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Database: UniProt
Entry: P18398
LinkDB: P18398
Original site: P18398 
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   03-SEP-2014, entry version 120.
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   RefSeq; WP_010967638.1; 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; K01533; -.
DR   OMA; RTLDHIM; -.
DR   OrthoDB; EOG6742RM; -.
DR   BioCyc; SMEL266834:GJF6-5667-MONOMER; -.
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: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   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   SUPFAM; SSF56784; SSF56784; 2.
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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