FIXL_RHIME
ID FIXL_RHIME Reviewed; 505 AA.
AC P10955;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Sensor protein FixL;
DE EC=2.7.13.3;
GN Name=fixL; OrderedLocusNames=RA0670; ORFNames=SMa1229;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2842062; DOI=10.1016/s0092-8674(88)80012-6;
RA David M., Daveran M.-L., Batut J., Dedieu A., Domergue O., Ghai J.,
RA Hertig C., Boistard P., Kahn D.;
RT "Cascade regulation of nif gene expression in Rhizobium meliloti.";
RL Cell 54:671-683(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP TOPOLOGY.
RX PubMed=8432704; DOI=10.1128/jb.175.4.1103-1109.1993;
RA Lois A.F., Ditta G.S., Helinski D.R.;
RT "The oxygen sensor FixL of Rhizobium meliloti is a membrane protein
RT containing four possible transmembrane segments.";
RL J. Bacteriol. 175:1103-1109(1993).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 122-251.
RX PubMed=10926518; DOI=10.1006/jmbi.2000.3954;
RA Miyatake H., Mukai M., Park S.-Y., Adachi S., Tamura K., Nakamura H.,
RA Nakamura K., Tsuchiya T., Iizuka T., Shiro Y.;
RT "Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti:
RT crystallographic, mutagenesis and resonance Raman spectroscopic studies.";
RL J. Mol. Biol. 301:415-431(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.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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DR EMBL; Z21854; CAA79897.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65328.1; -; Genomic_DNA.
DR PIR; F95345; F95345.
DR PIR; S39984; S39984.
DR RefSeq; NP_435916.1; NC_003037.1.
DR RefSeq; WP_010967649.1; NC_003037.1.
DR PDB; 1D06; X-ray; 1.40 A; A=125-251.
DR PDB; 1EW0; X-ray; 1.40 A; A=128-251.
DR PDBsum; 1D06; -.
DR PDBsum; 1EW0; -.
DR AlphaFoldDB; P10955; -.
DR SMR; P10955; -.
DR EnsemblBacteria; AAK65328; AAK65328; SMa1229.
DR GeneID; 61599438; -.
DR KEGG; sme:SMa1229; -.
DR PATRIC; fig|266834.11.peg.690; -.
DR HOGENOM; CLU_000445_114_39_5; -.
DR OMA; NGIIMRI; -.
DR BRENDA; 2.7.13.3; 5347.
DR EvolutionaryTrace; P10955; -.
DR Proteomes; UP000001976; Plasmid pSymA.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Heme; Iron;
KW Kinase; Membrane; Metal-binding; Nitrogen fixation; Nucleotide-binding;
KW Phosphoprotein; Plasmid; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..505
FT /note="Sensor protein FixL"
FT /id="PRO_0000074765"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 135..205
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 BINDING 194
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 285
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:1D06"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:1D06"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:1D06"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1D06"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:1D06"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:1D06"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:1D06"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:1D06"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:1D06"
FT STRAND 225..237
FT /evidence="ECO:0007829|PDB:1D06"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:1D06"
SQ SEQUENCE 505 AA; 55073 MW; 1634E16CD3D5686F CRC64;
MLSKSGIERT QWGRRVVRWR GDGVAAYIVA AIVTSSVLAI RMIRAEPIGE GLLLFSFIPA
ILVVALIGGR NPILFAAGLS LVAAVSHQQI SSADGPSVVE LLVFGSAVLL IVALGEVLEA
ARRAIDRTED VVRARDAHLR SILDTVPDAT VVSATDGTIV SFNAAAVRQF GYAEEEVIGQ
NLRILMPEPY RHEHDGYLQR YMATGEKRII GIDRVVSGQR KDGSTFPMKL AVGEMRSGGE
RFFTGFIRDL TEREESAARL EQIQAELARL ARLNEMGEMA STLAHELNQP LSAIANYSHG
CTRLLRDMDD AVATRIREAL EEVASQSLRA GQIIKHLREF VTKGETEKAP EDIRKLVEES
AALALVGSRE QGVRTVFEYL PGAEMVLVDR IQVQQVLINL MRNAIEAMRH VDRRELTIRT
MPADPGEVAV VVEDTGGGIP EEVAGQLFKP FVTTKASGMG IGLSISKRIV EAHGGEMTVS
KNEAGGATFR FTLPAYLDER IVAND
