ID SPF1_YEAST Reviewed; 1215 AA.
AC P39986; D3DLL8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 207.
DE RecName: Full=Endoplasmic reticulum transmembrane helix translocase {ECO:0000305};
DE EC=7.4.2.- {ECO:0000269|PubMed:32973005};
DE AltName: Full=Complexed with DOR1 protein 1 {ECO:0000303|PubMed:12058017};
DE AltName: Full=Endoplasmic reticulum P5A-ATPase {ECO:0000303|PubMed:32973005};
DE AltName: Full=Sensitivity to the P.farinosa killer toxin protein 1 {ECO:0000303|PubMed:10361284};
GN Name=SPF1 {ECO:0000303|PubMed:10361284, ECO:0000312|SGD:S000000757};
GN Synonyms=COD1 {ECO:0000303|PubMed:12058017}; OrderedLocusNames=YEL031W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=10361284; DOI=10.1046/j.1365-2958.1999.01400.x;
RA Suzuki C., Shimma Y.;
RT "P-type ATPase spf1 mutants show a novel resistance mechanism for the
RT killer toxin SMKT.";
RL Mol. Microbiol. 32:813-823(1999).
RN [4]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12058017; DOI=10.1083/jcb.200203052;
RA Cronin S.R., Rao R., Hampton R.Y.;
RT "Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+
RT homeostasis.";
RL J. Cell Biol. 157:1017-1028(2002).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-936, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP ATPASE ACTIVITY, ACTIVE SITE, COFACTOR, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-487.
RX PubMed=22745129; DOI=10.1074/jbc.m112.363465;
RA Corradi G.R., de Tezanos Pinto F., Mazzitelli L.R., Adamo H.P.;
RT "Shadows of an absent partner: ATP hydrolysis and phosphoenzyme turnover of
RT the Spf1 (sensitivity to Pichia farinosa killer toxin) P5-ATPase.";
RL J. Biol. Chem. 287:30477-30484(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22918956; DOI=10.1091/mbc.e11-12-0994;
RA Krumpe K., Frumkin I., Herzig Y., Rimon N., Oezbalci C., Bruegger B.,
RA Rapaport D., Schuldiner M.;
RT "Ergosterol content specifies targeting of tail-anchored proteins to
RT mitochondrial outer membranes.";
RL Mol. Biol. Cell 23:3927-3935(2012).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP ATPASE ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ASP-487.
RX PubMed=24392018; DOI=10.1371/journal.pone.0085519;
RA Cohen Y., Megyeri M., Chen O.C., Condomitti G., Riezman I.,
RA Loizides-Mangold U., Abdul-Sada A., Rimon N., Riezman H., Platt F.M.,
RA Futerman A.H., Schuldiner M.;
RT "The yeast p5 type ATPase, spf1, regulates manganese transport into the
RT endoplasmic reticulum.";
RL PLoS ONE 8:E85519-E85519(2013).
RN [12]
RP ATPASE ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, ACTIVE SITE,
RP AND MUTAGENESIS OF ASP-487.
RX PubMed=30785834; DOI=10.1091/mbc.e18-06-0365;
RA Soerensen D.M., Holen H.W., Pedersen J.T., Martens H.J., Silvestro D.,
RA Stanchev L.D., Costa S.R., Guenther Pomorski T., Lopez-Marques R.L.,
RA Palmgren M.;
RT "The P5A ATPase Spf1p is stimulated by phosphatidylinositol 4-phosphate and
RT influences cellular sterol homeostasis.";
RL Mol. Biol. Cell 30:1069-1084(2019).
RN [13]
RP ATPASE ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-487.
RX PubMed=32353073; DOI=10.1371/journal.pone.0232476;
RA Corradi G.R., Mazzitelli L.R., Petrovich G.D., Grenon P., Soerensen D.M.,
RA Palmgren M., de Tezanos Pinto F., Adamo H.P.;
RT "Reduction of the P5A-ATPase Spf1p phosphoenzyme by a Ca2+-dependent
RT phosphatase.";
RL PLoS ONE 15:e0232476-e0232476(2020).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM
RP AND NON-HYDROLYZABLE ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND DOMAIN.
RX PubMed=32973005; DOI=10.1126/science.abc5809;
RA McKenna M.J., Sim S.I., Ordureau A., Wei L., Harper J.W., Shao S., Park E.;
RT "The endoplasmic reticulum P5A-ATPase is a transmembrane helix dislocase.";
RL Science 369:0-0(2020).
