ID FIXI_RHIME Reviewed; 757 AA.
AC P18398;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 01-MAY-2013, entry version 113.
DE RecName: Full=Nitrogen fixation protein FixI;
DE AltName: Full=E1-E2 type cation ATPase FixI;
DE EC=3.6.3.-;
GN Name=fixI; OrderedLocusNames=RA0659; ORFNames=SMa1209;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RCR2011 / SU47;
RX PubMed=2536685;
RA Kahn D., David M., Domergue O., Daveran M.-L., Ghai J., Hirsch P.R.,
RA Batut J.;
RT "Rhizobium meliloti fixGHI sequence predicts involvement of a specific
RT cation pump in symbiotic nitrogen fixation.";
RL J. Bacteriol. 171:929-939(1989).
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.,
RA Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J.,
RA Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L.,
RA Kalman S., Keating D.H., Palm C., Peck M.C., Surzycki R., Wells D.H.,
RA Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire
RT Sinorhizobium 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.,
RA Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M.,
RA Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D.,
RA Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V.,
RA Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B.,
RA Ramsperger U., Surzycki R., Thebault P., Vandenbol M.,
RA Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: FixI is a pump of a specific cation involved in
CC symbiotic nitrogen fixation. The four proteins FixG, FixH, FixI,
CC and FixS may participate in a membrane-bound complex coupling the
CC FixI cation pump with a redox process catalyzed by FixG.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC (TC 3.A.3) family. Type IB subfamily.
CC -!- SIMILARITY: Contains 1 HMA domain.
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DR EMBL; Z21854; CAA79907.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65317.1; -; Genomic_DNA.
DR PIR; C32052; C32052.
DR PIR; C95344; C95344.
DR RefSeq; NP_435905.1; NC_003037.1.
DR ProteinModelPortal; P18398; -.
DR STRING; 266834.SMa1209; -.
DR EnsemblBacteria; AAK65317; AAK65317; SMa1209.
DR GeneID; 1235695; -.
DR KEGG; sme:SMa1209; -.
DR PATRIC; 23627800; VBISinMel96828_0679.
DR eggNOG; COG2217; -.
DR HOGENOM; HOG000250398; -.
DR KO; K01552; -.
DR OMA; HTISAVI; -.
DR ProtClustDB; CLSK864486; -.
DR BioCyc; SMEL266834:GJF6-5667-MONOMER; -.
DR GO; GO:0016021; C:integral to 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:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR Gene3D; 2.70.150.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
DR InterPro; IPR027256; Cation_transp_P-typ_ATPase_IB.
DR InterPro; IPR001757; Cation_transp_P_typ_ATPase.
DR InterPro; IPR023214; HAD-like_dom.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HeavyMe-assoc_HMA.
DR PANTHER; PTHR24093; PTHR24093; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SUPFAM; SSF56784; HAD-like_dom; 1.
DR SUPFAM; SSF55008; HeavyMe_transpt; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Nitrogen fixation; Nucleotide-binding;
KW Phosphoprotein; Plasmid; Transmembrane; Transmembrane helix.
FT CHAIN 1 757 Nitrogen fixation protein FixI.
FT /FTId=PRO_0000046156.
FT TOPO_DOM 1 121 Cytoplasmic (Potential).
FT TRANSMEM 122 143 Helical; (Potential).
FT TOPO_DOM 144 158 Extracellular (Potential).
FT TRANSMEM 159 178 Helical; (Potential).
FT TOPO_DOM 179 185 Cytoplasmic (Potential).
FT TRANSMEM 186 206 Helical; (Potential).
FT TOPO_DOM 207 218 Extracellular (Potential).
FT TRANSMEM 219 239 Helical; (Potential).
FT TOPO_DOM 240 368 Cytoplasmic (Potential).
FT TRANSMEM 369 391 Helical; (Potential).
FT TOPO_DOM 392 398 Extracellular (Potential).
FT TRANSMEM 399 416 Helical; (Potential).
FT TOPO_DOM 417 688 Cytoplasmic (Potential).
FT TRANSMEM 689 708 Helical; (Potential).
FT TOPO_DOM 709 713 Extracellular (Potential).
FT TRANSMEM 714 732 Helical; (Potential).
FT TOPO_DOM 733 757 Cytoplasmic (Potential).
FT DOMAIN 38 108 HMA.
FT ACT_SITE 454 454 4-aspartylphosphate intermediate (By
FT similarity).
FT METAL 48 48 Potential.
FT METAL 51 51 Potential.
FT METAL 634 634 Magnesium (By similarity).
FT METAL 638 638 Magnesium (By similarity).
SQ SEQUENCE 757 AA; 79559 MW; DE2E5C6249254AA5 CRC64;
MSCCASSAAI MVAEGGQASP ASEELWLASR DLGGGLRQTE LSVPNAYCGT CIATIEGALR
AKPEVERARV NLSSRRVSIV WKEEVGGRRT NPCDFLHAIA ERGYQTHLFS PGEEEGDDLL
KQLILAVAVS GFAATNIMLL SVSVWSGADA ATRDLFHWIS ALIAGPALIY AGRFFYKSAW
NAIRHGRTNM DVPIALAVSL SYGMSLHETI GHGEHAWFDA SVTLLFFLLI GRTLDHMMRG
RARTAISGLA RLSPRGATVV HPDGSREYRA VDEINPGDRL IVAAGERVPV DGRVLSGTSD
LDRSVVNGES SPTVVTTGDT VQAGTLNLTG PLTLEATAAA RDSFIAEIIG LMEAAEGGRA
RYRRIADRAA RYYSPAVHLL ALLTFVGWML VEGDVRHAML VAVAVLIITC PCALGLAVPV
VQVVAAGRLF QGGVMVKDGS AMERLAEIDT VLLDKTGTLT IGKPRLVNAH EISPGRLATA
AAIAVHSRHP IAVAIQNSAG AASPIAGDIR EIPGAGIEVK TEDGVYRLGS RDFAVGGSGP
DGRQSEAILS LDFRELACFR FEDQPRPASR ESIEALGRLG IATGILSGDR APVVAALASS
LGISNWYAEL SPREKVQVCA AAAEAGHKAL VVGDGINDAP VLRAAHVSMA PATAADVGRQ
AADFVFMHER LSAVPFAIET SRHAGQLIRQ NFALAIGYNV IAVPIAILGY ATPLVAAVAM
SSSSLVVVFN ALRLKRSLAA GRGATPGTLI HSGAVTS
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