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Plasma membrane ATPase (EC 3.6.3.6) (Proton pump)

 PMA1_KLULA              Reviewed;         899 AA.
P49380;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
10-OCT-2018, entry version 137.
RecName: Full=Plasma membrane ATPase;
EC=3.6.3.6;
AltName: Full=Proton pump;
Name=PMA1; OrderedLocusNames=KLLA0A09031g;
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
NCBI_TaxID=284590;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF MET-669.
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=7730265; DOI=10.1128/jb.177.9.2360-2367.1995;
Miranda M., Ramirez J., Pena A., Coria R.;
"Molecular cloning of the plasma membrane H(+)-ATPase from
Kluyveromyces lactis: a single nucleotide substitution in the gene
confers ethidium bromide resistance and deficiency in K+ uptake.";
J. Bacteriol. 177:2360-2367(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
WM37;
PubMed=15229592; DOI=10.1038/nature02579;
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
Wincker P., Souciet J.-L.;
"Genome evolution in yeasts.";
Nature 430:35-44(2004).
-!- FUNCTION: The plasma membrane ATPase of plants and fungi is a
hydrogen ion pump. The proton gradient it generates drives the
active transport of nutrients by H(+)-symport. The resulting
external acidification and/or internal alkinization may mediate
growth responses.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
H(+)(Out).
-!- ACTIVITY REGULATION: Activated by high pH or also by potassium
ions when the medium pH is low.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIIA subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L37875; AAA69688.1; -; Genomic_DNA.
EMBL; CR382121; CAH02983.1; -; Genomic_DNA.
RefSeq; XP_451395.1; XM_451395.1.
ProteinModelPortal; P49380; -.
SMR; P49380; -.
STRING; 284590.XP_451395.1; -.
PRIDE; P49380; -.
EnsemblFungi; CAH02983; CAH02983; KLLA0_A09031g.
GeneID; 2896449; -.
KEGG; kla:KLLA0_A09031g; -.
eggNOG; KOG0205; Eukaryota.
eggNOG; COG0474; LUCA.
HOGENOM; HOG000160005; -.
InParanoid; P49380; -.
KO; K01535; -.
OMA; HKYNVVE; -.
OrthoDB; EOG092C0HLD; -.
Proteomes; UP000000598; Chromosome A.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008553; F:proton-exporting ATPase activity, phosphorylative mechanism; IEA:UniProtKB-EC.
GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
CDD; cd02076; P-type_ATPase_H; 1.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006534; P-type_ATPase_IIIA.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00690; Cation_ATPase_N; 1.
PRINTS; PR00120; HATPASE.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Hydrogen ion transport;
Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 899 Plasma membrane ATPase.
/FTId=PRO_0000046267.
TOPO_DOM 1 96 Cytoplasmic. {ECO:0000255}.
TRANSMEM 97 117 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 118 121 Extracellular. {ECO:0000255}.
TRANSMEM 122 141 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 142 272 Cytoplasmic. {ECO:0000255}.
TRANSMEM 273 294 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 295 305 Extracellular. {ECO:0000255}.
TRANSMEM 306 328 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 329 700 Cytoplasmic. {ECO:0000255}.
TRANSMEM 701 719 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 720 735 Extracellular. {ECO:0000255}.
TRANSMEM 736 755 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 756 805 Cytoplasmic. {ECO:0000255}.
TRANSMEM 806 826 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 827 838 Extracellular. {ECO:0000255}.
TRANSMEM 839 855 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 856 899 Cytoplasmic. {ECO:0000255}.
COMPBIAS 566 571 Poly-Gly.
ACT_SITE 359 359 4-aspartylphosphate intermediate.
{ECO:0000250}.
METAL 615 615 Magnesium. {ECO:0000250}.
METAL 619 619 Magnesium. {ECO:0000250}.
MUTAGEN 669 669 M->I: In 3.3; low capacity to pump out
protons. {ECO:0000269|PubMed:7730265}.
SEQUENCE 899 AA; 98260 MW; F29DC853BDCF4396 CRC64;
MSAATEPTKE KPVNNQDSDD EDEDIDQLIE DLQSHHGLDD ESEDDEHVAA GSARPVPEEL
LQTDPSYGLT SDEVTKRRKK YGLNQMSEET ENLFVKFLMF FIGPIQFVME AAAILAAGLE
DWVDFGVICG LLFLNAAVGF IQEYQAGSIV DELKKTLANS AVVIRDGNLV EVPSNEVVPG
DILQLEDGVV IPADGRLVTE DCFIQIDQSA ITGESLAVDK RFGDSTFSSS TVKRGEAFMI
VTATGDSTFV GRAAALVNKA AAGSGHFTEV LNGIGTILLI LVIVTLLLVW VASFYRTNKI
VRILRYTLAI TIVGVPVGLP AVVTTTMAVG AAYLAKKQAI VQKLSAIESL AGVEILCSDK
TGTLTKNKLS LHEPYTVEGV DPDDLMLTAC LAASRKKKGL DAIDKAFLKS LISYPRAKAA
LTKYKLLEFH PFDPVSKKVT AIVESPEGER IICVKGAPLF VLKTVEEEHP IPEDVRENYE
NKVAELASRG FRALGVARKR GEGHWEILGV MPCMDPPRDD TAQTVNEARH LGLRVKMLTG
DAVGIAKETC RQLGLGTNIY NAERLGLGGG GDMPGSELAD FVENADGFAE VFPQHKYNVV
EILQQRGYLV AMTGDGVNDA PSLKKADTGI AVEGATDAAR SAADIVFLAP GLSAIIDALK
TSRQIFHRMY SYVVYRIALS LHLEIFLGLW IAILNRSLNI DLVVFIAIFA DVATLAIAYD
NAPYSPKPVK WNLRRLWGMS VILGIILAIG TWITLTTMFV PKGGIIQNFG SIDGVLFLQI
SLTENWLIFI TRAAGPFWSS IPSWQLSGAV LIVDIIATMF CLFGWWSQNW NDIVTVVRVW
IFSFGVFCVM GGAYYMMSES EAFDRFMNGK SRRDKPSGRS VEDFLMAMQR VSTQHEKEN


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