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Database: UniProt
Entry: A0A3M7TMT0_9BACI
LinkDB: A0A3M7TMT0_9BACI
Original site: A0A3M7TMT0_9BACI 
ID   A0A3M7TMT0_9BACI        Unreviewed;       739 AA.
AC   A0A3M7TMT0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE            EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN   ORFNames=EBO34_19580 {ECO:0000313|EMBL:RNA66372.1};
OS   Alteribacter keqinensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacter.
OX   NCBI_TaxID=2483800 {ECO:0000313|EMBL:RNA66372.1, ECO:0000313|Proteomes:UP000278746};
RN   [1] {ECO:0000313|EMBL:RNA66372.1, ECO:0000313|Proteomes:UP000278746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KQ-3 {ECO:0000313|EMBL:RNA66372.1,
RC   ECO:0000313|Proteomes:UP000278746};
RA   Wang H.;
RT   "Bacillus Keqinensis sp. nov., a moderately halophilic bacterium isolated
RT   from a saline-alkaline lake.";
RL   Submitted (OCT-2018) 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:RNA66372.1}.
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DR   EMBL; RHIB01000004; RNA66372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7TMT0; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000278746; 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   CDD; cd00371; HMA; 1.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 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; 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; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
DR   PRINTS; PR00942; CUATPASEI.
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   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS50846; HMA_2; 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:ARBA00023065};
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000278746};
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:ARBA00022448}.
FT   TRANSMEM        79..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        117..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        147..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        182..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        335..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        363..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        679..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        707..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..58
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   739 AA;  79481 MW;  85395654F6EDB23C CRC64;
     MHCASCVNRV EKKISRVDGV EAVNVNLATH QAQVTGDITD ERISEIISSV EKIGFGAKPL
     TDEKEEDLSK KQEAESKKLI RDFSFAAVAT VIVLIGSIPH MMHTWGSWVP GWMSNPFFLL
     ILTTYVQLVP GWRFYKNSYK VLRSKSADMN VLVAMGTTSA WAYSAAMTLF PGFLTNAGFP
     YQLYYDVTTV ITTLILLGRY FEAKAKGQTS TAIKKLMNLQ AKTARVIRSG QELELPVKEV
     RVGDHILVRP GERIPVDGTV IDGSSTVDES MLTGESIPVS KKENDPVIGA TINKSGSFTF
     EASKVGKDTT LAGIIRMVND AQGSKAPIQR MVDVISAYFV PAVVGLASLS FLIWLVFGPD
     PSFIFALTTF IAILIIACPC ALGLATPTAI MVGTEKGAEN GVLIKDASSL EQAHKIDTIL
     LDKTGTITQG RPALTDLVSL KGWTNETLLQ MVASIEMASE HPLGEAIVRA AKEQRLSLSK
     PGSFEAISGH GIEADWEGKR VFIGNARLME REGISTDELN QSAHKLAEEG KTPMFIASEG
     TLSGMVAVSD PLKEDAKSAV SMLKGMGIEV VMLTGDNKRT AAAIAKEAGI DRFEAEVLPE
     DKASYVKKLQ AEGKKVAMVG DGINDAPALA QADISIAIGT GTDVAMETAN ITLMRGDVMS
     IVTAVRLSKS TMRMIWQNLG WAFGYNIVLI PVAAGLLYPF FGLLLNPMLA GAAMAFSSVS
     VVLNTLRLKK FKTVVPASS
//
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