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-AUG-2022, entry version 157.
DE   RecName: Full=Nitrogen fixation protein FixI;
DE   AltName: Full=E1-E2 type cation ATPase FixI;
DE            EC=7.2.2.-;
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; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RCR2011 / SU47;
RX   PubMed=2536685; DOI=10.1128/jb.171.2.929-939.1989;
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., 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).
CC   -!- FUNCTION: FixI is a pump of a specific cation involved in symbiotic
CC       nitrogen fixation. The four proteins FixG, FixH, FixI, and FixS may
CC       participate in a membrane-bound complex coupling the FixI cation pump
CC       with a redox process catalyzed by FixG.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
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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   AlphaFoldDB; P18398; -.
DR   SMR; P18398; -.
DR   EnsemblBacteria; AAK65317; AAK65317; SMa1209.
DR   GeneID; 61599427; -.
DR   KEGG; sme:SMa1209; -.
DR   PATRIC; fig|266834.11.peg.679; -.
DR   HOGENOM; CLU_001771_0_3_5; -.
DR   OMA; CKTVYEI; -.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   PRINTS; PR00120; HATPASE.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 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; Magnesium; Membrane; Metal-binding;
KW   Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Plasmid;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..757
FT                   /note="Nitrogen fixation protein FixI"
FT                   /id="PRO_0000046156"
FT   TOPO_DOM        1..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..158
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..185
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..218
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..368
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        392..398
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        417..688
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        689..708
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        709..713
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        714..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        733..757
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..107
FT                   /note="HMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   ACT_SITE        454
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         51
FT                   /ligand="a metal cation"
FT                   /ligand_id="ChEBI:CHEBI:25213"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT   BINDING         634
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   BINDING         638
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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