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Database: UniProt
Entry: A0A0M2K4X7_9GAMM
LinkDB: A0A0M2K4X7_9GAMM
Original site: A0A0M2K4X7_9GAMM 
ID   A0A0M2K4X7_9GAMM        Unreviewed;       837 AA.
AC   A0A0M2K4X7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
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   Name=copA {ECO:0000313|EMBL:KKF34425.1};
GN   ORFNames=SY86_23965 {ECO:0000313|EMBL:KKF34425.1};
OS   Erwinia tracheiphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=65700 {ECO:0000313|EMBL:KKF34425.1, ECO:0000313|Proteomes:UP000033924};
RN   [1] {ECO:0000313|EMBL:KKF34425.1, ECO:0000313|Proteomes:UP000033924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BuffGH {ECO:0000313|EMBL:KKF34425.1,
RC   ECO:0000313|Proteomes:UP000033924};
RA   Shapiro L.R.;
RT   "Erwinia tracheiphila.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KKF34425.1}.
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DR   EMBL; JXNU01000004; KKF34425.1; -; Genomic_DNA.
DR   RefSeq; WP_016193059.1; NZ_JXNU01000004.1.
DR   AlphaFoldDB; A0A0M2K4X7; -.
DR   STRING; 65700.SY86_23965; -.
DR   PATRIC; fig|65700.7.peg.5935; -.
DR   Proteomes; UP000033924; 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:0015662; F:P-type ion transporter activity; IEA:UniProt.
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:SF6; COPPER-EXPORTING P-TYPE ATPASE; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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; PS01229; COF_2; 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   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:UP000033924};
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}.
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        218..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        256..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        284..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        437..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        465..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        779..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        804..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          3..64
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          100..163
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   837 AA;  88988 MW;  4CEF16BB640F72ED CRC64;
     MSHTTVLTLT GLSCGHCIKR VKEFLEKRDD VGHAEVSFSE ARILSTASAQ ALIAVVEQAG
     YHASQTEENP LPKSEPLTVP DVAPEALEVD LNKLPAQSEN SANLIIDGMS CASCVTRVEQ
     ALTAVPGVSR VRVNLAERTA LVTGDAGAGA LIESIQRAGY DAEIVEDDRQ RRKKQQQAAD
     KAIRRFRWQT ALALALGVPL MIWGMVGDGM VLTESNRTHW LLSGFLTLLV MVVSGGHFYR
     NAWRSLLKKT TTMDTLVTLG TTAAWVYSTI VTLWPAAFPP ASRHLYYEAS AMIIGLINLG
     HMLEQRARQR SSQALEHLLD LTPATARVVT EGGENIIRLS DVTPGMTLRL ATGDRVPVDG
     MIVQGRAWLD EAMLTGEPMP QEKSTGENIH AGTVVQDGSV LFIASAVGKN TTLSRIINLV
     RQAQSSKPET GRLADRIAAV FVPGVLIIAM CSALIWYLLG PAPQLVYTLM VAMTVLMIAC
     PCALGLATPM SIIAGVGRAA EAGILIRDAD ALQRASSLDV LVFDKTGTLT EGAPHIVDIT
     LFDDMTESQA LSWAAALEQG SQHPLACAIC HRAEGIDLPE ISQFRTLPGQ GVSGNIGETA
     LLLGNSMLLS QQNIAITEAA AQIATQSAKG ITPVLLAANG KIKAVFSVRD PLRDSSITTL
     KRLKNRGYQL MMLTGDNRAT ALAVAQEAGI EKVIADVLPE GKAEAIRRLQ QQGFRVAMIG
     DGINDSPALA QADVGIAMGG GSDVAIETAG MTLMRHDLTA LADGLAIAKA TLRNMKQNLL
     GAFIYNALSI PVAAGVLWPF TGTLLSPVVA AAAMALSSVT VVSNANRLLR YRPPAIA
//
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