NIFA_SINFN
ID NIFA_SINFN Reviewed; 594 AA.
AC Q53206;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Nif-specific regulatory protein;
GN Name=nifA; OrderedLocusNames=NGR_a01260; ORFNames=y4uN;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8796346; DOI=10.1101/gr.6.7.590;
RA Freiberg C., Perret X., Broughton W.J., Rosenthal A.;
RT "Sequencing the 500-kb GC-rich symbiotic replicon of Rhizobium sp. NGR234
RT using dye terminators and a thermostable 'sequenase': a beginning.";
RL Genome Res. 6:590-600(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- FUNCTION: Required for activation of most nif operons, which are
CC directly involved in nitrogen fixation.
CC -!- SUBUNIT: Interacts with sigma-54.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA92413.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z68203; CAA92413.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00090; AAB91886.1; -; Genomic_DNA.
DR RefSeq; NP_444099.1; NC_000914.2.
DR RefSeq; WP_010875164.1; NC_000914.2.
DR AlphaFoldDB; Q53206; -.
DR SMR; Q53206; -.
DR STRING; 394.NGR_a01260; -.
DR EnsemblBacteria; AAB91886; AAB91886; NGR_a01260.
DR KEGG; rhi:NGR_a01260; -.
DR PATRIC; fig|394.7.peg.110; -.
DR eggNOG; COG3604; Bacteria.
DR HOGENOM; CLU_000445_95_2_5; -.
DR OMA; RCKFPGN; -.
DR OrthoDB; 123059at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
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 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; 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 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 4: Predicted;
KW Activator; ATP-binding; DNA-binding; Metal-binding; Nitrogen fixation;
KW Nucleotide-binding; Plasmid; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..594
FT /note="Nif-specific regulatory protein"
FT /id="PRO_0000081314"
FT DOMAIN 69..210
FT /note="GAF"
FT DOMAIN 252..480
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 566..585
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 213..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..551
FT /note="Inter-domain linker"
FT REGION 552..594
FT /note="C-terminal DNA-binding domain"
FT BINDING 280..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 343..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 494
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P05407"
FT BINDING 499
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P05407"
SQ SEQUENCE 594 AA; 64886 MW; 576E209DD9130381 CRC64;
MQAQALDNVS KAAFSRREPR AVRTTLKVFP RKNWLDECMT ELSPKTMHKR DLGCSGLYRI
SKVLITSASL EIKLANVINT LPALLPMRRG AIVVVGAEGE PETTATFGVE PPSSGARHIA
AKAAIDRIVA KGAPLVVPDT CKSELFQDEL QSIVSGTGQV TFIGVPMKAD QETLGTLWID
RAKDGAATRT QFEEEVRFLS MVANLAARAV RLNGHESRDS RPIGEEGDRK ISGGDKELPE
PTRQRPTRID WIVGESPALR QVVESVKVVA QTNSAVLLRG ESGTGKEFFA KAIHELSPRR
KKPFVKLNCA ALSAGVLESE LFGHEKGAFT GAISQRAGRF ELADGGTLLL DEIGEISPAF
QAKLLRVLQE GELERVGGTK TLKVDVRLIC ATNKDLETAV AEGEFRADLY YRINVVPLFL
PPLRERNGDI PRLAKVFLDR FNRENNRNLE FTPAALEILS RCKFPGNVRE LENCVRRTAT
LARSATIVPS DFSCQNDQCF SSMLGKTADR PLGSHSLNGL AMSKRLPVES PASLGYPAGP
GGLTVAPHLS DRELLISAME KAGWVQAKAA RILGLTPRQV GYALRRHHIQ VKKI
