ID A0A0G1SBF0_9BACT Unreviewed; 784 AA.
AC A0A0G1SBF0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 36.
DE SubName: Full=ATPase, E1-E2 type:Copper-translocating P-type ATPase:Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:KKU66712.1};
GN ORFNames=UX89_C0019G0032 {ECO:0000313|EMBL:KKU66712.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_16.
OC Bacteria.
OX NCBI_TaxID=1618842 {ECO:0000313|EMBL:KKU66712.1, ECO:0000313|Proteomes:UP000034117};
RN [1] {ECO:0000313|EMBL:KKU66712.1, ECO:0000313|Proteomes:UP000034117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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:KKU66712.1}.
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; LCNX01000019; KKU66712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1SBF0; -.
DR STRING; 1618842.UX89_C0019G0032; -.
DR PATRIC; fig|1618842.3.peg.825; -.
DR Proteomes; UP000034117; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 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; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 127..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 409..433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 730..752
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 758..777
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 21..87
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 784 AA; 84538 MW; E15434FA431362B5 CRC64;
MGDGRRANYT NLRMDTNKIM NTKTFKIKGM HCASCAGIIE KTFKKTEGVE SAEVNYATET
AKVSFDESKI HPEHLSQKIE PLGYSLIVSE AKAMGMSENE HAAHLGLNQS KQEKLAELAD
MKSKLRIALP LTVFTVFVMS WDILAQFSFV APGSYFWKEF FHHLLPIFAT YILFVVGKPY
LLGVYRFLRY GKANMDTLIG IGTSVAFIYS FVVTAFEDSL KTFVDVNSIY YDVTIVVITF
IALGKYLEAR SKIKTGDAIE KLLNLQAKTA LVSLDGIEKE IPIEEVKHGD LIIVKPGGKI
PVDGVITEGE SFIDESMVSG EPMPVKKKIG DGVVAGTINT TGSFTFRATK VGSETLLAHI
IKMVEEAQGS KAPIQALADK ISGVFVPVVL VLSFVTLGVW LLVGTETLGF AAALSLGLTA
FVGILVIACP CALGLATPTA IIVGVGKGAK EGILIKDAAT LEKLHKVDTV VVDKTGTLTR
GKPELVSIRN FSEGGKQDKE LVSILATLEK KSEHPIAHAI IEYAKTHNVD TLPVENFETI
KGKGLKGAVA GMEYFVGNAK LAAELQLVVD VSSFEKETTQ GKTPIILMTK KEVLGVFMIA
DAIKQESVEA IRNLHKLGIK VVMLTGDDKN TAKAIANEVG IDEVFAEVLP DEKQNKIKEL
QNEGRIVAMA GDGVNDAPAL AQADVGIAMA TGTDVAIETA GITLLHGDVS KLVKAIKLSK
MTMRGIRQNL FFAFIYNIVG IPIAAGVLYP LYGWMLSPVF AGLAMALSSV SVVGNSLRLK
SMKL
//
