ID NIFL_AZOVI Reviewed; 519 AA.
AC P30663;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Nitrogen fixation regulatory protein;
DE EC=2.7.13.3;
GN Name=nifL;
OS Azotobacter vinelandii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=8231815; DOI=10.1111/j.1365-2958.1993.tb01745.x;
RA Blanco G., Drummond M., Woodley P., Kennedy C.;
RT "Sequence and molecular analysis of the nifL gene of Azotobacter
RT vinelandii.";
RL Mol. Microbiol. 9:869-879(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 417-519.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=2840552; DOI=10.1111/j.1365-2958.1988.tb00034.x;
RA Bennet L.T., Cannon F., Dean D.R.;
RT "Nucleotide sequence and mutagenesis of the nifA gene from Azotobacter
RT vinelandii.";
RL Mol. Microbiol. 2:315-321(1988).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9601070; DOI=10.1042/bj3320413;
RA Macheroux P., Hill S., Austin S., Eydmann T., Jones T., Kim S.-O.,
RA Poole R., Dixon R.;
RT "Electron donation to the flavoprotein NifL, a redox-sensing
RT transcriptional regulator.";
RL Biochem. J. 332:413-419(1998).
RN [4]
RP FAD AND ADP-BINDING.
RX PubMed=8700899; DOI=10.1073/pnas.93.5.2143;
RA Hill S., Austin S., Eydmann T., Jones T., Dixon R.;
RT "Azotobacter vinelandii NIFL is a flavoprotein that modulates
RT transcriptional activation of nitrogen-fixation genes via a redox-sensitive
RT switch.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2143-2148(1996).
RN [5]
RP FAD AND ADP-BINDING.
RX PubMed=9593306; DOI=10.1046/j.1365-2958.1998.00788.x;
RA Soederbaeck E., Reyes-Ramirez F., Eydmann T., Austin S., Hill S., Dixon R.;
RT "The redox- and fixed nitrogen-responsive regulatory protein NIFL from
RT Azotobacter vinelandii comprises discrete flavin and nucleotide-binding
RT domains.";
RL Mol. Microbiol. 28:179-192(1998).
RN [6]
RP CRYSTALLIZATION.
RX PubMed=11717509; DOI=10.1107/s0907444901015657;
RA Hefti M., Hendle J., Enroth C., Vervoort J., Tucker P.A.;
RT "Crystallization and preliminary crystallographic data of the PAS domain of
RT the NifL protein from Azotobacter vinelandii.";
RL Acta Crystallogr. D 57:1895-1896(2001).
CC -!- FUNCTION: Required for the inhibition of NifA activity in response to
CC oxygen and low level of fixed nitrogen.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -226 mV.;
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DR EMBL; X64832; CAA46044.1; -; Genomic_DNA.
DR EMBL; Y00554; CAA68632.1; -; Genomic_DNA.
DR PIR; S19883; S19883.
DR PDB; 2GJ3; X-ray; 1.04 A; A/B=21-140.
DR PDBsum; 2GJ3; -.
DR AlphaFoldDB; P30663; -.
DR SASBDB; P30663; -.
DR SMR; P30663; -.
DR IntAct; P30663; 1.
DR EvolutionaryTrace; P30663; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:CACAO.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR014285; N_fixation_neg-reg_NifL.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR02938; nifL_nitrog; 1.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; FAD; Flavoprotein; Kinase; Nitrogen fixation;
KW Nucleotide-binding; Phosphoprotein; Repeat; Transcription;
KW Transcription regulation; Transferase; Two-component regulatory system.
FT CHAIN 1..519
FT /note="Nitrogen fixation regulatory protein"
FT /id="PRO_0000074815"
FT DOMAIN 23..93
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 94..148
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 151..217
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 302..517
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 305
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:2GJ3"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:2GJ3"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:2GJ3"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:2GJ3"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2GJ3"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:2GJ3"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:2GJ3"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2GJ3"
FT STRAND 109..120
FT /evidence="ECO:0007829|PDB:2GJ3"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:2GJ3"
SQ SEQUENCE 519 AA; 57827 MW; A40B1E76BD3723CB CRC64;
MTPANPTLSN EPQAPHAESD ELLPEIFRQT VEHAPIAISI TDLKANILYA NRAFRTITGY
GSEEVLGKNE SILSNGTTPR LVYQALWGRL AQKKPWSGVL VNRRKDKTLY LAELTVAPVL
NEAGETIYYL GMHRDTSELH ELEQRVNNQR LMIEAVVNAA PAAMVVLDRQ HRVMLSNPSF
CRLARDLVED GSSESLVALL RENLAAPFET LENQGSAFSG KEISFDLGGR SPRWLSCHGR
AIHIENEQAH VFFAPTEERY LLLTINDISE LRQKQQDSRL NALKALMAEE ELLEGMRETF
NAAIHRLQGP VNLISAAMRM LERRLGDKAG NDPVLSAMRE ASTAGMEALE NLSGSIPVRM
AESKMPVNLN QLIREVITLC TDQLLAQGIV VDWQPALRLP WVMGGESSQR SMIKHLVDNA
IESMSQNQVS RRELFISTRV ENHLVRMEIT DSGPGIPPDL VLKVFEPFFS TKPPHRVGRG
MGLPVVQEIV AKHAGMVHVD TDYREGCRIV VELPFSAST
//
