ID A0A0G0JGI2_9BACT Unreviewed; 669 AA.
AC A0A0G0JGI2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 35.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:KKQ27231.1};
GN ORFNames=US42_C0012G0002 {ECO:0000313|EMBL:KKQ27231.1};
OS Candidatus Magasanikbacteria bacterium GW2011_GWC2_37_14.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1619046 {ECO:0000313|EMBL:KKQ27231.1, ECO:0000313|Proteomes:UP000034849};
RN [1] {ECO:0000313|EMBL:KKQ27231.1, ECO:0000313|Proteomes:UP000034849}
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:KKQ27231.1}.
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DR EMBL; LBSX01000012; KKQ27231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JGI2; -.
DR STRING; 1619046.US42_C0012G0002; -.
DR PATRIC; fig|1619046.3.peg.783; -.
DR Proteomes; UP000034849; 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 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; 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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 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 SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 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 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 63..86
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 98..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 278..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 312..339
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 617..636
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 72410 MW; 36A52F8AAEAC653F CRC64;
MSNITQPVDH AKMDHQQSQG YSKHEGHSVG IFKRKFYISL GLTIPVLVLS PIIQKFLGFS
ISFYGDMFVL FGFSSVVFFY GGLPFLKGSL TEIKNKMPGM MTLISLAIAV AYFYSSAVTF
GLSGEVFFWE LATLIDIMLL GHWLEMRSVM GASRALEKLS QLIPDKAHLV KGQQIIDINT
SELKTGDVII IKPGEKIPSD GVVVQGESFV NESMLTGESK PMSKKVGSKV IGGSINEDGS
LQIKIEMVGE ATYLSKVINL VKSAQASKSK TQVLADKAAF WLTIIAVSVG VATFVTWLLL
GKDIAFAIER AATVLIIACP HALGLAVPLV VAISTALSAQ NGLLIRNRTA FENSRRISTV
VFDKTGTLTE GTFTLTKIYN FNAQYNQDKT LAIAASLEKN SEHPIARAVV KEAENKGSKF
LGVKNFHAIK GKGTEGDVEE VPYILASPGF LKELGLNIPL ELKQTSATVV YLIEKNENKL
IGAFALSDVV RLESQKAIDL LKKEGIKVWM LTGDNAQVAK EVSEELGLDG YFAEVLPDQK
QDKIKELQEK GEFVAMVGDG INDAPALAQA DVGIAIGSGT DIAAETADII LVNSNPRDIA
SLIMFGKATY RKMVQNLIWA TGYNVVAIPL AAGVLYRYDL LLTPALGAVF MSLSTIIVAI
NAKTLKVKK
//
