ID A0A2H1A3E1_CANAR Unreviewed; 1135 AA.
AC A0A2H1A3E1; A0A5Q7YDF9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Phospholipid-transporting ATPase {ECO:0000256|RuleBase:RU362033};
DE EC=7.6.2.1 {ECO:0000256|RuleBase:RU362033};
GN ORFNames=B9J08_000018 {ECO:0000313|EMBL:PIS58572.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS58572.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS58572.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS58572.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
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 -!- 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:PIS58572.1}.
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DR EMBL; PEKT02000001; PIS58572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H1A3E1; -.
DR STRING; 498019.A0A2H1A3E1; -.
DR EnsemblFungi; B9J08_000018-t37_1; B9J08_000018-t37_1-p1; B9J08_000018.
DR VEuPathDB; FungiDB:B9J08_000018; -.
DR VEuPathDB; FungiDB:CJI96_0001455; -.
DR VEuPathDB; FungiDB:CJI97_000025; -.
DR VEuPathDB; FungiDB:CJJ07_003179; -.
DR VEuPathDB; FungiDB:CJJ09_001979; -.
DR VEuPathDB; FungiDB:QG37_05717; -.
DR OMA; IAITTWH; -.
DR OrthoDB; 275833at2759; -.
DR Proteomes; UP000230249; 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: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; 3.
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; PF00702; Hydrolase; 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:UP000230249};
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 409..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 433..452
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 958..978
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1008..1025
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1037..1054
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1066..1085
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
FT TRANSMEM 1097..1116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362033"
SQ SEQUENCE 1135 AA; 127700 MW; 172E0A125EE6D0EC CRC64;
MSENPWPTSG RLGSPSLHDS MDDFENSLDR AIKSATNNFF DYKPQSREGS QGSIAIPMST
LNPQGSAEHD DDNDSLPLMT GHDSTMSLPS SPTVASHSRG GLMRRALGLF RTIKEEVSRE
ITDRSLVNNP DPESDLGSER YVSPRNSSKK FPSNAISNAK YNPITFIPLI LYEQFKFFFN
LYFLLVALSQ IIPQLRIGYL SSYIVPLAFV LTVTMMKEAG DDIARRKRDS EQNNERYEVL
NRQSPITQDV SMVQSKNLKV GDLVRLHKDR RIPADMILLQ SSDANGEAFI KTDQLDGETD
WKLRVACNLT DSVDDINTLI NHVSLIVDKP TKSIHHFNGK LIYHQGSSNN KSVPLTIDQT
LWANTVLASG TAIGIVIYTG VETRQSMNTT MSGVKTGLLE LEINSLSKIL CVTVFLLSVI
LVMAHGFPLK KTWYIDILRF LILFSTIIPV SLRVNLDLAK SVYASHIQKD QEIPNTIVRT
STIPEDLGRI EYLLSDKTGT LTQNDMEMKK LHLGSICYAG DTFDIVADYI SKLLFQEDSG
SFAAKRKDMT TKVCDLALVL ALCHNVTPTE EDGQLSYQAA SPDEIAIVRF CEQVGLRLFK
RDRSNISLLH LATGKELKFE ILYNFPFNSD TKRMGIIVKD IERDEITFME KGADTVMANI
VMTTDWLDEE ISNMARDGLR TLVIGRKRLN AGLFQLFSKD YEEASLSMTS RDAQMQRVVS
KYLETDVELL GITGVEDKLQ KDVKTSIELL RNAGIKIWML TGDKVETAKC VAISAKLIAR
GQYVHQITKV HIAETAMSSL DYLINNFNSC LLIDGESIAF YMKHFRREFM EIVLRLPAVI
ACRCTPQQKA DIAMAIKEFT GRRVCCIGDG GNDVSMIQCA DVGVGIVGKE GKQASLSADF
SIDQFHFLSK LLLWHGRNSY KRSAKLGQFI IHRGLIISVA QAIYSISSKF EPLALYQGWL
MVGYSTLYTM APVFSLTLDR DIDERLTKMY PELYKELTLG KSLSYKTFFM WVVISLYQGS
VIQVLSQMFQ SLDTEKFLAM VTLSFGALIL NELMMVGMTI NTWNKTMVTT IVVTLLIYIG
SIPFLTEYLD LDYITDFSYY WQTALVLAVS LFPVWLTQTV NRKLRPPTYA KVQQD
//