CC -!- FUNCTION: Endoplasmic reticulum translocase required to remove
CC mitochondrial transmembrane proteins mistargeted to the endoplasmic
CC reticulum (PubMed:22918956, PubMed:32973005). Acts as a dislocase that
CC mediates the ATP-dependent extraction of mislocalized mitochondrial
CC transmembrane proteins from the endoplasmic reticulum membrane
CC (PubMed:32973005). Specifically binds mitochondrial tail-anchored
CC transmembrane proteins: has an atypically large substrate-binding
CC pocket that recognizes and binds moderately hydrophobic transmembranes
CC with short hydrophilic lumenal domains (PubMed:32973005).
CC {ECO:0000269|PubMed:22918956, ECO:0000269|PubMed:32973005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-with a C-terminal TM segment(out) + ATP + H2O =
CC [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:66168, Rhea:RHEA-COMP:16963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:90782, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:32973005};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:22745129, ECO:0000269|PubMed:32973005};
CC -!- ACTIVITY REGULATION: The ATPase activity is stimulated by
CC phosphatidylinositol 4-phosphate (PI4P). {ECO:0000269|PubMed:30785834}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12058017, ECO:0000269|PubMed:22745129,
CC ECO:0000269|PubMed:24392018, ECO:0000269|PubMed:30785834}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:32973005}. Note=Localizes to
CC endoplasmic reticulum regions devoid of phosphatidylinositol 4-
CC phosphate (PI4P) hydrolytic machinery. {ECO:0000269|PubMed:30785834}.
CC -!- DOMAIN: Contains a large substrate-binding pocket that recognizes
CC alpha-helical transmembranes, which alternately faces the endoplasmic
CC reticulum lumen and cytosol, while remaining accessible to the lipid
CC bilayer through a lateral opening (PubMed:32973005). The translocase
CC alternates between two conformations: inward-open (E1) and outward-open
CC (E2) states (PubMed:32973005). Undergoes a series of conformational
CC changes with ATP-binding, phosphorylation of the Asp active site and
CC subsequent dephosphorylation in a Post-Albers cycle (i.e., E1 -> E1-ATP
CC -> E1P-ADP -> E1P -> E2P -> E2-Pi -> E1) (PubMed:32973005). A substrate
CC transmembrane helix with a short, preferentially positively charged
CC lumenal segment binds to the outward-open pocket and the E2P-to-E1
CC transition flips the transmembrane by a switch from the outward-open to
CC inward-open conformation (PubMed:32973005).
CC {ECO:0000269|PubMed:32973005}.
CC -!- DISRUPTION PHENOTYPE: Impaired mitochondrial transmembrane tail-
CC anchored protein localization, characterized by mitochondrial
CC transmembrane tail-anchored protein accumulation at the endoplasmic
CC reticulum (PubMed:22918956). In addition, a wide spectrum of phenotypes
CC is observed, including induction of the endoplasmic reticulum unfolded
CC protein response, defects in lipid and sterol homeostasis, and
CC dysregulated protein N-glycosylation, topogenesis and turnover
CC (PubMed:12058017, PubMed:22918956, PubMed:24392018).
CC {ECO:0000269|PubMed:12058017, ECO:0000269|PubMed:22918956,
CC ECO:0000269|PubMed:24392018}.
CC -!- MISCELLANEOUS: Present with 1870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to mediate ion transport such as calcium
CC or manganese (PubMed:12058017, PubMed:24392018). However, different
CC publications have shown that it does not act as an ion transporter
CC (PubMed:22745129, PubMed:32353073, PubMed:32973005). Specifically binds
CC moderately hydrophobic transmembrane with short hydrophilic lumenal
CC domains that misinsert into the endoplasmic reticulum
CC (PubMed:32973005). {ECO:0000269|PubMed:12058017,
CC ECO:0000269|PubMed:22745129, ECO:0000269|PubMed:24392018,
CC ECO:0000269|PubMed:32353073, ECO:0000269|PubMed:32973005}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Wrong place - Issue 234 of
CC March 2021;
CC URL="https://web.expasy.org/spotlight/back_issues/234/";
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DR EMBL; U18530; AAB64508.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07622.1; -; Genomic_DNA.
DR PIR; S50428; S50428.
DR RefSeq; NP_010883.3; NM_001178846.3.
DR PDB; 6XMP; EM; 3.50 A; A=1-1215.
DR PDB; 6XMQ; EM; 3.70 A; A=1-1215.
DR PDB; 6XMS; EM; 3.40 A; A=1-1215.
DR PDB; 6XMT; EM; 3.30 A; A=1-1215.
DR PDB; 6XMU; EM; 3.30 A; A=1-1215.
DR PDBsum; 6XMP; -.
DR PDBsum; 6XMQ; -.
DR PDBsum; 6XMS; -.
DR PDBsum; 6XMT; -.
DR PDBsum; 6XMU; -.
