ID A0A0L0LBB1_9BACT Unreviewed; 764 AA.
AC A0A0L0LBB1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 33.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:KND47702.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:KND47702.1};
GN Name=copA {ECO:0000313|EMBL:KND47702.1};
GN ORFNames=AB201_02075 {ECO:0000313|EMBL:KND47702.1};
OS Parcubacteria bacterium C7867-006.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659200 {ECO:0000313|EMBL:KND47702.1, ECO:0000313|Proteomes:UP000037457};
RN [1] {ECO:0000313|EMBL:KND47702.1, ECO:0000313|Proteomes:UP000037457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-006 {ECO:0000313|EMBL:KND47702.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
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:KND47702.1}.
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DR EMBL; LFCP01000004; KND47702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LBB1; -.
DR STRING; 1659200.AB201_02075; -.
DR PATRIC; fig|1659200.3.peg.133; -.
DR Proteomes; UP000037457; 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; 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 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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 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 Hydrolase {ECO:0000313|EMBL:KND47702.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {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 107..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 210..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 363..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 397..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 710..732
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 738..757
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 3..69
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 764 AA; 82212 MW; 2DB4C052E6204178 CRC64;
MNHTQTYKIK GMHCASCASI IEKTFKKSDG VHSVEVNYGT ETAKIAFDES KTSPHHLSKN
IEKLGYSLDI PSAESMGMSA NEHAAHLGLN QSKKEKLAEV ADMRTKVLSA IPIAILAAFI
MGWDIFAEYN IAPAMSYTLK EFFHHLLPIL ATYILFVVGK PYLFGFYRFL RYGKANMDTL
IGIGTSTAFL YSFAVTAFED VLRPFINVEY QYYDVTIVVI TFIALGKYLE ARSKIKTGDA
IEKLLNLQAK TALVIRDGKE VEISVNDVKH NDLIIVKPGA KIPVDGVVTE GSSFIDESMV
TGEPMPVQKK VGDSVVSGTI NTNGSFTFKA TKVGSETLLA QIIKMVEEAQ GSRAPIQALA
DKISAIFVPI VLVIAFLTLG AWLIVGSQYL GFSQALSFGL VSFVGILVIA CPCALGLATP
TAIIVGVGKG AKEGILIKDA ATLEKLHKVN TVVVDKTGTI TIGKPTLVDI QNNSNLNDEE
FISILASLEK KSEHPIAHAI VNYAQEKNIP ISEALVFEAI QGKGLKGSIK GTEYFVGNTK
LVSDLILSFD NMKLNEFTSQ GKTPVILASK EKVLGFVMVA DEIKQESKQA VSDLHDLGVK
VVMLTGDDEK AAKYIASLVG IDEVVAHVLP QDKLEKIKEL QSHGLVVAMA GDGVNDAPAL
AQADVGIAMG TGTDVAIESA GITLLGGDIS KLVKAIKLSK ITMRGIKQNL FWAFIYNIVG
IPLAAGALYP VFGWLLNPVF AGFAMAMSSV SVVSNSLRIK AKKL
//
