ID R5J3D0_9FIRM Unreviewed; 840 AA.
AC R5J3D0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=BN480_00741 {ECO:0000313|EMBL:CCY43521.1};
OS Firmicutes bacterium CAG:124.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263002 {ECO:0000313|EMBL:CCY43521.1, ECO:0000313|Proteomes:UP000018269};
RN [1] {ECO:0000313|EMBL:CCY43521.1, ECO:0000313|Proteomes:UP000018269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:124 {ECO:0000313|Proteomes:UP000018269};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY43521.1}.
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DR EMBL; CAYD010000237; CCY43521.1; -; Genomic_DNA.
DR AlphaFoldDB; R5J3D0; -.
DR Proteomes; UP000018269; 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 GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
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; 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; 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; 1.
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:UP000018269};
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 90..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 351..373
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 385..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 692..715
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 721..742
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..63
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 772..837
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 840 AA; 87298 MW; 0103675F364344C1 CRC64;
MQQYTVTGMH CAACSASVEK AVKKVPGVTS CAVSLLTNSM GVEGTAEPAA IINAVEDAGY
GASVRGQEAA PAADASALED RQTPHLKKRL IASVAFLLIL MYFSMGHMMW GWPLPGWFDG
NHVAMGLVQL LLAGIVMVIN QEFFVSGTKS LLRGSPNMDT LVSLGAAASY GWSVYALFAM
TDAQLHGGSE AAMAYMDEFY FESAAMILTL ITVGKLLEAH SKGKTTDALK SLMALAPETA
TVIRDGKEVK IPAAQVRKGD VFVVRPGQSI PVDGVVLDGA SAVNEAALTG ESVPVDKAPG
DGVSAATVNC SGFLRCEATR VGEDTTLSQI IRMVSDAAAT KAPIAKTADK VAGVFVPAVI
SIALVTTIVW LLLGREFSFA LARGISVLVI SCPCALGLAT PVAIMVGSGV GAKNGILFKT
AASLEHTGRT RIVALDKTGT ITSGQPEVTD LIPADGVTER ELLQAAVSLE AKSEHPLAAA
IMKRGEEEKL QPEAAENFAA ITGSGLTATV LGAQLLGGSV KYMASQLALP QEIHKQADAL
SQSGKTPLLF AKNGRLLGLI AVADAIKPES PEAIRQLRGM GIRVVMLTGD NQRTADAIGK
LAGVDDVVAG VLPGGKEAVV RELQKYGPVA MVGDGINDAP ALTAADTGIA IGAGADVAID
AADVVLMKST LLDVAAAIRL SRAALRNIHE NLFWAFIYNV IGIPLAAGVF VGLGLTLNPM
YGAAAMSLSS FCVVSNALRL NLCKLYSAKH DHKGKPMPEI HLAEQNKEET GMTKTLHVKG
MMCGHCEARV KKALEAVDGV ASAVADHNNG TAVVTLTKDV SNETLKAAVE AQDYEVTGVE
//