DR AlphaFoldDB; P39986; -.
DR SMR; P39986; -.
DR BioGRID; 36698; 499.
DR DIP; DIP-6637N; -.
DR IntAct; P39986; 3.
DR STRING; 4932.YEL031W; -.
DR TCDB; 3.A.3.10.3; the p-type atpase (p-atpase) superfamily.
DR CarbonylDB; P39986; -.
DR iPTMnet; P39986; -.
DR MaxQB; P39986; -.
DR PaxDb; 4932-YEL031W; -.
DR PeptideAtlas; P39986; -.
DR EnsemblFungi; YEL031W_mRNA; YEL031W; YEL031W.
DR GeneID; 856681; -.
DR KEGG; sce:YEL031W; -.
DR AGR; SGD:S000000757; -.
DR SGD; S000000757; SPF1.
DR VEuPathDB; FungiDB:YEL031W; -.
DR eggNOG; KOG0209; Eukaryota.
DR GeneTree; ENSGT00550000075064; -.
DR HOGENOM; CLU_001828_4_1_1; -.
DR InParanoid; P39986; -.
DR OMA; WYYSLFN; -.
DR OrthoDB; 6047at2759; -.
DR BioCyc; YEAST:G3O-30153-MONOMER; -.
DR Reactome; R-SCE-936837; Ion transport by P-type ATPases.
DR BioGRID-ORCS; 856681; 0 hits in 10 CRISPR screens.
DR PRO; PR:P39986; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39986; Protein.
DR GO; GO:0005801; C:cis-Golgi network; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140567; F:membrane protein dislocase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0140569; P:extraction of mislocalized protein from ER membrane; IDA:UniProtKB.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:SGD.
DR GO; GO:0030026; P:intracellular manganese ion homeostasis; IMP:SGD.
DR GO; GO:0034214; P:protein hexamerization; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043335; P:protein unfolding; IDA:UniProtKB.
DR GO; GO:0055092; P:sterol homeostasis; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd07543; P-type_ATPase_cation; 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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047820; P5A-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Endoplasmic reticulum; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1215
FT /note="Endoplasmic reticulum transmembrane helix
FT translocase"
FT /id="PRO_0000046349"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 28..43
FT /note="Helical; Name=TMa"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 44..56
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 57..76
FT /note="Helical; Name=TMb"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 77..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 189..216
FT /note="Helical; Name=TM1"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 217
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 218..246
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 247..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 396..425
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 426..427
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 428..442
FT /note="Helical; Name=TM4a"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 446..464
FT /note="Helical; Name=TM4b"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 465..971
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 972..1011
FT /note="Helical; Name=TM5"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 1012..1017
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 1018..1035
FT /note="Helical; Name=TM6"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 1036..1055
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 1056..1084
FT /note="Helical; Name=TM7"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 1085..1099
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 1100..1121
FT /note="Helical; Name=TM8"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 1122..1133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 1134..1151
FT /note="Helical; Name=TM9"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 1152..1168
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TRANSMEM 1169..1197
FT /note="Helical; Name=TM10"
FT /evidence="ECO:0000305|PubMed:32973005"
FT TOPO_DOM 1198..1215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:32973005"
FT REGION 156..185
FT /note="A-domain; part 1"
FT /evidence="ECO:0000303|PubMed:32973005"
FT REGION 250..390
FT /note="A-domain; part 2"
FT /evidence="ECO:0000303|PubMed:32973005"
FT REGION 466..495
FT /note="P-domain; part 1"
FT /evidence="ECO:0000303|PubMed:32973005"
FT REGION 497..674
FT /note="N-domain"
FT /evidence="ECO:0000303|PubMed:32973005"
FT REGION 677..837
FT /note="P-domain; part 2"
FT /evidence="ECO:0000303|PubMed:32973005"
FT REGION 838..953
FT /note="Arm-like"
FT /evidence="ECO:0000303|PubMed:32973005"
FT REGION 954..969
FT /note="P-domain; part 3"
FT /evidence="ECO:0000303|PubMed:32973005"
FT ACT_SITE 487
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000305|PubMed:22745129,
FT ECO:0000305|PubMed:24392018, ECO:0000305|PubMed:30785834,
FT ECO:0000305|PubMed:32353073"
FT BINDING 487..489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:32973005"
FT BINDING 487
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:32973005"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:32973005"
FT BINDING 582
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Q0"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:32973005"
FT BINDING 699
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:32973005"
FT BINDING 816..820
