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Database: UniProt
Entry: I0V7M4_9PSEU
LinkDB: I0V7M4_9PSEU
Original site: I0V7M4_9PSEU 
ID   I0V7M4_9PSEU            Unreviewed;       938 AA.
AC   I0V7M4;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN   ORFNames=SacxiDRAFT_3936 {ECO:0000313|EMBL:EID56127.1};
OS   Saccharomonospora xinjiangensis XJ-54.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882086 {ECO:0000313|EMBL:EID56127.1, ECO:0000313|Proteomes:UP000004691};
RN   [1] {ECO:0000313|EMBL:EID56127.1, ECO:0000313|Proteomes:UP000004691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XJ-54 {ECO:0000313|EMBL:EID56127.1,
RC   ECO:0000313|Proteomes:UP000004691};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA   Klenk H.-P., Woyke T.;
RT   "Improved High-Quality Draft sequence of Saccharomonospora xinjiangensis
RT   XJ-54.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC       catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC       potassium ions across the plasma membrane. This action creates the
CC       electrochemical gradient of sodium and potassium ions, providing the
CC       energy for active transport of various nutrients.
CC       {ECO:0000256|ARBA:ARBA00037422}.
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         Evidence={ECO:0000256|ARBA:ARBA00001836};
CC   -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC       catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC       additional regulatory subunit. {ECO:0000256|ARBA:ARBA00038795}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; JH636049; EID56127.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0V7M4; -.
DR   STRING; 882086.SacxiDRAFT_3936; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_4_1_11; -.
DR   Proteomes; UP000004691; Unassembled WGS sequence.
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   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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR43294:SF13; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        81..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        786..812
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        832..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        865..887
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        899..917
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..105
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   938 AA;  100407 MW;  F78B72130A8EE5A3 CRC64;
     MATASQAPLP RVALRLYTPA YPRCQPGNVS QSDPREPVTL LLRDLRSKPG GLPSREAARR
     LEIYGPNELR RKQRTDWPRQ LIRQFTHPLA LLLWLAALLA MVSSSTELAV AVVAVIVLNA
     AFAFTQEQQA EKAVEALSAY LPARATVLRD GTRTAVEARD LVPGDVLVVE EGDRVSADAR
     LLDGSVEVDL SPLTGESLPA YRSAELKDVT GPLLDARDLL FSGTNCTGGQ ALAVVFATGM
     HTELGKIAAL SQRVGRDESP LEKQVKRVAW LIAAVAVGVG VAFLPLGAFV AGLPLDDALN
     FAIGLLVANV PEGLLPTITL ALAVGVRALA RGGAVVKRLS AVETLGSTTV ICTDKTGTLT
     RNRMRVTRLW TFAGELTGEA SGTPPEPARA LAEVVSACSN AELDPSDPGA EGSGDQTEIA
     LLRAARSLGE DVSPERRAGH RLRQFHFDAT LRLMSTLDRR GDRTVLNVKG APEAVLERAT
     TYLPGEGGPQ PLTDTERARV TEAIDRYAHQ GLRLLAVATR DVTGDAADAR RDELERDLTL
     IGVAAMIDPP RDGVPEAVAR CHSAGIRLIM VTGDHALTAG EIARKIGLAR DHPTVITGDR
     LAELSERELE SLLEGKRELV FARTSPEVKL RIADALRAQG NVVAMTGDGV NDAPALRRAD
     IGVAMGVTGT DVAREASTMV LTDDNFSTIV TAVEEGRRVY DNVRKFIVYI FAHATPEVIP
     FLLFALSGGR IPLPLTVLQI LAIDLGTETL PALALGREPA EPGVMSRPPR RRSENVITHA
     MLGRAWGLLG GVSAVLVLGG FFLTLFAGGW YFGAPVGEGT ALHPVWQQAT TMTFLGIVAC
     QIGTAFASRA QYASLRTVGP WSNRLLLWGI LFEVVFSAAV VTLPPLRAVF GTAPPPAEQL
     AMLVVFPFVV WGIDEWYRWW RRARGWGGRD VLAPAATG
//
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