ID S7Z822_PENO1 Unreviewed; 992 AA.
AC S7Z822;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Plasma membrane ATPase {ECO:0000256|RuleBase:RU362083};
DE EC=7.1.2.1 {ECO:0000256|RuleBase:RU362083};
GN ORFNames=PDE_01674 {ECO:0000313|EMBL:EPS26735.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26735.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS26735.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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 {ECO:0000256|ARBA:ARBA00003417}.
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|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}.
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DR EMBL; KB644409; EPS26735.1; -; Genomic_DNA.
DR AlphaFoldDB; S7Z822; -.
DR STRING; 933388.S7Z822; -.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_0_1; -.
DR OrthoDB; 1058547at2759; -.
DR PhylomeDB; S7Z822; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
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 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:SF31; PLASMA MEMBRANE ATPASE-RELATED; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 2.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000019376};
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 119..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 379..406
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 737..758
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 764..788
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 800..818
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT TRANSMEM 916..940
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362083"
FT DOMAIN 78..147
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 109300 MW; 2C774FC37D2C3ADD CRC64;
MAERRISYAP DVENGDRHRD AGDVNDGSLD EYSALNRYIS TARDGRRGST SSAAALSTKQ
KKKPFWKFWA KEGDGVVEGW QCPDEWLETD LRSGLSSSDI EPRRKKCGWN ELVTEKTNIF
VQFIGYFRGP ILYVMELAVL LAAGLRDWID LGVIIGILML NALVGWYQEK QAADVVASLK
GDIAMRAIVV RNGQEEEILA RELVTGDIVV VEEGHVIPAD VRLICDYSKP EMFEAYKEYL
ISSQDDTLKE KAEDDDEDSR EVHQGVSLIA CDQSAITGES LAVDKYMADT CYYTTGCKRG
KAYGIVTATA RQSFVGKTAA LVQGAKDSGH FKAVMDNIGT SLLVLVMFWI LAAWIGGFFR
HLGIATPENS ENTLLRYTLI LLIIGVPVGL PVVTTTTLAV GAAYLAEQKA IVQKLTAIES
LAGVDILCSD KTGTLTANQL SIREPYVAEG VDVNWMMAVA AIASSHNVKN LDPIDKVTIL
TLRRYPKARE ILARNWVTEK YSPFDPVSKR ITTVCTCDGV RYICAKGAPK AILNMSECSE
EEAKLYRDKA TEFARRGFRS LGVAVQKEGE PWQLLGMYPM FDPPREDTAH TIAEAQVLGL
SVKMLTGDAI AIAKETCKML ALGTKVYDSE RLIHGGLAGS AQHDLVEKAD GFAEVFPEHK
YQVVEMLQQR GHLTAMTGDG VNDAPSLKKA DCGIAVEGST EAAQAAADIV FLAPGLSTIV
DAIKLARQIF QRMKAYIQYR IALCLHLEIY LVTSMIIINE TVRADLIVFI ALFADLATIA
VAYDNAHFEA RPVEWQLPKI WVISVILGVL LAAATWIVRG SLFLSNGGLI QNWGSPQEIL
FLEIALTENW LIFVTRGGKT WPSWQLVIAI FIVDVLATLF CLFGWLSGGE FEQTSPKDPA
YFTENGHVDI VTVVVIWAYS IGVTVIIAVA YYLLTIIPAL DNLGRKTRSK ADTKIENMIA
HLSKLAIEHE VDREGKSRYT LGARADDVEE DE
//
