PMA1_KLULA
ID PMA1_KLULA Reviewed; 899 AA.
AC P49380;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Plasma membrane ATPase;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump;
GN Name=PMA1; OrderedLocusNames=KLLA0A09031g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF MET-669.
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=7730265; DOI=10.1128/jb.177.9.2360-2367.1995;
RA Miranda M., Ramirez J., Pena A., Coria R.;
RT "Molecular cloning of the plasma membrane H(+)-ATPase from Kluyveromyces
RT lactis: a single nucleotide substitution in the gene confers ethidium
RT bromide resistance and deficiency in K+ uptake.";
RL J. Bacteriol. 177:2360-2367(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen
CC ion pump. The proton gradient it generates drives the active transport
CC of nutrients by H(+)-symport. The resulting external acidification
CC and/or internal alkinization may mediate growth responses.
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 -!- ACTIVITY REGULATION: Activated by high pH or also by potassium ions
CC when the medium pH is low.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
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DR EMBL; L37875; AAA69688.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH02983.1; -; Genomic_DNA.
DR RefSeq; XP_451395.1; XM_451395.1.
DR AlphaFoldDB; P49380; -.
DR SMR; P49380; -.
DR STRING; 28985.XP_451395.1; -.
DR PRIDE; P49380; -.
DR EnsemblFungi; CAH02983; CAH02983; KLLA0_A09031g.
DR GeneID; 2896449; -.
DR KEGG; kla:KLLA0_A09031g; -.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_0_1; -.
DR InParanoid; P49380; -.
DR OMA; FTIFGWF; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR CDD; cd02076; P-type_ATPase_H; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00690; Cation_ATPase_N; 1.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Hydrogen ion transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..899
FT /note="Plasma membrane ATPase"
FT /id="PRO_0000046267"
FT TOPO_DOM 1..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..141
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..294
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..328
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 701..719
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..735
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..755
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 756..805
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 806..826
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 827..838
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 839..855
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 856..899
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 619
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 669
FT /note="M->I: In 3.3; low capacity to pump out protons."
FT /evidence="ECO:0000269|PubMed:7730265"
SQ 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
