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Database: UniProt
Entry: B6IT10_RHOCS
LinkDB: B6IT10_RHOCS
Original site: B6IT10_RHOCS 
ID   B6IT10_RHOCS            Unreviewed;       819 AA.
AC   B6IT10;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Nitrogen fixation protein FixI (Coupling cation pump) {ECO:0000313|EMBL:ACI98681.1};
GN   Name=fixI {ECO:0000313|EMBL:ACI98681.1};
GN   OrderedLocusNames=RC1_1274 {ECO:0000313|EMBL:ACI98681.1};
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI98681.1, ECO:0000313|Proteomes:UP000001591};
RN   [1] {ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI98681.1, ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX   PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA   Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA   Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA   Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT   "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT   proteobacterium Rhodospirillum centenum.";
RL   BMC Genomics 11:325-325(2010).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC       ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; CP000613; ACI98681.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6IT10; -.
DR   STRING; 414684.RC1_1274; -.
DR   KEGG; rce:RC1_1274; -.
DR   eggNOG; COG2217; Bacteria.
DR   eggNOG; COG2608; Bacteria.
DR   HOGENOM; CLU_001771_0_3_5; -.
DR   OrthoDB; 9760802at2; -.
DR   Proteomes; UP000001591; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR021993; ATPase-cat-bd.
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   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR   Pfam; PF12156; ATPase-cat_bd; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 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 {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001591};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        188..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        221..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        258..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        282..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        442..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        466..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        763..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          101..167
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   819 AA;  85542 MW;  71B534D5DAC4F42F CRC64;
     MSLALFDLDT APGDGLSARR PGEAGQAPGA GGCLHCGLPV PRPGDRFCCA GCEGAHALIH
     ELGLDAYYRR RETAPAEPLQ ATEEVKLDLL SQVEDRPDGS HCLRMRVDGL TCGACVWLIE
     TALAKQPQVE EVRVNLTTRR LTLRWSGPRE RAEGLVATVR RLGYRLAPFD TAAENDPQAR
     HERELLRCMA VAGFAAMNIM LLSVSVWSGH AGSMGDATRT LMHWLSALIA LPTVLYAGRP
     FFRSAIAALR AGRSNMDVPI SLGVTLASGI SLWETMNQGQ HAYFDGAVML LFFLLIGRYL
     DSRARGRARS AAEHLLALAR APVTVLQPDG SIALSAPSAV PAGATVLVAA GERVGVDGAV
     AEGRSEVDTS VVTGETRPLP VEPGTRLFAG MLNLSAPLRV TVTASGEGTL LAEIVRLMEA
     AEQGRARFVA LADRVARHYT PVVHTLALGT FLAWTLGVGL DWQPALLIAV AVLIITCPCA
     LALAVPAVQV VASDRLLRQG TLLKSATALE RLATVDTVVF DKTGTLTLGR PELLPDAGRD
     AAVLDRAATL ARNSRHPLSR ALARAAGPGP VAIGVRELPG RGLELDTADG TVRLGSRAFV
     GAPAAAAPGP SGAVADAELW LAEPGRAPVR FAFADRARSD AATVVSDLRR AGYRVELLSG
     DRPEAVAALA AETGLDDWRG GVDPAGKCAR LAELRAAGRR VLMVGDGLND AAALAAADVS
     ASPASAVDIA QTAADAVFQG DRLAPVADLL AVARMADRLV RQNLGFTLIY NMCAVPIAML
     GHATPLVAAV AMSSSSLIVI GNAMRLSGRR TGARAGGGS
//
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