NIFL_KLEPN
ID NIFL_KLEPN Reviewed; 495 AA.
AC P06772;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Nitrogen fixation regulatory protein;
GN Name=nifL;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3062178; DOI=10.1016/0022-2836(88)90205-7;
RA Arnold W., Rump A., Klipp W., Priefer U.B., Puehler A.;
RT "Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire
RT nitrogen fixation gene cluster of Klebsiella pneumoniae.";
RL J. Mol. Biol. 203:715-738(1988).
RN [2]
RP CHARACTERIZATION.
RX PubMed=10350621; DOI=10.1016/s0167-4838(99)00075-8;
RA Schmitz R.A.;
RT "NifL of Klebsiella pneumoniae: redox characterization in relation to the
RT nitrogen source.";
RL Biochim. Biophys. Acta 1431:462-470(1999).
RN [3]
RP FAD-BINDING.
RX PubMed=9435114; DOI=10.1111/j.1574-6968.1997.tb12791.x;
RA Schmitz R.A.;
RT "NifL of Klebsiella pneumoniae carries an N-terminally bound FAD cofactor,
RT which is not directly required for the inhibitory function of NifL.";
RL FEMS Microbiol. Lett. 157:313-318(1997).
CC -!- FUNCTION: Required for the inhibition of NifA activity in response to
CC oxygen and low level of fixed nitrogen.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9435114};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -277 mV.;
CC -!- INTERACTION:
CC P06772; Q9ZA65: glnK; NbExp=4; IntAct=EBI-8500088, EBI-8499900;
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DR EMBL; X13303; CAA31681.1; -; Genomic_DNA.
DR PIR; A48370; A48370.
DR AlphaFoldDB; P06772; -.
DR IntAct; P06772; 1.
DR MINT; P06772; -.
DR GO; GO:0009399; P:nitrogen fixation; IDA:CACAO.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR InterPro; IPR036890; HATPase_C_sf.
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 Pfam; PF00989; PAS; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR02938; nifL_nitrog; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Nitrogen fixation; Repeat; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..495
FT /note="Nitrogen fixation regulatory protein"
FT /id="PRO_0000074817"
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..174
FT /note="PAS 2; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
SQ SEQUENCE 495 AA; 55213 MW; 127DF145BB1C1957 CRC64;
MTLNMMLDNA VPEAIAGALT QQHPGLFFTM VEQASVAISL TDARANITYA NPAFCRQTGY
SLAQLLNQNP RLLASSQTPR EIYQEMWQTL LQRQPWRGQL INQARDGGLY LVDIDITPVL
NPQGELEHYL AMQRDISVSY TLEQRLRNHM TLMEAVLNNI PAAVVVVDEQ DRVVMDNLAY
KTFCADCGGK ELLVELQVSP RKMGPGAEQI LPVVVRGAVR WLSVTCWALP GVSEEASRYF
VDSAPARTLM VIADCTQQRQ QQEQGRLDRL KQQMTAGKLL AAIRESLDAA LIQLNCPINM
LAAARRLNGE GSGNVALDAA WREGEEAMAR LQRCRPSLEL ESNAVWPLQP FFDDLYALYR
TRFDDRARLQ VDMASPHLVG FGQRTQLLAC LSLWLDRTLA LAAELPSVPL EIELYAEEDE
GWLSLYLNDN VPLLQVRYAH SPDALNSPGK GMELRLIQTL VAYHRGAIEL ASRPQGGTSL
VLRFPLFNTL TGGEQ