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
//