ID U2VB70_9ACTN Unreviewed; 865 AA.
AC U2VB70;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Copper-exporting ATPase {ECO:0000313|EMBL:ERL09826.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:ERL09826.1};
GN ORFNames=HMPREF1316_1495 {ECO:0000313|EMBL:ERL09826.1};
OS Olsenella profusa F0195.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=1125712 {ECO:0000313|EMBL:ERL09826.1, ECO:0000313|Proteomes:UP000016638};
RN [1] {ECO:0000313|EMBL:ERL09826.1, ECO:0000313|Proteomes:UP000016638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0195 {ECO:0000313|EMBL:ERL09826.1,
RC ECO:0000313|Proteomes:UP000016638};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:ERL09826.1}.
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DR EMBL; AWEZ01000020; ERL09826.1; -; Genomic_DNA.
DR RefSeq; WP_021725454.1; NZ_AWEZ01000020.1.
DR AlphaFoldDB; U2VB70; -.
DR STRING; 1125712.HMPREF1316_1495; -.
DR PATRIC; fig|1125712.3.peg.557; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000016638; 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:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 2.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; IPR006122; HMA_Cu_ion-bd.
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 NCBIfam; TIGR00003; copper ion binding protein; 2.
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; 2.
DR Pfam; PF00702; Hydrolase; 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; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Hydrolase {ECO:0000313|EMBL:ERL09826.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
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 Reference proteome {ECO:0000313|Proteomes:UP000016638};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 106..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 369..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 403..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 716..739
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 745..766
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 6..72
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 797..862
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 865 AA; 89619 MW; D77BE2AC7F0456DC CRC64;
MAQTQRRETF DIRGMTCAAC EARVQRSAAA VKGVSEASVN LLKNSMELSY DGDPKTIDAV
VAAIDRAGYG AVPRSTGRVT TRQKAPAFVD PKVNAQKAVR ARRNQLVGSL VFGVPLFYLA
MGPMLGWPEV PGLDGMGNMM AAAVTQLLLA VCVMFVNRSY FTMGFKTLLH GSPNMDSLIA
IGSAASFGYS LVGVYQMAFA LGHMDVGAAH DAMMHALFFD SAGTILVLIT LGKYFEARAK
GKTTSSISAL IDLAPKEATV VRGGEEVKIP TGEVSVGDRV VVRAGESVPV DGVVVEGSAS
VDESAITGEP LPVEKAAGDT VTGATVSRRG WFAMEASAVG ADTTLARIIR LVDEATSSKA
PIERQADRIA GVFVPVVLGI AAVTFVAWVA LLVPGDLATA INHAVSVLVI SCPCALGLAT
PTAVMVGTER GAKAGILVKS AEALETAGSL DTVVLDKTGT ITAGTPEVTD LRLAPGITKR
DLLRVAAALE RKSEHPLAEA VCAYADEEAP GVDATAEVTD FTQVAGGGLV ATVDGHAVVA
GNARLMGQRG IDLTDLSADA DALAAQAKTP LSFASDGRAL GVVGVADVVK PTSADAIARL
RAMGIRTVML TGDQERTAHA IASQVGVDEV VAGVLPDQKE RKVHDLQRQG HRVAMVGDGI
NDAPALARAD VGIAIGAGTD VAIESADVVL MRSDPGDVAT AIELSRATMR DIRQNLFWAL
FYNAICIPVA MGALTPLGIT LNPMIGAAAM GFSSVFVVSN ALRLFAWRPS TGGAPAATPP
TAIATSVEGK EGNETMTTKT LDIEGMMCDH CVQHVTQALE GVRGVKNVHV SLEDHKATLE
AGALVSNKRL ENAVEDAGYK VTGIA
//
