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Database: UniProt
Entry: A0A1H1H289_9ACTN
LinkDB: A0A1H1H289_9ACTN
Original site: A0A1H1H289_9ACTN 
ID   A0A1H1H289_9ACTN        Unreviewed;       821 AA.
AC   A0A1H1H289;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Cu+-exporting ATPase {ECO:0000313|EMBL:SDR19560.1};
GN   ORFNames=SAMN04489765_3757 {ECO:0000313|EMBL:SDR19560.1};
OS   Tsukamurella pulmonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=47312 {ECO:0000313|EMBL:SDR19560.1, ECO:0000313|Proteomes:UP000183053};
RN   [1] {ECO:0000313|Proteomes:UP000183053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44142 {ECO:0000313|Proteomes:UP000183053};
RA   Varghese N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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}.
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DR   EMBL; FNLF01000002; SDR19560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1H289; -.
DR   STRING; 47312.SAMN04489765_3757; -.
DR   OrthoDB; 7059309at2; -.
DR   Proteomes; UP000183053; 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   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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   Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 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; IPR009078; Ferritin-like_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   InterPro; IPR012348; RNR-like.
DR   InterPro; IPR007029; YHS_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   Pfam; PF04945; YHS; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
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; SSF47240; Ferritin-like; 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; PS01229; COF_2; 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        103..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        126..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        164..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        359..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        387..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        702..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        725..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          11..75
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   821 AA;  84325 MW;  E8188B0C64C31879 CRC64;
     MSTPGSGTGD ASIELEIGGM TCASCANRIE RRLNKIDGVS ATVNYATEKA KVTAPEGIDP
     QRIIDEVVGT GYTATLAGAA QSGADGEDAS PADAELASLR TRLIGAAVLG VPVIAMAMIP
     ALQFTYWQWA SLALASPVIL WGAWPFHKAA WANLKHGTAT MDTLISMGTL SAFLWSLYAL
     FFGTAGEPGM KHPFTLTLAP SDGAANIYLE VAAGVTMFIL AGRYFEKRSK RQAGAALRAL
     LELGAKEVSV LRDGAEVKIG IDELRAGDEF VVRPGEKIAT DGVVVSGTSA VDASMLTGES
     VPVEVGPGDA VTGATVNAGG RLVVRATRVG SDTQLAQMAR LVEEAQTGKA EVQRLADRIS
     GVFVPIVIAI AAIALGGWLG AGFPVSAAFT AAVAVLVIAC PCALGLATPT ALLVGTGRGA
     QLGVLIKGPE VLESTRRVDT VVLDKTGTVT TGRMTLVDVI AEEGVDPTDV LRYAGALEDA
     SEHPIAQAIA KGAAEKFGTL SPVEGFANIE GQGVQGVVDG HGVIVGRESL LADWALHLSA
     GLAKTKADAE AQGATVVAVG WDGAARGVLV VGDTVKPTSA EAIRELRALG LTPVLLTGDN
     EAAARHIAAQ VGIDEVIAEV LPQDKVAVVT HLQGEGRVVA MVGDGVNDAP ALAAADLGLA
     MGTGTDVAIE AADITLVRGD LRAAVDAIRL SRSTLRTIKT NLFWAFAYNV AAIPVAALGM
     LNPMLAGAAM AFSSVFVVGN SLRLRGFRGV AAKSPAESAP VPAPADEKTT CPVMVGNPVV
     KSTAEAAGLY RDYDGERYFF CCPSCAPKFD ADPAKYATHH A
//
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