ID A0A1F8S8Z9_9CHLR Unreviewed; 785 AA.
AC A0A1F8S8Z9;
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:OGO56326.1};
GN ORFNames=A2V85_10785 {ECO:0000313|EMBL:OGO56326.1};
OS Chloroflexi bacterium RBG_16_72_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797663 {ECO:0000313|EMBL:OGO56326.1, ECO:0000313|Proteomes:UP000176218};
RN [1] {ECO:0000313|EMBL:OGO56326.1, ECO:0000313|Proteomes:UP000176218}
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:OGO56326.1}.
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DR EMBL; MGOE01000091; OGO56326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8S8Z9; -.
DR STRING; 1797663.A2V85_10785; -.
DR Proteomes; UP000176218; 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 PRINTS; PR00942; CUATPASEI.
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 113..132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 178..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 395..418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 713..735
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 741..760
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 9..75
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 785 AA; 81413 MW; D74F53423FF2FB22 CRC64;
MTSPSTPLEI VSFPIEGMTC ASCVNRITRF LDKVEGVEEA SVNLASESAT VRFDPARVTL
ADLVGAVDAA GYVARVEQVA SAEHSVDVAE AAAAKAERDE AAARHAADLR RRFIVSALLT
LPLLGGLARM TVAPWLPAFL TNPLFQLAVA TPVQLWAGWP FYTGAIKALR HRASDMNTLI
AVGTSAAYGY SVATILLPDF FMAAGLGMDG AELPMYFDTS AAIITLILLG RYLEARARSH
TSDAIRRLIN LAPRTARVIR DGIELDVAVA DVRVGDTVRV RPGETIAVDG VVTEGASGVD
ESMITGESLP VSKRVEDLVV GGTLNTTGTL TFRATRVGAD TVLAKIIRLV SEAQGSRAPI
QRLADVVTSY FVPAVLGLAA FTFVVWFAFG PQPAFNLALL STVAVLIIAC PCALGLATPT
SIMVGTGKGA ENGILFRNAE ALERLGSVKA VILDKTGTLT EGKPRVTDIV RAAGAPPEDD
LLALVAAAER GSEHPLADAI VRETIERRRL TVADATDFLS VPGGGVSATI GGHRVLVGRP
GFLESAGIDV ASLAGAADAL AADGKTPVLA AIDGRAAAVI AIADTLKAGS VEAVAELHRL
GIAVAMLTGD NLRTAEAIAR SVGIDRVVAD VRPDGKAAAV RALQAGGKVV AMVGDGVNDA
PALASADVGV AMGTGTDVAM ESAGVTLMSG DLRGLVTAIA LSRATMWNIR QNLFWAFAYN
VILIPVAMGA LYPFTGLLLD PILAAGAMAL SSVTVVSNAL RLRRFEARPT TVQAQPRPAT
LPSIP
//
