NIFA_KLEOX
ID NIFA_KLEOX Reviewed; 524 AA.
AC P56266;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Nif-specific regulatory protein;
GN Name=nifA;
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NG13;
RX PubMed=3027503; DOI=10.1007/bf00430436;
RA Kim Y.-M., Ahn K.-J., Beppu T., Uozumi T.;
RT "Nucleotide sequence of the nifLA operon of Klebsiella oxytoca NG13 and
RT characterization of the gene products.";
RL Mol. Gen. Genet. 205:253-259(1986).
CC -!- FUNCTION: Required for activation of most nif operons, which are
CC directly involved in nitrogen fixation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with sigma-54. {ECO:0000250}.
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DR EMBL; D00339; BAA00245.1; -; Genomic_DNA.
DR RefSeq; WP_004122422.1; NZ_CABGYY010000023.1.
DR AlphaFoldDB; P56266; -.
DR SMR; P56266; -.
DR STRING; 571.MC52_26865; -.
DR eggNOG; COG3604; Bacteria.
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 3: Inferred from homology;
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_0000081308"
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; 58650 MW; E0677A3605E6F9EE CRC64;
MIHKSDSDTT VRRFDLSQQF TAMQRISVVL SRATEASKTL QEVLSVLHND AFMQHGMICL
YDSQQEILSI EALQQTENQT LPGSTQIRYR PGEGLVGTVL AQGQSLVLPR VADDQRFLDR
LSLYDYDLPF IAVPLMGPHS RPIGVLAAQP MARQEERLPA CTRFLETVAN LIAQTIRLMI
LPTSAAQPPQ QSPRVERPRA CTSSRGFGLE 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