ID A0A6A3WWC1_9STRA Unreviewed; 1376 AA.
AC A0A6A3WWC1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-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 ORFNames=PF001_g23000 {ECO:0000313|EMBL:KAE9283109.1}, PF002_g24248
GN {ECO:0000313|EMBL:KAE9192270.1}, PF004_g22718
GN {ECO:0000313|EMBL:KAE9187707.1}, PF005_g23214
GN {ECO:0000313|EMBL:KAE9180585.1}, PF006_g22331
GN {ECO:0000313|EMBL:KAE9102807.1}, PF007_g23340
GN {ECO:0000313|EMBL:KAE9079715.1}, PF009_g17608
GN {ECO:0000313|EMBL:KAE8932358.1}, PF010_g22664
GN {ECO:0000313|EMBL:KAE9079685.1};
OS Phytophthora fragariae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=53985 {ECO:0000313|EMBL:KAE9192270.1, ECO:0000313|Proteomes:UP000440367};
RN [1] {ECO:0000313|Proteomes:UP000429523, ECO:0000313|Proteomes:UP000433483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4 {ECO:0000313|EMBL:KAE9283109.1,
RC ECO:0000313|Proteomes:UP000437068}, BC-1
RC {ECO:0000313|EMBL:KAE9192270.1, ECO:0000313|Proteomes:UP000440367},
RC BC-23 {ECO:0000313|EMBL:KAE9187707.1,
RC ECO:0000313|Proteomes:UP000476176}, NOV-27
RC {ECO:0000313|EMBL:KAE9180585.1, ECO:0000313|Proteomes:UP000433483},
RC NOV-5 {ECO:0000313|EMBL:KAE9102807.1,
RC ECO:0000313|Proteomes:UP000440732}, NOV-71
RC {ECO:0000313|EMBL:KAE9079715.1, ECO:0000313|Proteomes:UP000441208},
RC NOV-9 {ECO:0000313|EMBL:KAE8932358.1,
RC ECO:0000313|Proteomes:UP000429523}, and ONT-3
RC {ECO:0000313|EMBL:KAE9079685.1, ECO:0000313|Proteomes:UP000488956};
RA Adams T.M., Armitage A.D., Sobczyk M.K., Bates H.J., Dunwell J.M.,
RA Nellist C.F., Harrison R.J.;
RT "Genomic investigation of the strawberry pathogen Phytophthora fragariae
RT indicates pathogenicity is determined by transcriptional variation in three
RT key races.";
RL Submitted (AUG-2018) 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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAE9192270.1}.
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DR EMBL; QXGF01001127; KAE8932358.1; -; Genomic_DNA.
DR EMBL; QXFX01002190; KAE9079685.1; -; Genomic_DNA.
DR EMBL; QXFZ01002190; KAE9079715.1; -; Genomic_DNA.
DR EMBL; QXGA01002159; KAE9102807.1; -; Genomic_DNA.
DR EMBL; QXGB01002182; KAE9180585.1; -; Genomic_DNA.
DR EMBL; QXGC01002320; KAE9187707.1; -; Genomic_DNA.
DR EMBL; QXGD01002187; KAE9192270.1; -; Genomic_DNA.
DR EMBL; QXGE01002296; KAE9283109.1; -; Genomic_DNA.
DR Proteomes; UP000429523; Unassembled WGS sequence.
DR Proteomes; UP000433483; Unassembled WGS sequence.
DR Proteomes; UP000437068; Unassembled WGS sequence.
DR Proteomes; UP000440367; Unassembled WGS sequence.
DR Proteomes; UP000440732; Unassembled WGS sequence.
DR Proteomes; UP000441208; Unassembled WGS sequence.
DR Proteomes; UP000476176; Unassembled WGS sequence.
DR Proteomes; UP000488956; Unassembled WGS sequence.
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:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
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; 1.
DR PANTHER; PTHR24092:SF214; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_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:UP000433483};
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 370..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 421..440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 967..985
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 997..1020
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1050..1072
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1087..1105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1117..1138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1158..1177
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 96..161
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 936..1187
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 41..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1376 AA; 151978 MW; 2C1359EE596D240A CRC64;
MAAKRSTSRI FRGSRVEDEV ALCSSVAPAG VDNALGSSTS GYNTLGSPAP VLQSPRQSRS
QQLPDEDELV DYATPVSVSA TAAAAGSDAN DSLREVYINY APGNAVFDKC SNVVVTSKYS
LVTFVPKFLR ESFSKVANFF FLMVCVLQSI PSISNTYGYP TNAPVLFFVI SIDAVFAVME
DLRRHKSDSE ANGATCHVIQ DGHVVDRKWA DIKVGDFLQI RNREVIPADV LVLAVSEPVG
EPPSGICYVE TKSLDGETNL KLRQAVAATM SSLANAAELA LLRGVVKCEQ PNPHINKFAG
KVEVTVGDGC GVEVMPLSVK NVLLRGCNLR NTDWAFGLVI NTGNDTKIMQ SASAAPSKWS
DLMLHINRMI VMLCMGLFVA CAVAATCYIT WQYDIVRNTW YIQLTEAERT RTRFVAFIQM
LFYYFLLLYQ VIPISLYVSM TSVKFLQSRF MAWDLEMYDA ETDTPAIVRT MELNEELGQI
SYVFSDKTGT LTCNVMEFRK CSINGTSYGS GITEIGRAAL VRAGKPIPPE PKLDPSIKRI
PFVNFVDKAL FDGMKGSAGD EQKHKIMQFF EHLAVCHTVI PEKLESGEVR LSASSPDEQA
LVAGAAFAGF KFESRSVGTA TVEVLGQRVS YEILDVLEFN STRKRMSVVV RKPSGELLLY
TKGADMMIYQ RLKDDPAMMK LKNITRDHME KYADDGLRTL ALAMKPLDER WFQQWKMRFD
DAQGNVAEID RRKDGKPNAI DALMEEIEEG LELIGATAIE DKLQDGVPQC LANLTRAGIK
VWMLTGDKEE TAINISYACS LLDNSIQQVI VNATTCPDEA AIRAKLNAAA REFMENAKGM
AGGGEREISL IIDGEALEMA LRPGTAPHLL SFAKLCRAVI CNRVSPAQKA EMVKLVRDNI
TTVRTLAIGD GANDVAMIQA AHVGVGISGQ EGMQAVNSSD YAIAQFRFLE RLLLVHGRWN
YIRISKLVLY MFYKNITLVL AQYWYGYLSG ASGSKMYWEI GVQLYNVAFT GLPIVVVGVL
DKDLPAPFSL EYPDLYRRGP ERFYFNMYTF GRWIAAAFYE SMIIFVVMSY GFNASEKAAG
SESRVEFGMV AFSLTVLIVN MKIWMIADRW TVLSFSLWFG SVMSWFVFAA IGTETPYFAT
YKVGYDEFGA FAPTFKTWGY FLVLIMGCSL ALGRHIAYNL YQRTFHPDLA QLLQESMGGA
AQHKYQRRLT INHSEEQTLS MSLDDVHTTG YLSDFGHTDA EILKAQHPQS FTAATLYEQP
KKSSGSRTSA PQSAASASVS SGVTESYSAS VFSESISEDA TWERVPAKMF RPTTSRRNMG
FAFSCDEETT LAESYIASNS LPRSDAISTA MRNSTASSTG GASARRVSMG RVRLLS
//
