FIXL_BRADU
ID FIXL_BRADU Reviewed; 505 AA.
AC P23222;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Sensor protein FixL;
DE EC=2.7.13.3;
GN Name=fixL; OrderedLocusNames=bll2760;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=2000090; DOI=10.1007/bf00282640;
RA Anthamatten D., Hennecke H.;
RT "The regulatory status of the fixL- and fixJ-like genes in Bradyrhizobium
RT japonicum may be different from that in Rhizobium meliloti.";
RL Mol. Gen. Genet. 225:38-48(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 154-270.
RX PubMed=9860942; DOI=10.1073/pnas.95.26.15177;
RA Gong W., Hao B., Mansy S.S., Gonzalez G., Gilles-Gonzalez M.-A., Chan M.K.;
RT "Structure of a biological oxygen sensor: a new mechanism for heme-driven
RT signal transduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15177-15182(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 154-270.
RX PubMed=10747783; DOI=10.1021/bi992346w;
RA Gong W., Hao B., Chan M.K.;
RT "New mechanistic insights from structural studies of the oxygen-sensing
RT domain of Bradyrhizobium japonicum FixL.";
RL Biochemistry 39:3955-3962(2000).
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;
CC Note=Binds 1 heme group per subunit.;
CC -!- ACTIVITY REGULATION: The heme moiety regulates the kinase activity.
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DR EMBL; X56808; CAA40143.1; -; Genomic_DNA.
DR EMBL; AJ005001; CAA06276.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC48025.1; -; Genomic_DNA.
DR PIR; S13330; S13330.
DR RefSeq; NP_769400.1; NC_004463.1.
DR RefSeq; WP_011085545.1; NZ_CP011360.1.
DR PDB; 1DP6; X-ray; 2.30 A; A=141-270.
DR PDB; 1DP8; X-ray; 2.50 A; A=141-270.
DR PDB; 1DP9; X-ray; 2.60 A; A=141-270.
DR PDB; 1DRM; X-ray; 2.40 A; A=141-270.
DR PDB; 1LSV; X-ray; 2.40 A; A=141-270.
DR PDB; 1LSW; X-ray; 2.20 A; A=141-270.
DR PDB; 1LSX; X-ray; 2.70 A; A=141-270.
DR PDB; 1LT0; X-ray; 2.40 A; A=141-270.
DR PDB; 1XJ2; X-ray; 2.00 A; A=154-269.
DR PDB; 1XJ3; X-ray; 1.90 A; A=154-269.
DR PDB; 1XJ4; X-ray; 1.80 A; A/B=151-269.
DR PDB; 1XJ6; X-ray; 1.90 A; A/B=151-269.
DR PDB; 1Y28; X-ray; 2.10 A; A=141-270.
DR PDB; 2CMN; X-ray; 2.30 A; A=141-270.
DR PDB; 2OWH; X-ray; 2.50 A; A=154-269.
DR PDB; 2OWJ; X-ray; 2.50 A; A=154-269.
DR PDB; 2VV6; X-ray; 1.50 A; A/B/C/D=151-269.
DR PDB; 2VV7; X-ray; 1.81 A; A/B/C/D=151-269.
DR PDB; 2VV8; X-ray; 1.61 A; A/B/C/D=151-269.
DR PDB; 4GCZ; X-ray; 2.30 A; A/B=257-505.
DR PDBsum; 1DP6; -.
DR PDBsum; 1DP8; -.
DR PDBsum; 1DP9; -.
DR PDBsum; 1DRM; -.
DR PDBsum; 1LSV; -.
DR PDBsum; 1LSW; -.
DR PDBsum; 1LSX; -.
DR PDBsum; 1LT0; -.
DR PDBsum; 1XJ2; -.
DR PDBsum; 1XJ3; -.
DR PDBsum; 1XJ4; -.
DR PDBsum; 1XJ6; -.
DR PDBsum; 1Y28; -.
DR PDBsum; 2CMN; -.
