P49380 (PMA1_KLULA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Plasma membrane ATPase
EC=3.6.3.6

Alternative name(s):
Proton pump

Gene names

Name:	PMA1
Ordered Locus Names:	KLLA0A09031g

Organism

Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) [Complete proteome]

Taxonomic identifier

284590 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Kluyveromyces

Protein attributes

Sequence length	899 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 + H2O + H+(In) = ADP + phosphate + H+(Out).
Enzyme regulation	Activated by high pH or also by potassium ions when the medium pH is low.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily. [View classification]

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 899	899	Plasma membrane ATPase		PRO_0000046267
Regions
	Topological domain	1 – 96	96	Cytoplasmic Potential
	Transmembrane	97 – 117	21	Helical; Name=1; Potential
	Topological domain	118 – 121	4	Extracellular Potential
	Transmembrane	122 – 141	20	Helical; Name=2; Potential
	Topological domain	142 – 272	131	Cytoplasmic Potential
	Transmembrane	273 – 294	22	Helical; Name=3; Potential
	Topological domain	295 – 305	11	Extracellular Potential
	Transmembrane	306 – 328	23	Helical; Name=4; Potential
	Topological domain	329 – 700	372	Cytoplasmic Potential
	Transmembrane	701 – 719	19	Helical; Name=5; Potential
	Topological domain	720 – 735	16	Extracellular Potential
	Transmembrane	736 – 755	20	Helical; Name=6; Potential
	Topological domain	756 – 805	50	Cytoplasmic Potential
	Transmembrane	806 – 826	21	Helical; Name=7; Potential
	Topological domain	827 – 838	12	Extracellular Potential
	Transmembrane	839 – 855	17	Helical; Name=8; Potential
	Topological domain	856 – 899	44	Cytoplasmic Potential
	Compositional bias	566 – 571	6	Poly-Gly
Sites
	Active site	359	1	4-aspartylphosphate intermediate By similarity
	Metal binding	615	1	Magnesium By similarity
	Metal binding	619	1	Magnesium By similarity
Experimental info
	Mutagenesis	669	1	M → I in 3.3; low capacity to pump out protons. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49380 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: F29DC853BDCF4396	FASTA	899	98,260
	10 20 30 40 50 60 MSAATEPTKE KPVNNQDSDD EDEDIDQLIE DLQSHHGLDD ESEDDEHVAA GSARPVPEEL 70 80 90 100 110 120 LQTDPSYGLT SDEVTKRRKK YGLNQMSEET ENLFVKFLMF FIGPIQFVME AAAILAAGLE 130 140 150 160 170 180 DWVDFGVICG LLFLNAAVGF IQEYQAGSIV DELKKTLANS AVVIRDGNLV EVPSNEVVPG 190 200 210 220 230 240 DILQLEDGVV IPADGRLVTE DCFIQIDQSA ITGESLAVDK RFGDSTFSSS TVKRGEAFMI 250 260 270 280 290 300 VTATGDSTFV GRAAALVNKA AAGSGHFTEV LNGIGTILLI LVIVTLLLVW VASFYRTNKI 310 320 330 340 350 360 VRILRYTLAI TIVGVPVGLP AVVTTTMAVG AAYLAKKQAI VQKLSAIESL AGVEILCSDK 370 380 390 400 410 420 TGTLTKNKLS LHEPYTVEGV DPDDLMLTAC LAASRKKKGL DAIDKAFLKS LISYPRAKAA 430 440 450 460 470 480 LTKYKLLEFH PFDPVSKKVT AIVESPEGER IICVKGAPLF VLKTVEEEHP IPEDVRENYE 490 500 510 520 530 540 NKVAELASRG FRALGVARKR GEGHWEILGV MPCMDPPRDD TAQTVNEARH LGLRVKMLTG 550 560 570 580 590 600 DAVGIAKETC RQLGLGTNIY NAERLGLGGG GDMPGSELAD FVENADGFAE VFPQHKYNVV 610 620 630 640 650 660 EILQQRGYLV AMTGDGVNDA PSLKKADTGI AVEGATDAAR SAADIVFLAP GLSAIIDALK 670 680 690 700 710 720 TSRQIFHRMY SYVVYRIALS LHLEIFLGLW IAILNRSLNI DLVVFIAIFA DVATLAIAYD 730 740 750 760 770 780 NAPYSPKPVK WNLRRLWGMS VILGIILAIG TWITLTTMFV PKGGIIQNFG SIDGVLFLQI 790 800 810 820 830 840 SLTENWLIFI TRAAGPFWSS IPSWQLSGAV LIVDIIATMF CLFGWWSQNW NDIVTVVRVW 850 860 870 880 890 IFSFGVFCVM GGAYYMMSES EAFDRFMNGK SRRDKPSGRS VEDFLMAMQR VSTQHEKEN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Miranda M., Ramirez J., Pena A., Coria R. J. Bacteriol. 177:2360-2367(1995) [PubMed: 7730265] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF MET-669. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
[2]	"Genome evolution in yeasts." 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. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L37875 Genomic DNA. Translation: AAA69688.1. CR382121 Genomic DNA. Translation: CAH02983.1.
RefSeq	XP_451395.1. XM_451395.1.
3D structure databases
ProteinModelPortal	P49380.
SMR	P49380. Positions 28-897.
ModBase	Search...
Protein-protein interaction databases
STRING	P49380.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2896449.
GenomeReviews	Gene locus KLLA0A09031g in contig CR382121_GR.
KEGG	kla:KLLA0A09031g.
Phylogenomic databases
eggNOG	fuNOG06156.
HOGENOM	HBG706356.
OMA	TQHEKEN.
OrthoDB	EOG4M68RQ.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006534. ATPase_P-typ_PM_proton-efflux. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 2 hits. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
KO	K01535.
PANTHER	PTHR24093:SF61. PTHR24093:SF61. 1 hit.
Pfam	PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01647. ATPase-IIIA_H. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PMA1_KLULA

Accession

Primary (citable) accession number: P49380

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program