FIXL_AZOC5
ID FIXL_AZOC5 Reviewed; 504 AA.
AC P26489; A8I016;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Sensor protein FixL;
DE EC=2.7.13.3;
GN Name=fixL; OrderedLocusNames=AZC_4654;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2046550; DOI=10.1111/j.1365-2958.1991.tb00738.x;
RA Kaminski P.A., Elmerich C.;
RT "Involvement of fixLJ in the regulation of nitrogen fixation in
RT Azorhizobium caulinodans.";
RL Mol. Microbiol. 5:665-673(1991).
RN [2]
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.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RX PubMed=1766374; DOI=10.1111/j.1365-2958.1991.tb00820.x;
RA Kaminski P.A., Mandon K., Arigoni F., Desnoues N., Elmerich C.;
RT "Regulation of nitrogen fixation in Azorhizobium caulinodans:
RT identification of a fixK-like gene, a positive regulator of nifA.";
RL Mol. Microbiol. 5:1983-1991(1991).
CC -!- FUNCTION: Putative oxygen sensor; modulates the activity of FixJ, a
CC transcriptional activator of nitrogen fixation fixK gene. FixL probably
CC acts as a kinase that phosphorylates FixJ.
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=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 1 heme group per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: The heme moiety regulates the kinase activity.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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DR EMBL; X56658; CAA39979.1; -; Genomic_DNA.
DR EMBL; AP009384; BAF90652.1; -; Genomic_DNA.
DR EMBL; X59071; CAA41795.1; -; Genomic_DNA.
DR PIR; S15166; S15166.
DR RefSeq; WP_012173173.1; NC_009937.1.
DR AlphaFoldDB; P26489; -.
DR SMR; P26489; -.
DR STRING; 438753.AZC_4654; -.
DR EnsemblBacteria; BAF90652; BAF90652; AZC_4654.
DR KEGG; azc:AZC_4654; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_5; -.
DR OMA; NGIIMRI; -.
DR OrthoDB; 1755994at2; -.
DR BRENDA; 2.7.13.3; 609.
DR Proteomes; UP000000270; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
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 Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Heme; Iron; Kinase;
KW Membrane; Metal-binding; Nitrogen fixation; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..504
FT /note="Sensor protein FixL"
FT /id="PRO_0000074763"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 72..99
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..202
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 203..262
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 282..497
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 285
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 504 AA; 54319 MW; 2CF669C40B8A4E26 CRC64;
MTDTPTQALP PKAPQAGPTV PGTVRRAVPG SAAAALVIAA SHFAALSAFD PRILLVLLVI
VVLASSGGLF AGLAATAVSA LGLALRGLLS GDTVVADWQS LGLLTIAGAG IAVLGERLRR
TRLDAVARDR ALLAREAHLS SILDTVPDAM IVIDERGIMQ SFSITAERLF GYSPSEVIGR
NVSMLMPNPH RDQHDLYLSR YLTTGERRII GIGRVVTGER KDGATFPMEL AVGEMHSVSG
RFFTGFIRDL TERQNTEARL QELQAELVHI SRLTALGEMA STLAHELNQP LSAIANYIKG
SRRLLDDGDP KRIPMLQGAL DKAAEQALRA GQIIRRLRDF VSRGETERRV ESLSKLIEEA
SALALVGAKE HGIQVRYQID TSCDLVLADK VQVQQVLLNL MRNALEAMMD ASRRQLLVQT
TPAEDDMVTV SVCDTGHGIS DEMRAQLFTP FVTTKAQGMG VGLSISRTII EAHGGRIWAE
PNAGGGTIFR FTLRTVDEEA MNDA
