ID   NIFA_KLEPN              Reviewed;         524 AA.
AC   P03027;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Nif-specific regulatory protein;
GN   Name=nifA;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3062178; DOI=10.1016/0022-2836(88)90205-7;
RA   Arnold W., Rump A., Klipp W., Priefer U.B., Puehler A.;
RT   "Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire
RT   nitrogen fixation gene cluster of Klebsiella pneumoniae.";
RL   J. Mol. Biol. 203:715-738(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3011408; DOI=10.1002/j.1460-2075.1986.tb04230.x;
RA   Drummond M., Whitty P., Wootton J.;
RT   "Sequence and domain relationships of ntrC and nifA from Klebsiella
RT   pneumoniae: homologies to other regulatory proteins.";
RL   EMBO J. 5:441-447(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2989799; DOI=10.1093/nar/13.12.4539;
RA   Buikema W.J., Szeto W.W., Lemley P.V., Orme-Johnson W.H., Ausubel F.M.;
RT   "Nitrogen fixation specific regulatory genes of Klebsiella pneumoniae and
RT   Rhizobium meliloti share homology with the general nitrogen regulatory gene
RT   ntrC of K. pneumoniae.";
RL   Nucleic Acids Res. 13:4539-4555(1985).
CC   -!- FUNCTION: Required for activation of most nif operons, which are
CC       directly involved in nitrogen fixation.
CC   -!- SUBUNIT: Interacts with sigma-54.
CC   -!- INTERACTION:
CC       P03027; Q9ZA65: glnK; NbExp=5; IntAct=EBI-8499916, EBI-8499900;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26472.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X13303; CAA31682.1; -; Genomic_DNA.
DR   EMBL; X02616; CAA26472.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X03580; CAA27260.1; -; Genomic_DNA.
DR   PIR; A91060; RGKBAP.
DR   AlphaFoldDB; P03027; -.
DR   SMR; P03027; -.
DR   IntAct; P03027; 1.
DR   MINT; P03027; -.
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: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   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; IPR009057; Homeobox-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   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; SSF46689; SSF46689; 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; Nitrogen fixation; Nucleotide-binding;
KW   Transcription; Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..524
FT                   /note="Nif-specific regulatory protein"
FT                   /id="PRO_0000081309"
FT   DOMAIN          35..176
FT                   /note="GAF"
FT   DOMAIN          212..481
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        496..515
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          1..182
FT                   /note="A domain"
FT   REGION          482..524
FT                   /note="C-terminal DNA-binding domain"
FT   BINDING         240..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         303..312
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
SQ   SEQUENCE   524 AA;  58632 MW;  F35B8511E580E5EB CRC64;
     MIHKSDSDTT VRRFDLSQQF TAMQRISVVL SRATEASKTL QEVLSVLHND AFMQHGMICL
     YDSQQEILSI EALQQTEDQT LPGSTQIRYR PGEGLVGTVL AQGQSLVLPR VADDQRFLDR
     LSLYDYDLPF IAVPLMGPHS RPIGVLAAHA MARQEERLPA CTRFLETVAN LIAQTIRLMI
     LPTSAAQAPQ QSPRIERPRA CTPSRGFGLE NMVGKSPAMR QIMDIIRQVS RWDTTVLVRG
     ESGTGKELIA NAIHHNSPRA AAAFVKFNCA ALPDNLLESE LFGHEKGAFT GAVRQRKGRF
     ELADGGTLFL DEIGESSASF QAKLLRILQE GEMERVGGDE TLRVNVRIIA ATNRHLEEEV
     RLGHFREDLY YRLNVMPIAL PPLRERQEDI AELAHFLVRK IAHSQGRTLR ISDGAIRLLM
     EYSWPGNVRE LENCLERSAV LSESGLIDRD VILFNHRDNP PKALASSGPA EDGWLDNSLD
     ERQRLIAALE KAGWVQAKAA RLLGMTPRQV AYRIQIMDIT MPRL