQA LDSNPLLEQT DLHDEVETKE
AEDRESLDTV DALEQKEMPE ELPLDASWDE IYTAGTPSGN GVDYQDDELP VYQGETTQSL
QDYLMWQVEL TPFTDTDRAI ATSIVDAVDD TGYLTISVED IVESIGDDEI GLEEVEAVLK
RIQRFDPVGV AAKDLRDCLL VQLSQFAKET PWIEEARLII SDHLDLLANH DFRSLMRVTR
LKEEVLKEAV NLIQSLDPRP GQSIQTGEPE YVIPDVLVRK VNDRWVVELN SDSLPRLKIN
QQYAAMGNST RNDADGQFIR SNLQEARWLI KSLESRNDTL LRVSRCIVEQ QQAFFEQGEE
FMKPMVLADI AQAVEMHEST ISRVTTQKYL HSPRGIFELK YFFSSHVNTE GGGEASSTAI
RALVKKLIAA ENPAKPLSDS KLTTMLSDQG IMVARRTVAK YRESLSIPPS NQRKQLV