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:32973005"
FT BINDING 816
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:32973005"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 487
FT /note="D->N: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:22745129,
FT ECO:0000269|PubMed:24392018, ECO:0000269|PubMed:30785834,
FT ECO:0000269|PubMed:32353073"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 58..73
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6XMP"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6XMP"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 173..177
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 219..246
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6XMS"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6XMS"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 304..308
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:6XMP"
FT HELIX 397..424
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 428..440
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 447..462
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 498..501
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:6XMP"
FT HELIX 523..531
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 547..556
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:6XMU"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 607..611
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 621..629
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 637..642
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 656..659
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 664..667
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 679..687
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 688..690
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 692..696
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 701..711
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 718..729
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 732..740
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 742..744
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 754..757
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 758..760
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 762..765
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 767..771
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 772..775
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 779..783
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 785..789
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 796..807
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 817..819
FT /evidence="ECO:0007829|PDB:6XMP"
FT HELIX 821..826
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 827..833
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 838..853
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 956..961
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 963..968
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 973..1009
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 1010..1013
FT /evidence="ECO:0007829|PDB:6XMU"
FT HELIX 1019..1034
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 1053..1055
FT /evidence="ECO:0007829|PDB:6XMS"
FT HELIX 1056..1083
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 1100..1118
FT /evidence="ECO:0007829|PDB:6XMT"
FT TURN 1124..1126
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 1130..1132
FT /evidence="ECO:0007829|PDB:6XMU"
FT HELIX 1134..1151
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 1156..1161
FT /evidence="ECO:0007829|PDB:6XMT"
FT HELIX 1170..1196
FT /evidence="ECO:0007829|PDB:6XMT"
FT STRAND 1198..1200
FT /evidence="ECO:0007829|PDB:6XMP"
FT TURN 1204..1206
FT /evidence="ECO:0007829|PDB:6XMT"
SQ SEQUENCE 1215 AA; 135269 MW; 7A9960D34B91B5AE CRC64;
MTKKSFVSSP IVRDSTLLVP KSLIAKPYVL PFFPLYATFA QLYFQQYDRY IKGPEWTFVY
LGTLVSLNIL VMLMPAWNVK IKAKFNYSTT KNVNEATHIL IYTTPNNGSD GIVEIQRVTE
AGSLQTFFQF QKKRFLWHEN EQVFSSPKFL VDESPKIGDF QKCKGHSGDL THLKRLYGEN
SFDIPIPTFM ELFKEHAVAP LFVFQVFCVA LWLLDEFWYY SLFNLFMIIS MEAAAVFQRL
TALKEFRTMG IKPYTINVFR NKKWVALQTN ELLPMDLVSI TRTAEESAIP CDLILLDGSA
IVNEAMLSGE STPLLKESIK LRPSEDNLQL DGVDKIAVLH GGTKALQVTP PEHKSDIPPP
PDGGALAIVT KTGFETSQGS LVRVMIYSAE RVSVDNKEAL MFILFLLIFA VIASWYVWVE
GTKMGRIQSK LILDCILIIT SVVPPELPME LTMAVNSSLA ALAKFYVYCT EPFRIPFAGR
IDVCCFDKTG TLTGEDLVFE GLAGISADSE NIRHLYSAAE APESTILVIG AAHALVKLED
GDIVGDPMEK ATLKAVGWAV ERKNSNYREG TGKLDIIRRF QFSSALKRSA SIASHNDALF
AAVKGAPETI RERLSDIPKN YDEIYKSFTR SGSRVLALAS KSLPKMSQSK IDDLNRDDVE
SELTFNGFLI FHCPLKDDAI ETIKMLNESS HRSIMITGDN PLTAVHVAKE VGIVFGETLI
LDRAGKSDDN QLLFRDVEET VSIPFDPSKD TFDHSKLFDR YDIAVTGYAL NALEGHSQLR
DLLRHTWVYA RVSPSQKEFL LNTLKDMGYQ TLMCGDGTND VGALKQAHVG IALLNGTEEG
LKKLGEQRRL EGMKMMYIKQ TEFMARWNQP QPPVPEPIAH LFPPGPKNPH YLKALESKGT
VITPEIRKAV EEANSKPVEV IKPNGLSEKK PADLASLLLN SAGDAQGDEA PALKLGDASC
AAPFTSKLAN VSAVTNIIRQ GRCALVNTIQ MYKILALNCL ISAYSLSIIY MAGVKFGDGQ
ATVSGLLLSV CFLSISRGKP LEKLSKQRPQ SGIFNVYIMG SILSQFAVHI ATLVYITTEI
YKLEPREPQV DLEKEFAPSL LNTGIFIIQL VQQVSTFAVN YQGEPFRENI RSNKGMYYGL
LGVTGLALAS ATEFLPELNE AMKFVPMTDD FKIKLTLTLL LDFFGSWGVE HFFKFFFMDD
KPSDISVQQV KIASK
//
