ID A0A3D9LEW4_9MICC Unreviewed; 871 AA.
AC A0A3D9LEW4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Cu+-exporting ATPase {ECO:0000313|EMBL:REE04390.1};
GN ORFNames=C8E99_2225 {ECO:0000313|EMBL:REE04390.1};
OS Citricoccus muralis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Citricoccus.
OX NCBI_TaxID=169134 {ECO:0000313|EMBL:REE04390.1, ECO:0000313|Proteomes:UP000256727};
RN [1] {ECO:0000313|EMBL:REE04390.1, ECO:0000313|Proteomes:UP000256727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14442 {ECO:0000313|EMBL:REE04390.1,
RC ECO:0000313|Proteomes:UP000256727};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUL-2018) 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:REE04390.1}.
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DR EMBL; QREH01000001; REE04390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9LEW4; -.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000256727; 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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000256727};
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 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 193..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 272..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 424..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 452..479
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 824..843
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 849..867
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 16..80
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 82..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 89478 MW; D53D87A5BDBDA620 CRC64;
MSETVKSAAA EDSGTRRVDL DITGMTCASC VGRVERKLGK LEGVTATVNL PLEAAAVTVP
TSVTDEEIIA AVDRAGYSAS IRRAPSDTGT STASATVTRS GHPELGDGEE SSDGDHGKHD
NHPDHDGHGH QGEHDVQGTH SNHGPDGHEG HENHLNHGPS GDVVKPRLIG AAVLTLPLFL
ISMVPALQFP HWGWVALALA TPVTFWAAWP FHTAAFKAAR HGSSTMDTLV SIGVLAAWGF
STAELLLEPD MTAHAGAAMG GGGMASMADH QLYFETAGVV TTFLLLGRWL EARAKKRAGH
ALKSLLDLGA KTATVLRDGV EVTVPAAQLV PGDEFVVRPG EKVATDGYVV SGHSAVDTSL
ITGESVPEEV GPEDTVTGAT VNTSGRLLVR ATRTGSDTTL AQMGRLVSDA QTGKAPIARL
ADRISAVFVP IVLVIAVITF ALWLLFSGDL HAAFRAAVAV LVIACPCALG LATPVGLLAG
TGRASQLGIL IRGPEVLEDT RTVDTIVLDK TGTVTAGDLA VTAVTPLNGH DADQVLRLAG
AVESHSEHPI AAAITTAARD AAASSEASDY SDSADFSGST VPEVTGFESA AGGGVRGTVA
FPRNHRDDSG VAVAIGRQSP QQLPTQTLGE PGPADFRTHT VAAGRSSYIA TQLSSGSLTA
DEQQQLADAE AAGATAIWVS VDGQVAGIIS LQDTIKESSA PAIAEFKRLG LRPILLTGDN
AEVAAQVAAA VGISAQDVFA GVRPEDKVAK VIELQEAGRV VAMVGDGVND APALAQADLG
IAMGSGTDVA REAADITVMG SSLGQVVQSV QLSRKTLGII KSNLFWAFAY NTLGIPVAAL
GLLNPMLAGA AMAASSVLVV ANSLRLTRFG R
//
