ID   Q42932_NICPL            Unreviewed;       956 AA.
AC   Q42932;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE            EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092 {ECO:0000313|EMBL:AAA34052.1};
RN   [1] {ECO:0000313|EMBL:AAA34052.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2527030; DOI=10.1016/0006-291X(89)92348-6;
RA   Boutry M., Michelet B., Goffeau A.;
RT   "Molecular cloning of a family of plant genes encoding a protein homologous
RT   to plasma membrane H+-translocating ATPases.";
RL   Biochem. Biophys. Res. Commun. 162:567-574(1989).
RN   [2] {ECO:0007829|PDB:3M50, ECO:0007829|PDB:3M51}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 927-954.
RX   PubMed=20437433; DOI=10.1002/anie.200907203;
RA   Rose R., Erdmann S., Bovens S., Wolf A., Rose M., Hennig S., Waldmann H.,
RA   Ottmann C.;
RT   "Identification and structure of small-molecule stabilizers of 14-3-3
RT   protein-protein interactions.";
RL   Angew. Chem. Int. Ed. 49:4129-4132(2010).
RN   [3] {ECO:0007829|PDB:4DX0}
RP   X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 927-954.
RX   PubMed=22467351; DOI=10.1002/chem.201103761;
RA   Richter A., Rose R., Hedberg C., Waldmann H., Ottmann C.;
RT   "An optimised small-molecule stabiliser of the 14-3-3-PMA2 protein-protein
RT   interaction.";
RL   Chemistry 18:6520-6527(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001250,
CC         ECO:0000256|RuleBase:RU362083};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362083};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU362083}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804,
CC       ECO:0000256|RuleBase:RU362083}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M27888; AAA34052.1; -; Genomic_DNA.
DR   PIR; A43637; A43637.
DR   PDB; 3M50; X-ray; 2.60 A; P=927-956.
DR   PDB; 3M51; X-ray; 3.25 A; P=927-956.
DR   PDB; 4DX0; X-ray; 3.40 A; P=926-956.
DR   PDBsum; 3M50; -.
DR   PDBsum; 3M51; -.
DR   PDBsum; 4DX0; -.
DR   AlphaFoldDB; Q42932; -.
DR   SMR; Q42932; -.
DR   EvolutionaryTrace; Q42932; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:UniProtKB-UniRule.
DR   CDD; cd02076; P-type_ATPase_H; 1.
DR   Gene3D; 6.10.140.890; -; 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; 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; IPR006534; P-type_ATPase_IIIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF125; PLASMA MEMBRANE ATPASE; 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   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3M50, ECO:0007829|PDB:3M51};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362083};
KW   Hydrogen ion transport {ECO:0000256|RuleBase:RU362083};
KW   Ion transport {ECO:0000256|RuleBase:RU362083};
KW   Magnesium {ECO:0000256|RuleBase:RU362083};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362083};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362083};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362083};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362083};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362083}; Transport {ECO:0000256|RuleBase:RU362083}.
FT   TRANSMEM        65..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        100..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        243..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        281..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        649..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        714..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        792..817
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   TRANSMEM        823..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362083"
FT   DOMAIN          17..89
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   956 AA;  105048 MW;  EC09622F256CDFD6 CRC64;
     MGEKPEVLDA VLKETVDLEN IPIEEVFENL RCTKEGLSGP AAQERLAIFG YNKLEEKKES
     KFLKFLGFMW NPLSWVMEAA AIMAIALANG GGKPPDWQDF VGIITLLVIN STISFIEENN
     AGNAAAALMA RLAPKAKVLR DGKWDEQDAA ILVPGDIISI KLGDIIPADA RLLEGDPLKI
     DQSALTGESL PVTKGPGDGV YSGSTCKQGE IEAVVIATGV HTFFGKAAHL VDSTNQVGHF
     QKVLTAIGNF CICSIAVGMI IEIIVMYPIQ HRKYRPGIDN LLVLLIGGIP IAMPTVLSVT
     MAIGSHRLAQ QGAITKRMTA IEEMAGMDVL CSDKTGTLTL NKLTVDKNLV EVFAKGVDAD
     TVVLMAARAS RTENQDAIDT AIVGMLSDPK EARAGIREIH FLPFNPTDKR TALTYLDGEG
     KMHRVSKGAP EQILNLAHNK SDIERRVHSV IDKFAERGLR SLGVAYQEVP EGRKESTGGP
     WQFIGLLPLF DPPRHDSAET IRRALNLGVN VKMITGDQLA IGKETGRRLG MGTNMYPSSA
     LLGQTKDESI ASLPIDELIE KADGFAGVFP EHKYEIVKRL QARKHICGMT GDGVNDAPAL
     KKADIGIAVD DATDAARSAS DIVLTEPGLS VIISAVLTSR AIFQRMKNYT IYAVSITIRI
     VLGFMLLALI WKFDFPPFMV LIIAILNDGT IMTISKDRVK PSPLPDSWKL AEIFTTGVVL
     GGYLAMMTVI FFWAAYETDF FPRVFGVSTL QKTATDDFRK LASAIYLQVS TISQALIFVT
     RSRSWSFVER PGLLLVVAFL IAQLVATLIA VYANWAFAAI EGIGWGWAGV IWLYNLVFYF
     PLDIIKFLIR YALSGRAWDL VLEQRIAFTR KKDFGKEQRE LQWAHAQRTL HGLQVPDTKL
     FSEATNFNEL NQLAEEAKRR AEIARQRELH TLKGHVESVV KLKGLDIETI QQSYTV
//