ID A0A1F5TNB2_9BACT Unreviewed; 723 AA.
AC A0A1F5TNB2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:OGF40443.1};
GN ORFNames=A2531_02820 {ECO:0000313|EMBL:OGF40443.1};
OS Candidatus Falkowbacteria bacterium RIFOXYD2_FULL_34_120.
OC Bacteria; Candidatus Falkowbacteria.
OX NCBI_TaxID=1798007 {ECO:0000313|EMBL:OGF40443.1, ECO:0000313|Proteomes:UP000177579};
RN [1] {ECO:0000313|EMBL:OGF40443.1, ECO:0000313|Proteomes:UP000177579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGF40443.1}.
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DR EMBL; MFGO01000029; OGF40443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5TNB2; -.
DR Proteomes; UP000177579; 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; IPR017969; Heavy-metal-associated_CS.
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; 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; PS01047; HMA_1; 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|ARBA:ARBA00022723,
KW 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 89..107
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 127..145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 181..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 678..697
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 723 AA; 80371 MW; 8C362C221FB0B978 CRC64;
MSKITLKIKG MDCASCALTI SHRLKKQEGI KRVDINFASE KAIIEYIEEE ININKIKEVI
KSTGYEIDDS NRWEAHEHTH AMDEKKQKIN VIFAAILTLP IVIRMFWAWE IPGEFLGISL
TNWLQHWLSF IVVFLFGWQF HANTFKQLKT FQVGMDALVS MGTLSAYFYS LWALFTSHHL
YFESAASIAT LILLGRFLEY KTRERASYAM RKLLELGVKQ ALTIQDGREI YKNIEEIKVG
DVVLVKPSEK IPLDGVVVEG ESSVVESMLT GESMPVYKKR DSIVFGATIN KTGILKIKIT
KKGKDTVLSK IIKSIEEAQS SKPPMQKLAD KVSGIFVPVV IGIAILTFIG WFLKTGNVAI
SLINAVSVLI ISCPCALGIA TPIAVMVGTS VGVQNGILIK SGDSFEKAKD IDVVVFDKTG
TLTLGEPKII KTISNPEYNE EENEIIKVAN LVARNSQHPL SRAVVNLAKE KNINLDGVCD
FREVPGQGVV GKCDEHRYEI LLGNMKLISN KKLKTLWADN LMIEFEISGE TVLYVAHENK
VIGAFLITDE LRENTQKTID KIKEMKLEPI MLSGDNEKAA GMIAEELGIS NYLAGVLPNE
KQKMVKNLQR NDKKVIFVGD GINDAPSLVQ ADLGIAFGSG TDIAKESGDI ILMQNDPYKV
IEAIKLSRKT FKIIKQNLFW AFFYNVVAIP LAVMGMVNPM VGAIAMSLSD VSVIGNSLRI
YRK
//
