ID A0A5S6PN58_BRUMA Unreviewed; 1473 AA.
AC A0A5S6PN58;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN Name=Bma-tat-2 {ECO:0000313|WBParaSite:Bm4626b.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|Proteomes:UP000006672, ECO:0000313|WBParaSite:Bm4626b.1};
RN [1] {ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|WBParaSite:Bm4626b.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A5S6PN58; -.
DR STRING; 6279.A0A5S6PN58; -.
DR EnsemblMetazoa; Bm4626b.1; Bm4626b.1; WBGene00224887.
DR WBParaSite; Bm4626b.1; Bm4626b.1; WBGene00224887.
DR InParanoid; A0A5S6PN58; -.
DR Proteomes; UP000006672; 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 CDD; cd02073; P-type_ATPase_APLT_Dnf-like; 1.
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:SF150; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000006672};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 348..373
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 406..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 989..1007
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1019..1039
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1068..1093
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1105..1125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1137..1157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1178..1200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT DOMAIN 92..156
FT /note="P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16209"
FT DOMAIN 955..1205
FT /note="P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16212"
FT REGION 1226..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1473 AA; 167722 MW; 90D61D948DEFC46E CRC64;
MQGATWILLL LLLLLLEPVL VIALIMMSDN SEYLSKKQPN ITVKSSSGSF LNSWLMSLTK
LFTCRSSANS GRKHDQRGSN QFTTPVTERI LRANDREFNE QFKYADNYIR TSKYNLITFV
PLNLLEQFQR LANFYFLILM ILQLIPWISS IAWYSTAIPL FFVLIFSGAK DAYDDIQRHQ
SDNQVNNRIS YVVRNGQLIA ERWMNVKVGD VIRMENDQFV AADLLLLSTS EPHGLCYIET
SELDGETNLK VRQALPETSI MGDKLLQISE FEGQIHCELP NNKLNQFEGR LHYNGNILPL
DNGKTLLRGC VLRNTRWCYG VVIFAGKDTK LMMNSGKTKC KRTSLDHFLN ILIMGIVVFL
IAMCLICTTL CGIREWTIER HFTIHLNLDG SVIPDHMEQS PEQTSILSFL MFFSYLILLN
TVVPISLYVS VEIIRFVHSM WINFDTEMYY EKGDTAARAR TTTLNEELGQ VQYIFSDKTG
TLTQNTMVFR KCSINGHSYG DVYDANGKII DVTEKTPTID FSKNRWFEPN FKFYDQKLMK
DTTKGLHEVA EFWRLLALCH TSMPERKNGR LEYQAQSPDE AALTSAARNF GYVFKSRTAQ
TITLEIAGSE EVYDLLAILD FNNVRKRMSV IVRNPLGELI LYCKGADTII LDRISHDTAP
LLKSATIQHL DKFAADGFRT LCLAYKKIST DVFNKWHEQQ KEAAVALTNR QEQLDRIYDE
LEQEMILLGA TAIEDKLQDG VPDTIAELAR ANIKIWILTG DKQETAINIG YSCNLLTENL
REVFVIDGET EREVEVQLKD VRRRIEQTLG PDALLDDGKL TSQYINDAIT ANGNLQSDGT
KNLAFIHESN MEIQDHLSAN EWKKLEGYAL IVNGPSLTYA LKRELERTFL DIGCLCRAVV
CCRVTPLQKA MVVDLVKRNK KAITLAVGDG ANDVSMIKTA HIGVGISGQE GMQAVLASDY
SIGQFRYLKR LLLVHGRWSY FRMTKFLRYF FYKNFAFTLT HFWYSFFCGY SAQSIYSPVL
IACYNLFFTS LPVLAMGIFD QDLDDVCSMK YAKLYIPGQY NLFFNMRIFI YSVLHGMISS
LVIFFVPYGI LYNGVDSAGR DFNDYSLLAF TCFTSLIIVV TGQIAFDTNY WTIFNHIVIW
GSVIFYFCLS YILYEALPIK LVSKFESAQS YGVMQRAFIS LQFWLSLLMV SVILLLPVLV
NRFFWLDTHP TYADRLRMQQ KLLTSEEDEK PPSITTTTSH STTGRGRRTS LRSGYAFSHQ
QGFGDLIIKG ELFKQVEQLI NTGSSPQKIV SPFRQLAEKG TTTVLTPKTL LSQRNNKIAP
LEQAKNESKY INHIESGPEQ LTKISKEQNA CSTNNSSDGG IDMMKSSQFL HKIIVNDDEV
PFKHSDDKTY NKKISRKQQK RSASLILGSI NRTTLTSHPS YTNVKRDTFP QSFQSATYPN
SLNSESTLNS LNACVDIIGT KSTAYKTLDE TKL
//
