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Database: UniProt
Entry: A0A0P6WX80_9BACI
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Original site: A0A0P6WX80_9BACI 
ID   A0A0P6WX80_9BACI        Unreviewed;       893 AA.
AC   A0A0P6WX80;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN   ORFNames=AM506_00695 {ECO:0000313|EMBL:KPL61187.1};
OS   Rossellomorea vietnamensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX   NCBI_TaxID=218284 {ECO:0000313|EMBL:KPL61187.1, ECO:0000313|Proteomes:UP000050398};
RN   [1] {ECO:0000313|EMBL:KPL61187.1, ECO:0000313|Proteomes:UP000050398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-SED5 {ECO:0000313|EMBL:KPL61187.1,
RC   ECO:0000313|Proteomes:UP000050398};
RA   Lee R.D., Jospin G., Lang J.M., Coil D.A., Eisen J.A.;
RT   "Draft Genome Sequence of Bacillus vietnamensis UCD-SED5.";
RL   Submitted (AUG-2015) 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   -!- 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPL61187.1}.
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DR   EMBL; LIXZ01000001; KPL61187.1; -; Genomic_DNA.
DR   RefSeq; WP_060669824.1; NZ_LIXZ01000001.1.
DR   AlphaFoldDB; A0A0P6WX80; -.
DR   PATRIC; fig|218284.4.peg.143; -.
DR   eggNOG; COG0474; Bacteria.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000050398; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   CDD; cd02089; P-type_ATPase_Ca_prok; 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; 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; PF13246; Cation_ATPase; 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; SFLDS00003; Haloacid_Dehalogenase; 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   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050398};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        48..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        268..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        693..715
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        721..742
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        770..789
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        795..813
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        834..854
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        869..889
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..76
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   893 AA;  97785 MW;  65F4C398C036D313 CRC64;
     MKFHEMRQED IEQSLNTNYQ EGLSTEEVAI RRKQFGYNQL EEAEKQSALL LFFSQFKDFM
     VLVLLAATLI SGLLGEYIDA IAIIAIVFIN GFLGFFQERK AERSLQALKE LSAPQVSVLR
     DGKWVKIVSK DVIIGDVIRF ASGDRIGADV RLIEANNLEI EESALTGESL PVTKSTNPVN
     GENMSLGDLE NMAFMGTMVT RGNGIGVVTS IGMKTAMGQI ADMIQNAETI TTPLQRRLEE
     LGKILITVAL VLTGLVVGIG VIQGHDMYTM FLAGVSLAVA AIPEGLPAIV TVALSLGVQR
     MIKKKAIVRK LPAVETLGCA SVICSDKTGT LTQNKMTVTH LWSGGRTWTV TGTGYEPDGQ
     FYTGEKRVTP HSENALQQLL TFGMLCNHAE LVTREKTFIV DGDPTEGALL VAGLKAGLSR
     ESLQKKFTIV KEFPFDSTRK MMSIIVVDQN GKHFSVTKGA PDVLVGKSES ILWEGRLQPK
     SHEITEKVEG AISEMSSNAL RNIAIAYKPI KDRAVETLVE QDVEEGVTFI GLQGMIDPPR
     PEVKQAVKEC RAAGIKTVMI TGDHVLTAKA IAKQLGILKN KDRVIEGKEL NLMEVHELEE
     IVDEVSVFAR VSPEHKLKIV KALQNRGHVV AMTGDGVNDA PAIKSSDIGV AMGITGTDVS
     KESSSLVLLD DNFATIKSAI QEGRNIYENI RKFIRYLLAS NVGEILVMLF AMILALPLPL
     VPIQILWVNL VTDGLPAMAL GLDKPEDDVM RRKPRHPKEG VFARGLGWKV VSRGFLIGGA
     TLLAFMLSYK THPDHLAYAQ TVAFATLVMA QLIHVFDCRS EVSVFSRNPF GNMYLVFAVL
     SSLILMLLVI YVPSLQPIFH TVPIVFKDWL LIIGLSSVPT FLLAGSFFAR KKQ
//
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