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Database: UniProt
Entry: A0A261GAT7_9BIFI
LinkDB: A0A261GAT7_9BIFI
Original site: A0A261GAT7_9BIFI 
ID   A0A261GAT7_9BIFI        Unreviewed;       991 AA.
AC   A0A261GAT7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE            EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN   ORFNames=BAQU_0342 {ECO:0000313|EMBL:OZG68524.1};
OS   Bifidobacterium aquikefiri.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1653207 {ECO:0000313|EMBL:OZG68524.1, ECO:0000313|Proteomes:UP000216451};
RN   [1] {ECO:0000313|EMBL:OZG68524.1, ECO:0000313|Proteomes:UP000216451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 28769 {ECO:0000313|EMBL:OZG68524.1,
RC   ECO:0000313|Proteomes:UP000216451};
RX   PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA   Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA   Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA   van Sinderen D., Ventura M.;
RT   "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT   family.";
RL   BMC Genomics 18:568-568(2017).
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}.
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:OZG68524.1}.
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DR   EMBL; MWXA01000002; OZG68524.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261GAT7; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000216451; 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   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; 3.
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; PR00121; NAKATPASE.
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   Reference proteome {ECO:0000313|Proteomes:UP000216451};
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        91..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        768..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        804..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        854..878
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        898..918
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        930..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        962..981
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          33..107
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   991 AA;  105632 MW;  D504E41BA04FB592 CRC64;
     MTGPTSEHIE VSVPQVAGNS PASDIQADIQ DQDPSQLDAR NVLRAMHVDA STGLSSQEAE
     RRLERFGRNE LESAPPVPKW KKFLEQFRDP LVYLLFVATG ISVVAWFIER SQASHGGEGS
     EVLPFDAMVI VLILVLNAVL GYLQEAKAEK AVDALAKMTA PQTSVLRDGR VSHINTAELV
     PGDIMVLGEG DTVSADGRLL SAASLRIAEA SLTGESVPVS KKPETLASAK ALGDRTNMVF
     NGTAVTQGTG RAIITGTGMN TQVGKIADML SQTEDETTPL QKEMAHVSKI LGIAVCIIAV
     LVLVALATIS GFHSTQDVID SLLLAVSLAV AAVPEGLAAI LTVVLALGVQ RMAQHHAIVK
     KLSSVETLGS ASIICSDKTG TLTRNEMTVE KIVTPSGEVE LTGTGYAPIG QMVGTGGSDL
     SLDAPERVET LSTLAIGAIA NDGDVRKDDN SNEWKIVGDP TEVSLVVAAR KVHADKQLNS
     MNRIAEIPFT SERKRMSIIA EDKGDGNKLS VFAKGAPDVL LQYCTRIRVN GQVRRLTEGD
     RQTILATVER LSGQAYRTLG QAYRPLGTAA LSEVPGVISN AAGQVSDISE QDEAIEKDFI
     WTGMVGIIDP PRTEVRSAVA EAHRAGIRTV MITGDHPLTA ARIASDLGII RPGEQAKTGD
     DLDSLSEKDF DATTSDVSVY ARVAPEHKLK IVSSLQRQRN IVAMTGDGVN DAPAVKTSDI
     GVAMGITGTE VTKESAKMIL ADDNFSTIVA AVREGRVIFD NIRKFLRYLL SSNVGEVLTV
     FGGVIFAGFL GITQPGVEGV TVPLLATQLL WINLLTDAAP ALAMGVDPQT DDVMGRAPRG
     LYDRVIDGKM WGDIIFIGII MAAVTLIGMD MHLSGGLFTD RSVEAMGHDA QMVEARTMGF
     TILVFAQLFN AIASRSARQS AFIGLFTNKW LWGAIGLSIA LQLLVIYVPF LNTAFGTTAL
     NPMAWIECIA LAAFVLVASE LRKFVLRAMK R
//
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