ID A0A4P6XMH7_9ASCO Unreviewed; 1169 AA.
AC A0A4P6XMH7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=MPUL0C04380 {ECO:0000313|EMBL:QBM88470.1};
GN ORFNames=METSCH_C04380 {ECO:0000313|EMBL:QBM88470.1};
OS Metschnikowia aff. pulcherrima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=2163413 {ECO:0000313|EMBL:QBM88470.1, ECO:0000313|Proteomes:UP000292447};
RN [1] {ECO:0000313|Proteomes:UP000292447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APC 1.2 {ECO:0000313|Proteomes:UP000292447};
RA Gore-Lloyd D., Sumann I., Brachmann A.O., Schneeberger K.,
RA Ortiz-Merino R.A., Moreno-Beltran M., Schlaefli M., Kirner P.,
RA Santos Kron A., Wolfe K.H., Piel J., Ahrens C.H., Henk D., Freimoser F.M.;
RT "Snf2 controls pulcherriminic acid biosynthesis and connects pigmentation
RT and antifungal activity of the yeast Metschnikowia pulcherrima.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00034036,
CC ECO:0000256|RuleBase:RU362033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000256|ARBA:ARBA00035097};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000256|ARBA:ARBA00008109,
CC ECO:0000256|RuleBase:RU362033}.
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; CP034458; QBM88470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P6XMH7; -.
DR STRING; 2163413.A0A4P6XMH7; -.
DR Proteomes; UP000292447; Chromosome iii.
DR GO; GO:0016020; C: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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IEA:RHEA.
DR GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR GO; GO:0045332; P:phospholipid translocation; IEA:UniProt.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01652; ATPase-Plipid; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24092:SF5; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362033};
KW Magnesium {ECO:0000256|RuleBase:RU362033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362033};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362033};
KW Reference proteome {ECO:0000313|Proteomes:UP000292447};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362033};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362033};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362033}.
FT TRANSMEM 210..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 233..251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 440..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 468..487
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1042..1059
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1071..1093
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1100..1119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1131..1151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 182..233
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 930..1160
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 130927 MW; 2664C62CB941BBBA CRC64;
MAKPDSRTLR SASPNGADTF DEEFENSLDK ALHSASSNYF NWTGRRGSLG ANLRLALGIL
LETLNAPNQP SIGTSFDRNS DSFDRSWGSD VNPLIGGGEI TGNTYLHGSN DPNGPDYSRN
SLIHRMGRFL QSLLGLYRFL RSQVSRELQQ QQTHADLQHF SGDNTASAAV LEERMVSPQN
SHQKQPVLNA VLNAKYNPVT FVPVILYEQF KFFFNLYFLL VALSQIVPQL RIGYLLSYIV
PLAFVLLVTM LKEAGDDIAR RRRDIEQNNE QYEVLNRSFL LSADVSLVPA KNLKVGDLVR
LHKGMRVPAD MVLLHSSDSN GEAFIKTDQL DGETDWKLRV ACPVTQSTPD VAQISERVSL
VVGRPEKSIH SFQGKLVYHS PTGTDRTVPL SVDQTLWANT VLASGTALGI IIYTGVETRQ
LLNTTMSGVK TGLLEIEINS LLKILCVTVF LLSVVLVLAQ RFPPGGTWYI DILRFLILFS
SIIPVSLRVN LDLAKSVYAS QIQKDNDIPA TIVRTSTIPE DLGRIEYLLS DKTGTLTQND
MEMKKLHLGA VCYAGETLDI VSENVSKMFV HEKGGNTTKR RDLATKVCDF ALVLALCHNV
TPSEDDGVIS YQAASPDEVA IVKFCEQIGL RLLKRDRHSI TLLHLASLQE LLFQILYIFP
FNSDTKRMGI VVKDTQKNEI WFMEKGADTV MTRIVNTSDW LDEETANMAR EGLRTLVIGR
KKLGTSVFEE FTKAYEHASL SMQERDSNMQ RVVEKYLETN VELLGLTGVE DKLQKNVKQS
IELLRNAGVK IWMLTGDKVE TAKCVAISAK LISRGQFVHQ ITKVTSPEMA MSHLDQITNT
ANSVLLIDGE SLAMYMKHFS QEFFEMCILL PAVIACRCTP QQKADIALAI KKATGKRVCC
IGDGGNDVSM IQCADVGVGI VGKEGKQASL SADFSIDQFH FLLKLLLWHG RNSYKRSAKL
AQFVIHRGLI ISVAQAIYSI SSHFEPLALY QGWLMVGYST LYTMAPVFSL TLDTDVDVRL
TKLYPELYKE LTLGKSLSYR SFFMWVAISL FQGSVIQLLS QSFQTLSENK FPAMVSISFT
TLILNELFMV AFTIRTWNKI MFATIVITFM IYVLLIPFLK EYFDLDYITS VSFLWQSALI
LVTSLFPVWL VRTLSRKLRP PSYAKVQQH
//
