ID   NIFA_AZOBR              Reviewed;         625 AA.
AC   P30667;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Nif-specific regulatory protein;
GN   Name=nifA;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=1779763; DOI=10.1111/j.1365-2958.1991.tb01982.x;
RA   Liang Y.Y., Kaminski P.A., Elmerich C.;
RT   "Identification of a nifA-like regulatory gene of Azospirillum brasilense
RT   Sp7 expressed under conditions of nitrogen fixation and in the presence of
RT   air and ammonia.";
RL   Mol. Microbiol. 5:2735-2744(1991).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1362170; DOI=10.1111/j.1574-6968.1992.tb14028.x;
RA   Liang Y.Y., de Zamaroczy M., Arsene F., Paquelin A., Elmerich C.;
RT   "Regulation of nitrogen fixation in Azospirillum brasilense Sp7:
RT   involvement of nifA, glnA and glnB gene products.";
RL   FEMS Microbiol. Lett. 79:113-119(1992).
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; X60714; CAA43126.1; -; Genomic_DNA.
DR   PIR; S18420; S18420.
DR   AlphaFoldDB; P30667; -.
DR   SMR; P30667; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IMP:CACAO.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_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   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; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01817; nifA; 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   1: Evidence at protein level;
KW   Activator; ATP-binding; DNA-binding; Metal-binding; Nitrogen fixation;
KW   Nucleotide-binding; Transcription; Transcription regulation;
KW   Two-component regulatory system.
FT   CHAIN           1..625
FT                   /note="Nif-specific regulatory protein"
FT                   /id="PRO_0000081300"
FT   DOMAIN          29..171
FT                   /note="GAF"
FT   DOMAIN          205..433
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        597..616
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          434..582
FT                   /note="Inter-domain linker"
FT   REGION          478..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          583..625
FT                   /note="C-terminal DNA-binding domain"
FT   COMPBIAS        539..573
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         233..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         296..305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         447
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P05407"
FT   BINDING         452
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P05407"
SQ   SEQUENCE   625 AA;  67855 MW;  D060EA86CB1FECC3 CRC64;
     MPGAMRQSTS NLELLTIYEV SKILGSSLDL QQTLREVLRA LAYQLQMHRG RVYLVGEDNV
     LRLVAANGLS NEAAAQIEFR DGEGITGRIL KTGMPAVVPN LAEEPLFLNR TGGREDLDEQ
     VASLVGVPIK AAGVVVGVLT IDRISDEGPQ GHFGSDVRFL TMVANLIGQT VRLHRTVAEE
     RRFMMRETFR MQKELRPVAA PINDVVCTSP NMLEVMAQVH RVAPFKSTVL IRGESGTGKE
     LIARAIHNMS PRKDAPFIRV NCAALPESLL ESELFGHEKG AFTGAQKDHK GRFELASGGT
     LFLDEIGDIS PNFQAKLLRV LQEQEFERVG GSKTIKTDVR LICATNLNLE EAVGHGKFRA
     DLYFRINVVT IHLPPLRERR QDIGPLARHF VAKFAKDNGM ALVMEDEALE VLNRCTWPGN
     VRELENCIER AATQSRDGII RTESLSCSLN LCNSSVLFQY RTLGASVGGL APSMGPGAIN
     RVPPGRPGGP AAANAPKTPA MPAPVPEPAG AAAARGRPAR RVVPRPLAGL RRRPAGGSGP
     PDPACPCPSR APLPPQAPPP SPAAAPPPAA EVPLDEPESG SLRDRLLWAM ERTGWVQAKA
     ARLLGMTTRQ VSYALRKYNI EIKRF