GenomeNet

Database: UniProt
Entry: NIFA_AZOC5
LinkDB: NIFA_AZOC5
Original site: NIFA_AZOC5 
ID   NIFA_AZOC5              Reviewed;         615 AA.
AC   P09133; A8HQP2;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Nif-specific regulatory protein;
GN   Name=nifA; OrderedLocusNames=AZC_1049;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2664425; DOI=10.1111/j.1365-2958.1989.tb00231.x;
RA   Ratet P., Pawlowski K., Schell J., de Bruijn F.J.;
RT   "The Azorhizobium caulinodans nitrogen-fixation regulatory gene, nifA, is
RT   controlled by the cellular nitrogen and oxygen status.";
RL   Mol. Microbiol. 3:825-838(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3186446; DOI=10.1093/nar/16.20.9839;
RA   Nees D.W., Stein P.A., Ludwig R.A.;
RT   "The Azorhizobium caulinodans nifA gene: identification of upstream-
RT   activating sequences including a new element, the 'anaerobox'.";
RL   Nucleic Acids Res. 16:9839-9853(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC   13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for activation of most nif operons, which are
CC       directly involved in nitrogen fixation.
CC   -!- SUBUNIT: Interacts with sigma-54.
CC   -!- INDUCTION: NifA transcriptional activity seems to be controlled by both
CC       the general nitrogen regulatory (ntr) system and the O(2)-regulatory
CC       (FNR) system.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA30816.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA32837.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X14716; CAA32836.1; -; Genomic_DNA.
DR   EMBL; X14716; CAA32837.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X08014; CAA30816.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP009384; BAF87047.1; -; Genomic_DNA.
DR   PIR; S06977; S06977.
DR   AlphaFoldDB; P09133; -.
DR   SMR; P09133; -.
DR   STRING; 438753.AZC_1049; -.
DR   KEGG; azc:AZC_1049; -.
DR   eggNOG; COG3604; Bacteria.
DR   HOGENOM; CLU_000445_95_2_5; -.
DR   Proteomes; UP000000270; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01817; nifA; 1.
DR   PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR32071:SF95; TRANSCRIPTIONAL REGULATORY PROTEIN ZRAR; 1.
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; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   2: Evidence at transcript level;
KW   Activator; ATP-binding; DNA-binding; Metal-binding; Nitrogen fixation;
KW   Nucleotide-binding; Reference proteome; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..615
FT                   /note="Nif-specific regulatory protein"
FT                   /id="PRO_0000081301"
FT   DOMAIN          68..210
FT                   /note="GAF"
FT   DOMAIN          256..484
FT                   /note="Sigma-54 factor interaction"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   DNA_BIND        587..606
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000250"
FT   REGION          485..572
FT                   /note="Inter-domain linker"
FT   REGION          573..615
FT                   /note="C-terminal DNA-binding domain"
FT   BINDING         284..291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         347..356
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT   BINDING         498
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P05407"
FT   BINDING         503
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P05407"
SQ   SEQUENCE   615 AA;  66794 MW;  3F1CF9D5F5A7B89E CRC64;
     MPMTDAFQVR VPRVSSSTAG DIAASSITTR GALPRPGGMP VSMSRGTSPE VALIGVYEIS
     KILTAPRRLE VTLANVVNVL SSMLQMRHGM ICILDSEGDP DMVATTGWTP EMAGQIRAHV
     PQKAIDQIVA TQMPLVVQDV TADPLFAGHE DLFGPPEEAT VSFIGVPIKA DHHVMGTLSI
     DRIWDGTARF RFDEDVRFLT MVANLVGQTV RLHKLVASDR DRLIAQTHRL EKALREEKSG
     AEPEVAEAAN GSAMGIVGDS PLVKRLIATA QVVARSNSTV LLRGESGTGK ELFARAIHEL
     SPRKGKPFVK VNCAALPESV LESELFGHEK GAFTGALNMR QGRFELAHGG TLFLDEIGEI
     TPAFQAKLLR VLQEGEFERV GGNRTLKVDV RLVCATNKNL EEAVSKGEFR ADLYYRIHVV
     PLILPPLRER PGDIPKLAKN FLDRFNKENK LHMMLSAPAI DVLRRCYFPG NVRELENCIR
     RTATLAHDAV ITPHDFACDS GQCLSAMLWK GSAPKPVMPH VPPAPTPLTP LSPAPLATAA
     PAAASPAPAA DSLPVTCPGT EACPAVPPRQ SEKEQLLQAM ERSGWVQAKA ARLLNLTPRQ
     VGYALRKYDI DIKRF
//
DBGET integrated database retrieval system