ID U2LJN0_9FIRM Unreviewed; 844 AA.
AC U2LJN0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 ORFNames=RUMCAL_03354 {ECO:0000313|EMBL:ERJ87318.1};
OS Ruminococcus callidus ATCC 27760.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=411473 {ECO:0000313|EMBL:ERJ87318.1, ECO:0000313|Proteomes:UP000016662};
RN [1] {ECO:0000313|EMBL:ERJ87318.1, ECO:0000313|Proteomes:UP000016662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27760 {ECO:0000313|EMBL:ERJ87318.1,
RC ECO:0000313|Proteomes:UP000016662};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (JUL-2013) 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}.
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:ERJ87318.1}.
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DR EMBL; AWVF01000447; ERJ87318.1; -; Genomic_DNA.
DR RefSeq; WP_021681664.1; NZ_KI260360.1.
DR AlphaFoldDB; U2LJN0; -.
DR STRING; 411473.RUMCAL_03354; -.
DR GeneID; 78475039; -.
DR PATRIC; fig|411473.3.peg.2817; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_9; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000016662; 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; 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; 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 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 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 123..141
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 162..180
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 200..218
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 352..374
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 386..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 693..716
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 722..744
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..63
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 778..843
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 844 AA; 88965 MW; 1199751283ABE947 CRC64;
MEQYNVTGMS CAACSARVEK AVSKVDGVTS CSVSLLTNSM GVEGTASPEA IIDAVQKAGY
GASRKGGSDE AAAPDSDALA DRETPVLKRR LIASVGFLAV LMYISMGHMM WGFPLPPFFN
GNHVAMGLVQ MLLTIIIMVI NRKFFVSGFQ SLLHRAPNMD TLVALGSGAA FVYSTYALFA
MTDAQVKGDM DAVMSYMHEF YFESAAMILT LITVGKMLEA HSKGKTTNAL KGLMNLSPKT
AVLLRNGEEV TVPVEQVHRG EQFVVRPGES IPVDGVIVEG TSAVNESALT GESIPVDKAV
GDNVSAATIN QSGFLRCEAT RVGEDTTLSQ IIRMVSDAAA TKAPIAKIAD KVSGVFVPAV
IAIAVVTIVV WLLVGQTVGY ALARGISVLV ISCPCALGLA TPVAIMVGNG VGAKHGILFK
TAVSLEEAGK VQIVALDKTG TITCGEPRVT DILPAADVTE QELLSAATAL EQKSEHPLAK
AILQYSEEHQ IPASPVTEFQ ALVGNGLTAK WNGQVLYGGN AGCIAQATTI PEEVQQQAEM
LAKAGKTPLF FARDNQLLGI IAVADVLKEE SPEAIRQLQN MGIQVVMLTG DNEQTARAIG
KQAGVDHVIA DVLPDGKEAV IRKLSALGKV AMVGDGINDA PALTRADIGI AIGAGTDVAI
DAADVVLMKS RLTDVPAAIR LSRAALRNIH ENLFWAFIYN VIGIPLAAGV WIPLLGWKLN
PMFGAAAMSL SSFCVVTNAL RLNLFQLNRS DRDKKLKHAV AAIQLEQQTG ATGKNSGMQV
TLHIKGMMCS HCEATVKKCL EAFPEVDEAV VSHTEGTAVV SLNAPADLAA LKKAVTEQGY
KVLK
//
