ID A0A0F9ZHG0_9BACT Unreviewed; 845 AA.
AC A0A0F9ZHG0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE SubName: Full=Cation-transporting P-type ATPase {ECO:0000313|EMBL:KKP43544.1};
GN ORFNames=UR31_C0003G0002 {ECO:0000313|EMBL:KKP43544.1};
OS Parcubacteria group bacterium GW2011_GWA2_33_14.
OC Bacteria.
OX NCBI_TaxID=1618807 {ECO:0000313|EMBL:KKP43544.1, ECO:0000313|Proteomes:UP000034294};
RN [1] {ECO:0000313|EMBL:KKP43544.1, ECO:0000313|Proteomes:UP000034294}
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 -!- 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:KKP43544.1}.
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DR EMBL; LBOS01000003; KKP43544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZHG0; -.
DR PATRIC; fig|1618807.3.peg.126; -.
DR Proteomes; UP000034294; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF31; PLASMA MEMBRANE ATPASE-RELATED; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 809..826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..80
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 845 AA; 93554 MW; 754BE3D563D634AF CRC64;
MDKKIYSYSS IDNNKLEKSL SFSLKRGLSV KEAKKRLKEE GANELENPHS QWWHILFRQF
KSPFIYLLFL AAVLALFLGG LLDAGMIVLF ILINSFLGFY QEFKSDQALK LLQQYTKSTA
RVVRDGRQII IPSSELVRGD LVILETGDLV PADVRLLEDH NYVTVDEEVL TGESVAVHKS
GLLLGSAPKN IYEAKNIVFT GTVIIDGRIT GVVIATGNYT FFAEIKKLAT GIAKESIFSK
GISQFSSFIL KLTVITLVFV FLANIFIKGS SANITELIIF AIALAVSVIP EALPVVFTLS
LSRGALRLAK QKVIIKRLSA VEDLGSIEIL CTDKTGTITE NKLQVKEILP IDGRTNLLLF
ANLAGTFLKE SLEPFDIALK KALEDKKVLL GFEKLATRPF EPKKRSNSVV VKDSLGNHIL
IVRGAPEEVM KLCSNLDEKE KKIFKEWGIN KGQEAQRVLA VATKKIENLD NGSFDILNFE
NDLNFEGCIS FIDPIKKSAF GAIKKAKELG IGIRIITGDS SAVAFAVARE IGLAKNPNQV
ILASDFVALT SGEQEKILPT VQVFARTDPE QKHHLIKLLQ KKYEVGFLGE GINDLPALKS
AGVSIAVQGA SDIARQTADV ILLNKDLSVI IDGIEEGRKI FINTVKYLKA TLASNFGNFY
AVAIASLFID FLPMLPIQLL LLNLLSDFPM ISISMDSVDA SEIKEPKKYN IKDIILITTF
LGIVSTIFDF MFFGFFYKIS PEVLQTNWFI GSVLTELVFL FSIRTSLPFY KAVWPSKTVI
WSSGGAFLAT IILPFTSLGK NIFHFTPPAF GHMAIILGLV VTYFIFSETI KIIYYKTLGN
NKSSR
//