ID N1Z2F8_9CLOT Unreviewed; 846 AA.
AC N1Z2F8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN Name=copA {ECO:0000313|EMBL:USF29453.1};
GN ORFNames=C820_000844 {ECO:0000313|EMBL:USF29453.1}, C820_02452
GN {ECO:0000313|EMBL:EMZ11292.1}, FMM67_11695
GN {ECO:0000313|EMBL:NDO47476.1};
OS Clostridium sp. MD294.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ11292.1};
RN [1] {ECO:0000313|EMBL:EMZ11292.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|EMBL:EMZ11292.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:NDO47476.1, ECO:0000313|Proteomes:UP000462571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|Proteomes:UP000462571}, and MD294
RC {ECO:0000313|EMBL:NDO47476.1};
RA Elie C., Mathieu A., Saliou A., Darnaud M., Leulier F., Tamellini A.;
RT "Draft genome sequences of 15 bacterial species constituting the stable
RT defined intestinal microbiota of the GM15 gnotobiotic mouse model.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:USF29453.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF356 {ECO:0000313|EMBL:USF29453.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) 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; AQFQ01000028; EMZ11292.1; -; Genomic_DNA.
DR EMBL; VIRC01000022; NDO47476.1; -; Genomic_DNA.
DR EMBL; CP097810; USF29453.1; -; Genomic_DNA.
DR AlphaFoldDB; N1Z2F8; -.
DR STRING; 97138.C820_02452; -.
DR PATRIC; fig|97138.3.peg.2469; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_9; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000012445; Chromosome.
DR Proteomes; UP000462571; 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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; 2.
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 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:UP000012445};
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 93..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 203..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 383..404
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 697..721
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 727..746
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..67
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 779..843
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 846 AA; 91623 MW; F457F42B0CBC530F CRC64;
MKQKFDVTGM TCSACSAHVE KSVNKLAGIF SVNVNLLQNS MTVEYEETKL TDEEIIKAVE
QGGYGAKVHG SEKTNHTSEN IAQSEMDTMK KRLIWSFVFL IPLFYISMGH MMGMPLPSIL
LGHENIMSFA LTQLFLTLPI LYLNRKYFSV GFKALWNRSP NMDTLIALGS TAAFCYSVIA
IYAMGYYMGH GDMVAAHSYG MEFYFESSGM ILTLITVGKY METRSKGKTS EAITKLLDLA
PKKATILKNG KEIEIAIEEV QKGDIIVVRP GQSIPVDGEI IEGFSAVDES ALTGESIPVE
KKAGDMVIGA TVNKTGYFQF RAEKVGNDTT LSQIIQLVEE ASASKAPIAK LADKVSGIFV
PVVITIALAV TAIWLLLGYS FSFALSIGIA VLVISCPCAL GLATPTAIMV GTGKGAENGI
LIKSAESLEI AHEVDTIILD KTGTVTEGKP KVTDVLLAEG VFENKLLRNA LAVEQLSEHP
LSEAIVNYVK QKNITVPNGE NFTAIAGQGV KATVSGKEII AGNLKMMKEQ DISENFLFEK
GEKLAEEGKT PLYFAEENKL LGVIAVADVV KPTSKQAIAE FRKMGIDVVM LTGDNKRTAE
AIGKQMNLTR VVAEVLPQDK EKEVRQIQQQ GKKVAMIGDG INDAPALARA DVGVAIGAGT
DVAIESADIV LMKSDLLDGV AAIQLSRAVI RNIKQNLFWA FFYNVIGIPL AAGLFFTTLG
WKLNPMFAAA AMSCSSVFVV TNALRLKLFQ PDFKKGKTIE NNNTIVEEQQ KEYKEEIKMK
KVLTIEGMMC GHCTGRVEQA LNALEGVKAE VSLDDKTATV TAVEEIAEEL LVKAVTDAGY
TVVDVQ
//