DR PDBsum; 2OWH; -.
DR PDBsum; 2OWJ; -.
DR PDBsum; 2VV6; -.
DR PDBsum; 2VV7; -.
DR PDBsum; 2VV8; -.
DR PDBsum; 4GCZ; -.
DR AlphaFoldDB; P23222; -.
DR SMR; P23222; -.
DR STRING; 224911.27351017; -.
DR DrugBank; DB02671; 1-Methylimidazole.
DR DrugBank; DB03366; Imidazole.
DR EnsemblBacteria; BAC48025; BAC48025; BAC48025.
DR GeneID; 64022517; -.
DR KEGG; bja:bll2760; -.
DR PATRIC; fig|224911.44.peg.2381; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_5; -.
DR InParanoid; P23222; -.
DR OMA; MVQFRDI; -.
DR PhylomeDB; P23222; -.
DR BRENDA; 2.7.13.3; 929.
DR EvolutionaryTrace; P23222; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
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; 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 Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Heme; Iron; Kinase; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Two-component regulatory system.
FT CHAIN 1..505
FT /note="Sensor protein FixL"
FT /id="PRO_0000074764"
FT DOMAIN 14..85
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 88..140
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 141..208
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 209..268
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 288..503
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT BINDING 200
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 291
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:2VV6"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2VV6"
FT HELIX 170..176
FT /evidence="ECO:0007829|PDB:2VV6"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2VV6"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2VV6"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:2VV6"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2VV6"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:2VV6"
FT STRAND 231..243
FT /evidence="ECO:0007829|PDB:2VV6"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:2VV6"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:1XJ3"
FT HELIX 277..311
FT /evidence="ECO:0007829|PDB:4GCZ"
FT HELIX 319..347
FT /evidence="ECO:0007829|PDB:4GCZ"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:4GCZ"
FT HELIX 359..370
FT /evidence="ECO:0007829|PDB:4GCZ"
FT TURN 371..378
FT /evidence="ECO:0007829|PDB:4GCZ"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:4GCZ"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:4GCZ"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:4GCZ"
FT HELIX 396..413
FT /evidence="ECO:0007829|PDB:4GCZ"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:4GCZ"
FT STRAND 421..429
FT /evidence="ECO:0007829|PDB:4GCZ"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:4GCZ"
FT STRAND 433..439
FT /evidence="ECO:0007829|PDB:4GCZ"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:4GCZ"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:4GCZ"
FT HELIX 468..478
FT /evidence="ECO:0007829|PDB:4GCZ"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:4GCZ"
FT STRAND 491..501
FT /evidence="ECO:0007829|PDB:4GCZ"
SQ SEQUENCE 505 AA; 55652 MW; 1854A0C7EDAC32C6 CRC64;
MAPTRVTHPP DDGRGEHFRV RIEGFGVGTW DLDLKTWALD WSDTARTLLG IGQDQPASYD
LFLSRLEPDD RERVESAIKR VSERGGGFDV SFRVAGTSNA GQWIRARAGL IRDEAGTARH
LSGIFLDIDE EKQVEGALRT RETHLRSILH TIPDAMIVID GHGIIQLFST AAERLFGWSE
LEAIGQNVNI LMPEPDRSRH DSYISRYRTT SDPHIIGIGR IVTGKRRDGT TFPMHLSIGE
MQSGGEPYFT GFVRDLTEHQ QTQARLQELQ SELVHVSRLS AMGEMASALA HELNQPLAAI
SNYMKGSRRL LAGSSDPNTP KVESALDRAA EQALRAGQII RRLRDFVARG ESEKRVESLS
KLIEEAGALG LAGAREQNVQ LRFSLDPGAD LVLADRVQIQ QVLVNLFRNA LEAMAQSQRR
ELVVTNTPAA DDMIEVEVSD TGSGFQDDVI PNLFQTFFTT KDTGMGVGLS ISRSIIEAHG
GRMWAESNAS GGATFRFTLP AADEN
