ID D3QZU9_MAGIU Unreviewed; 793 AA.
AC D3QZU9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN OrderedLocusNames=HMPREF0868_0104 {ECO:0000313|EMBL:ADC91637.1};
OS Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. BVAB3
OS (strain UPII9-5)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Mageeibacillus.
OX NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC91637.1, ECO:0000313|Proteomes:UP000008234};
RN [1] {ECO:0000313|Proteomes:UP000008234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:456216; EC=7.2.2.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001390};
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}.
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DR EMBL; CP001850; ADC91637.1; -; Genomic_DNA.
DR RefSeq; WP_012994173.1; NC_013895.2.
DR AlphaFoldDB; D3QZU9; -.
DR STRING; 699246.HMPREF0868_0104; -.
DR KEGG; clo:HMPREF0868_0104; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_9; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000008234; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:RHEA.
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; PR00120; HATPASE.
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 Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Hydrolase {ECO:0000313|EMBL:ADC91637.1};
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:UP000008234};
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 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 162..179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 191..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 235..257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 391..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 735..756
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 762..782
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 77..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 82636 MW; 3670CC85074D96C0 CRC64;
MTKAKFTVSG MSCAACALRV EKAVRQLEGV RTANVNLLTN SMQVEFAADK TGVAEIISQV
DKVGYAAEEV GGRARDGRCD SSFAGGSRSK SRGQKTSNGG PEMLSETAEL IAKGMAGTAA
ELRMTKKRLI GSAVFGLPLF YIAMGHMMHW PLPNFLLEPE NCLVFGLIQL ALSLAVCLIN
RSIFLHGLKN LYYLAPNMDS LIAVGAGAAM LYGWVELAIM GYQLGHCELN AAVKLVSNLY
FESAGTILLL IMLGNFLEIR AKGKSSEVIG KLVSLVPPRA TVLVDGVPTE KPVGKLGLGD
IILVKAGEVI AADGLVVEGS GTVDESMLTG ESLPVCRKTG DTVNGATLNL SGYLHVKVTR
LGEDSMLAQI IRAVDEATLS KAPIAKIADK VSGIFVPVVI GLAVLTGIGW LLAGAAAATA
LNFAICVLVI SCPCALGLAT PTAITVGAGV GAGKGVLFKS AAEIERLAKV DFAVLDKTGT
ITYGRPEVTD VLPNKGVTEA ELLQLAAALE VKSEHPLAGA IMAAAAKAKI DHTVFSLESF
VQVPGGGIKA KIQGTECLGG NRRLLEKAGI DLGEWQAVTE SLAAAGKTPL IFSSGGVIAG
VIAVADVVKP ESAAAVKCLR HLGLATLMIT GDNKYTAAVI GKAVEVDEVV AEVLPQEKAA
RIAELQKCGK IVIMVGDGIN DAPALVQADV GVAIGGGTDI AIEAADVVLM HGKLTDLVVA
VKLGRAVLRN IKENLFWAFA YNVLGIPLAA GIFYPWTGIR LTPMLAALAM SCSSIFVVTN
ALRLRLWRGK LKK
//
