ID A0A0R1H7V3_9LACO Unreviewed; 818 AA.
AC A0A0R1H7V3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=FC07_GL002999 {ECO:0000313|EMBL:KRK40707.1};
OS Loigolactobacillus bifermentans DSM 20003.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423726 {ECO:0000313|EMBL:KRK40707.1, ECO:0000313|Proteomes:UP000051461};
RN [1] {ECO:0000313|EMBL:KRK40707.1, ECO:0000313|Proteomes:UP000051461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20003 {ECO:0000313|EMBL:KRK40707.1,
RC ECO:0000313|Proteomes:UP000051461};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK40707.1}.
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DR EMBL; AZDA01000005; KRK40707.1; -; Genomic_DNA.
DR RefSeq; WP_057903365.1; NZ_AZDA01000005.1.
DR AlphaFoldDB; A0A0R1H7V3; -.
DR STRING; 1423726.FC07_GL002999; -.
DR PATRIC; fig|1423726.3.peg.3113; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000051461; 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; 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:UP000051461};
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 165..184
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 196..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 419..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 447..468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 762..785
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 791..809
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 72..138
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 818 AA; 85824 MW; EA156B6F397268B2 CRC64;
MTEAMFNING MMCASCAQTV THATQKLPGV QQANVNLAAE KMQVTYDAAQ VTVPDIETAV
ADAGYEAQQI TADMTFTIDG MMCASCAQTI EKAVNALPGV TQAAVNLASE KMQVSFVAAQ
VDVATIVQTV TDAGYQATPE VTAEKSSETQ AAKKQVQLQN MWHRFVWSAI FTVPLLYISM
GGMLNAPLPM WLQGMHNPQV TSLVELLLTL PVLYFGREYY LVGYKTLFKG HPNMDALVAL
GTSAAFGESL WHTAQYWFAG QAFNDGLYYE AAATILTLIT LGKYFETLSK TKTSSALTAL
LKLQPQQAWR VVNGQTEQVA VAAVQVGDEL LVKPGEQLPV DGVVLTGATS IDESMLTGES
MPVEKQVGDS VVGGSLNQTG QVTYRATKVG QDTALAQIVK LVEDAQLSKA PIAKLADVIS
GYFVPVIMGL ALLAGLGWLI NGAGFGYSVQ IFVAVLVIAC PCALGLATPT AIMVGTGKGA
ENGILIKNGT ALEVTQQLET LVFDKTGTVT QGHPAVTDVA PQAGTTSDEL LSLAASLEQY
SEHPLAVAIQ QAATEQALTV PASRDFKALP GYGVTGVVAD QVAWLGNLAL MQQQQITITP
AQQQTAAALA QAGKTPFYLA VGAELKGILA VADPVKASSA QALAALKQQG KHLVLLTGDN
QQTAQAIAEQ VGIDEVISDV LPADKAAVIA KLQAKGQKVG MVGDGINDAP ALVQADVGLA
MGSGTDVAID AADIVLLNHQ LTSVPTALAL SQRTMRTIKQ NLFWAFAYNA CGVPIAMGLL
ALFGGPLLNP MIAGAAMSFS SVSVLLNALR LKRFKPVI
//
