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Database: UniProt
Entry: A0A0U5AM99_9BACT
LinkDB: A0A0U5AM99_9BACT
Original site: A0A0U5AM99_9BACT 
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
//
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