ID   RP54_ACIGI              Reviewed;         482 AA.
AC   P33983;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=RNA polymerase sigma-54 factor;
GN   Name=rpoN; Synonyms=ntrA;
OS   Acinetobacter guillouiae (Acinetobacter genomosp. 11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=106649;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11171 / DSM 590 / CCUG 2491 / LMG 988 / NCIMB 8250 / CIP 63.46
RC   / B94;
RX   PubMed=8206826; DOI=10.1128/jb.176.12.3493-3499.1994;
RA   Ehrt S., Ornston L.N., Hillen W.;
RT   "RpoN (sigma 54) is required for conversion of phenol to catechol in
RT   Acinetobacter calcoaceticus.";
RL   J. Bacteriol. 176:3493-3499(1994).
CC   -!- FUNCTION: Sigma factors are initiation factors that promote the
CC       attachment of RNA polymerase to specific initiation sites and are then
CC       released.
CC   -!- SIMILARITY: Belongs to the sigma-54 factor family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA21615.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L26051; AAA21615.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004723732.1; NZ_VZOG01000042.1.
DR   AlphaFoldDB; P33983; -.
DR   SMR; P33983; -.
DR   STRING; 106649.GCA_000829655_01554; -.
DR   PRIDE; P33983; -.
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   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; Nucleotidyltransferase;
KW   Sigma factor; Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..482
FT                   /note="RNA polymerase sigma-54 factor"
FT                   /id="PRO_0000205520"
FT   DNA_BIND        371..390
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   REGION          50..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           459..467
FT                   /note="RPON box"
FT   COMPBIAS        50..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   482 AA;  54901 MW;  A3BD6E1C51F823E0 CRC64;
     MKLSVGLKVA NSLSLTPQLQ QAIRLLQLSS LELEQEIQIQ LDSNPLLEKV EEETHESPEN
     VKQEQQEYEL SDSLNANHLP DELPVDTDWD DVYTHQSTAM ERPEFEDRED NRHSEASLKE
     HMLGQVNLLH FSPVDKLIAY CIVDALDEKG FLAADIEEIV SSVQHLLQQM DYDIEVEEDE
     VLVVLKHIQR LEPIGIGARS LAECLFVQIE ALATTTLFRK EALMLLKHYE LLVSNDLNKL
     IKQTGLNAEL LKSAIDLLKT LKPYPGAEFE QKESDYQIPD VMVSKKNDHW YVQLNPDILP
     KLRINSFYSG MIKRADQSDD NQYLRNQMLE AKNFIKSVDE RHKTLLKVAS CIVQHQREFL
     EIGAEGMKPL VLRDVAEEVE LHESTVSRVT TNKFLLTPRG LFELKYFFSS HVGTTSGGEA
     SSTAIRAKIK KLVADENPRK PLSDNTIANL LKEEGIDVAR RTVAKYRESL HIPSSSDRKV
     LI