ID   NIFA_AZOVI              Reviewed;         522 AA.
AC   P09570;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 138.
DE   RecName: Full=Nif-specific regulatory protein;
GN   Name=nifA;
OS   Azotobacter vinelandii.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=2840552; DOI=10.1111/j.1365-2958.1988.tb00034.x;
RA   Bennet L.T., Cannon F., Dean D.R.;
RT   "Nucleotide sequence and mutagenesis of the nifA gene from Azotobacter
RT   vinelandii.";
RL   Mol. Microbiol. 2:315-321(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 394-522.
RX   PubMed=2450865; DOI=10.1128/jb.170.4.1475-1487.1988;
RA   Joerger R.D., Bishop P.E.;
RT   "Nucleotide sequence and genetic analysis of the nifB-nifQ region from
RT   Azotobacter vinelandii.";
RL   J. Bacteriol. 170:1475-1487(1988).
CC   -!- FUNCTION: Required for activation of most nif operons, which are
CC       directly involved in nitrogen fixation.
CC   -!- SUBUNIT: Interacts with sigma-54.
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DR   EMBL; Y00554; CAA68633.1; -; Genomic_DNA.
DR   EMBL; J03411; AAA22147.1; -; Genomic_DNA.
DR   PIR; S01927; S01927.
DR   AlphaFoldDB; P09570; -.
DR   SMR; P09570; -.
DR   IntAct; P09570; 1.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   FunFam; 3.40.50.300:FF:000006; DNA-binding transcriptional regulator NtrC; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR058031; AAA_lid_NorR.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR009057; Homeodomain-like_sf.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR010113; Nif-specific_regulatory_prot.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002078; Sigma_54_int.
DR   InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR   InterPro; IPR025944; Sigma_54_int_dom_CS.
DR   NCBIfam; TIGR01817; nifA; 1.
DR   PANTHER; PTHR32071:SF117; PTS-DEPENDENT DIHYDROXYACETONE KINASE OPERON REGULATORY PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF25601; AAA_lid_14; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02954; HTH_8; 1.
DR   Pfam; PF00158; Sigma54_activat; 1.
DR   PRINTS; PR01590; HTHFIS.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00065; GAF; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50813; GAF; 1.
DR   PROSITE; PS52089; HTH_NTRC; 1.
DR   PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR   PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR   PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR   PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE   4: Predicted;
KW   Activator; ATP-binding; DNA-binding; Nitrogen fixation; Nucleotide-binding;
KW   Transcription; Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..522
FT                   /note="Nif-specific regulatory protein"
FT                   /id="PRO_0000081304"
FT   DOMAIN          21..179
FT                   /note="GAF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01434"
FT   DOMAIN          211..439
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DOMAIN          469..518
FT                   /note="HTH NtrC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01435"
FT   DNA_BIND        494..517
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01435"
FT   REGION          1..184
FT                   /note="A domain"
FT   REGION          440..479
FT                   /note="Inter-domain linker"
FT   REGION          480..522
FT                   /note="C-terminal DNA-binding domain"
FT   BINDING         239..246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         302..311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
SQ   SEQUENCE   522 AA;  58123 MW;  9556A07EE8A7B209 CRC64;
     MNATIPQRSA KQNPVELYDL QLQALASIAR TLSREQQIDE LLEQVLAVLH NDLGLLHGLV
     TISDPEHGAL QIGAIHTDSE AVAQACEGVR YRSGEGVIGN VLKHGNSVVL GRISADPRFL
     DRLALYDLEM PFIAVPIKNP EGNTIGVLAA QPDCRADEHM PARTRFLEIV ANLLAQTVRL
     VVNIEDGREA ADERDELRRE VRGKYGFENM VVGHTPTMRR VFDQIRRVAK WNSTVLVLGE
     SGTGKELIAS AIHYKSPRAH RPFVRLNCAA LPETLLESEL FGHEKGAFTG AVKQRKGRFE
     QADGGTLFLD EIGEISPMFQ AKLLRVLQEG EFERVGGNQT VRVNVRIVAA TNRDLESEVE
     KGKFREDLYY RLNVMAIRIP PLRERTADIP ELAEFLLGKI GRQQGRPLTV TDSAIRLLMS
     HRWPGNVREL ENCLERSAIM SEDGTITRDV VSLTGVDNES PPLAAPLPEV NLADETLDDR
     ERVIAALEQA GWVQAKAARL LGMTPRQIAY RIQTLNIHMR KI
//