ID A0A0U5AM99_9BACT Unreviewed; 861 AA.
AC A0A0U5AM99;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Na(+)/K(+)-exchanging ATPase {ECO:0000256|ARBA:ARBA00039096};
DE EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
GN ORFNames=THC_0765 {ECO:0000313|EMBL:BAU23156.1};
OS Caldimicrobium thiodismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU23156.1, ECO:0000313|Proteomes:UP000068196};
RN [1] {ECO:0000313|EMBL:BAU23156.1, ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|EMBL:BAU23156.1,
RC ECO:0000313|Proteomes:UP000068196};
RX PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring, and emended description of the genus
RT Caldimicrobium.";
RL Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN [2] {ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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}.
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DR EMBL; AP014945; BAU23156.1; -; Genomic_DNA.
DR RefSeq; WP_068513567.1; NZ_AP014945.1.
DR AlphaFoldDB; A0A0U5AM99; -.
DR STRING; 1653476.THC_0765; -.
DR KEGG; cthi:THC_0765; -.
DR OrthoDB; 9759222at2; -.
DR Proteomes; UP000068196; Chromosome.
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 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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000068196};
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 51..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..821
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 833..852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..75
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 861 AA; 96326 MW; 57C6F88502182C11 CRC64;
MRINELSSEE VFRVLRTTSE GLSEEEARRR LIQFGYNEIK ETRKYVLLKK FISQFTHFLA
LILWIGAFLA FLADYLQPGE GMRHLGFAIL TVILINAIFA FFQEYKAEKS LEKLKELLPS
YIRVIRDGKE REISVREIVP GDLLLLYEGD KVPADARVIE AYALSLDKSH LTGEANPLFL
ITEPFKGELF QSPNIAFAGS TVLSGWGKAV VFATGSQTEF GRIARLTETV KIEKTPLQKE
ISKTSRLIAL FATSIGLIFF LIGHFLEKSF WENFTFAIGV IVALVPEGLL PTVTLSLAMV
SQRMLKRKAL VKVLTAVEGL GSVSVICTDK TGTLTQNKME VRDLWIFDEK AFPMFLKIAL
LCNNTKEMEG ELKGDPTEVA LYKFAKTYLK ETPSERLSEI PFDPIRKRMT TQNKLDEGLL
FLTKGATEGI LPLCTHALIS GKKVKLDEKL REEILKNYES LMEKGLRVLA LAFSEAEPEK
DMTFVGLIGL EDPPRPEVKE AIRKCKEAGI RIILVTGDAS KTALAISREI GLASNPVIIE
GEEFHKMTDE ELKEKLKAKE ILFTRMSPKD KLRIVTLLQE LGERVAVTGD GVNDAPAIKK
ADIGIAMGSG TEVAKEVSSI ILLDDNFATI VSAIEEGRGV YENIKKFLAY FLTSNVAELV
PYILYAFYRL PLPLTIMQIL AIDLGTDILP GLALGIEKPT GEEMKKPPRS PKEKLFSLLL
ILRVCLLLAP FEVIAGLFGY FYVLYTGGWS LGTLLEPTNL LYQQATTACL TGIVLTQIGN
VMACRTFRTP VLKIGLFSNP FLLIGILFEV FLQLFIVYHP LGQKIFSTYA LPLHIWLILF
PFALALFITT DLSKYLMSKK F
//