ID   NIFA_AZOBR     STANDARD;      PRT;   625 AA.
AC   P30667;
DT   01-APR-1993 (Rel. 25, Created)
DT   01-APR-1993 (Rel. 25, Last sequence update)
DT   05-JUL-2004 (Rel. 44, Last annotation update)
DE   Nif-specific regulatory protein.
GN   Name=nifA;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sp7 / ATCC 29145;
RX   MEDLINE=92140038; PubMed=1779763;
RA   Liang Y.Y., Kaminski P.A., Elmerich C.;
RT   "Identification of a nifA-like regulatory gene of Azospirillum
RT   brasilense Sp7 expressed under conditions of nitrogen fixation and in
RT   the presence of air and ammonia.";
RL   Mol. Microbiol. 5:2735-2744(1991).
RN   [2]
RP   CHARACTERIZATION.
RX   MEDLINE=93122522; PubMed=1362170;
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.
CC   -!- SIMILARITY: Contains 1 sigma-54 factor interaction ATP-binding
CC       domain.
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CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
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DR   EMBL; X60714; CAA43126.1; -.
DR   PIR; S18420; S18420.
DR   InterPro; IPR003593; AAA_ATPase.
DR   InterPro; IPR008931; FIS-like.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR002197; HTH_Fis.
DR   InterPro; IPR010113; NifA.
DR   InterPro; IPR002078; Sig54_interact.
DR   Pfam; PF01590; GAF; 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   TIGRFAMs; TIGR01199; HTH_fis; 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.
KW   Activator; ATP-binding; DNA-binding; Nitrogen fixation;
KW   Transcription regulation; Two-component regulatory system.
FT   DOMAIN      205    433       Sigma-54 factor interaction (Potential).
FT   DOMAIN      434    582       Inter-domain linker.
FT   DOMAIN      583    625       C-terminal DNA-binding domain.
FT   NP_BIND     233    240       ATP (Potential).
FT   NP_BIND     296    305       ATP (Potential).
FT   METAL       447    447       By similarity.
FT   METAL       452    452       By similarity.
FT   DNA_BIND    597    616       H-T-H motif (By similarity).
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
//