NIFA_RHOCB
ID NIFA_RHOCB Reviewed; 579 AA.
AC D5ARW9; P09434; Q8RU04;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Nif-specific regulatory protein;
GN Name=nifA1; Synonyms=nifA; OrderedLocusNames=RCAP_rcc03267;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-121.
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2710108; DOI=10.1007/bf00427050;
RA Jones R., Haselkorn R.;
RT "The DNA sequence of the Rhodobacter capsulatus ntrA, ntrB and ntrC gene
RT analogues required for nitrogen fixation.";
RL Mol. Gen. Genet. 215:507-516(1989).
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=CAA30920.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP001312; ADE86991.1; -; Genomic_DNA.
DR EMBL; X12358; CAA30920.1; ALT_FRAME; Genomic_DNA.
DR PIR; S03828; S03828.
DR RefSeq; WP_013068963.1; NC_014034.1.
DR AlphaFoldDB; D5ARW9; -.
DR SMR; D5ARW9; -.
DR STRING; 272942.RCAP_rcc03267; -.
DR EnsemblBacteria; ADE86991; ADE86991; RCAP_rcc03267.
DR GeneID; 31492048; -.
DR KEGG; rcp:RCAP_rcc03267; -.
DR eggNOG; COG3604; Bacteria.
DR HOGENOM; CLU_000445_95_2_5; -.
DR OMA; RCKFPGN; -.
DR OrthoDB; 123059at2; -.
DR Proteomes; UP000002361; Chromosome.
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; 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 4: Predicted;
KW Activator; ATP-binding; DNA-binding; Metal-binding; Nitrogen fixation;
KW Nucleotide-binding; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..579
FT /note="Nif-specific regulatory protein"
FT /id="PRO_0000410439"
FT DOMAIN 40..187
FT /note="GAF"
FT DOMAIN 226..454
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT REPEAT 505..506
FT /note="1"
FT REPEAT 507..508
FT /note="2"
FT REPEAT 509..510
FT /note="3"
FT REPEAT 511..512
FT /note="4"
FT REPEAT 513..514
FT /note="5"
FT REPEAT 515..516
FT /note="6"
FT REPEAT 517..518
FT /note="7"
FT DNA_BIND 551..570
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 464..536
FT /note="Inter-domain linker"
FT REGION 502..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..518
FT /note="7 X 2 AA tandem repeats of X-P"
FT REGION 537..579
FT /note="C-terminal DNA-binding domain"
FT COMPBIAS 503..521
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 254..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 317..326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 468
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P05407"
FT BINDING 473
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P05407"
SQ SEQUENCE 579 AA; 62898 MW; 65BF55942F8E1CD4 CRC64;
MTDQQSRPAS PRRRSTQSIA DRLALDALYE IAKTFAAAPD PVAEVPQIFN VLSSFLDLRH
GVLALLAEPG EGAGVNPYVI AATAFQRSPE APAADVLPDA VARIVFRSGV PFVSFDLAAE
FGAEAVPKRL RDAGQTLIAV PLRDPERSHF VLGVLAAYRS HDHNRSGFSD ADVRVLTMVA
SLLEQALRFR RRIARDRERA LEDTRRMLQT VTEQRGPAAP VSLDGIVGSS PAIAEVVAQI
KRVASTRMPV LLRGESGTGK ELFARAVHAQ SPRAKGPFIR VNCAALSETL LESELFGHEK
GAFTGATALK KGRFELADGG TLFLDEIGEI SPAFQSKLLR VLQEGEFERV GGAKTIKVDT
RIVAATNRDL EDAVARGQFR ADLYFRICVV PIVLPPLRNR KSDIKPLAQL FLDRFNKQNA
TNVKFAADAF DQICRCQFPG NVRELENCVN RAAALSDGAI VLAEELACRQ GACLSAELFR
LQDGTSPIGG LAVGRVITPT VRVSAPPPEP APAPEPAPEA PPREEVPLRT KTAQLSREEL
LRALESAGWV QAKAARLLGM TPRQIAYALQ KFEIELRKI
