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Database: UniProt
Entry: A0A0R2HV65_CARDV
LinkDB: A0A0R2HV65_CARDV
Original site: A0A0R2HV65_CARDV 
ID   A0A0R2HV65_CARDV        Unreviewed;       669 AA.
AC   A0A0R2HV65;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE            EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN   ORFNames=IV74_GL002052 {ECO:0000313|EMBL:KRN54469.1};
OS   Carnobacterium divergens DSM 20623.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1449336 {ECO:0000313|EMBL:KRN54469.1, ECO:0000313|Proteomes:UP000051658};
RN   [1] {ECO:0000313|EMBL:KRN54469.1, ECO:0000313|Proteomes:UP000051658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20623 {ECO:0000313|EMBL:KRN54469.1,
RC   ECO:0000313|Proteomes:UP000051658};
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:KRN54469.1}.
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DR   EMBL; JQBS01000035; KRN54469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2HV65; -.
DR   PATRIC; fig|1449336.4.peg.2089; -.
DR   eggNOG; COG2217; Bacteria.
DR   Proteomes; UP000051658; 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; cd07552; P-type_ATPase_Cu-like; 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; 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; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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   PROSITE; PS00154; ATPASE_E1_E2; 1.
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|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051658};
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        57..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        87..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        121..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        279..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        617..639
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        645..665
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   669 AA;  71950 MW;  37D3E65B8CB1E02E CRC64;
     MKGMDHEEMS GMEHMAHMGN LKQKFLVSLL LAIPIILLSP MMGLELPFQI TFKGSDWLVL
     LLGTILFFYG GKPFLSGAKM ELKAHSPAMM TLIALGISVS YFYSVYAFIS NHFLPNQPHV
     MDFFWELATL IVIMLLGHWI EMRAISNAGD ALKKMAELLP NEATIIDSTS LKTKQIPLSE
     VAIGDLLQVK AGEKIPADGI VEAGTTSINE AMVTGEAKSV KKQVKDKVIG GSVNGEGTIT
     ISVTGTGESG YLAQVMALVG SAKEEKSAVE SLSDRVAKWL FYVALSVGIL AFVSWLFITK
     EINTPLERMV TVLVIACPHA LGLAVPLVTA RSTSLGAKNG LLIRNKNALE SAKKVDVILM
     DKTGTLTEGD FSVTAIESFK SDYSRLDILK IAGALEQKSS HPLATGILKR VEEEKVKLPT
     ASEVQAIPGV GLSGTINHQN IKIVTASYLM KQKGAFDQEQ FNQLAGEGNS VSYLMIEETV
     IGLIAQGDKI KENASQFIKE LLDRGIQPVM LTGDNQAAAK IVADKVGIQT FYANLLPEEK
     EKMVARYQQK EKTVMMLGDG VNDAPSLAKA DVGIAIGAGT DIAIDSADVI LVKSDPLDTL
     HFLSLAKNTT RKMIENLWWG AGYNIIAIPL AAGILAPIGV VLSPAVGSVL MSLSTVVVAF
     NALLLKIDH
//
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