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Database: UniProt
Entry: C0DZD0_9CORY
LinkDB: C0DZD0_9CORY
Original site: C0DZD0_9CORY 
ID   C0DZD0_9CORY            Unreviewed;       716 AA.
AC   C0DZD0;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   SubName: Full=Copper-exporting ATPase {ECO:0000313|EMBL:EEG28356.1};
DE            EC=3.6.3.4 {ECO:0000313|EMBL:EEG28356.1};
GN   ORFNames=CORMATOL_00008 {ECO:0000313|EMBL:EEG28356.1};
OS   Corynebacterium matruchotii ATCC 33806.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=566549 {ECO:0000313|EMBL:EEG28356.1, ECO:0000313|Proteomes:UP000006247};
RN   [1] {ECO:0000313|EMBL:EEG28356.1, ECO:0000313|Proteomes:UP000006247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33806 {ECO:0000313|EMBL:EEG28356.1,
RC   ECO:0000313|Proteomes:UP000006247};
RA   Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA   Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA   Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:EEG28356.1}.
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DR   EMBL; ACEB01000001; EEG28356.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0DZD0; -.
DR   HOGENOM; CLU_001771_0_3_11; -.
DR   Proteomes; UP000006247; 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   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01512; ATPase-IB2_Cd; 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; PR00120; HATPASE.
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; PS01229; COF_2; 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   Hydrolase {ECO:0000313|EMBL:EEG28356.1};
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   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        89..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        112..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        150..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        193..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        348..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        375..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        666..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        689..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          1..48
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          50..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  74963 MW;  FF1C9A557032F717 CRC64;
     MERKLNKVPG AQATVNFATE TANVRYDPAS VKIPQLIDVV RGAGYDAFEI TPDSPTPDND
     AGPELSEASG TDATSAARDA HAADLRKRLI ISAVLSVPVL ALSMIPQLQF DNWQWLSFAL
     VGPVFFYGGK PFHVAALQNL RHGAFTMDTL ISLGTSAAFF WSVWALFFGN AGMNDMRMSM
     SLSAHSHEGM DQIYLESVGM VIVFLLLGRW FETRAKGRSS EALRALLDMG AKDVSVLVDG
     ATHRIPINKL AVGDMFVVKP GEKIATDGVV VEGHSAVDES MLTGESVPVE VTKDSVVTGA
     TMNSSGRLVV RATRVGADTT LAQMAKLVSD AQAKKAPVQK LADRISQVFV PVVILVSVAT
     LLVHAFVLGH GLAEAFTAAV AVLIIACPCA LGLATPTALL VGTGRGAQMG LLIKGPEVLE
     HTQKITTIVM DKTGTITTGI MSVSSIQPEA GFEKDEVLRL AAAVENASEH PIARAIVAEA
     TDIPEVTEFQ STTGVGVSGM VAGRRVEVGR AESGGDTGAT VVAVHVDKQL AGHISVMDQP
     KETSAAAVDK LKAMGLTPIL LTGDNEGAAR QAATKVGIDT VIAGVLPADK VTKVAELQQS
     GQVVAMVGDG INDAAALAQA DLGLAMGAGT DVAIEASDIT LMNDDPRGIV DAIRLSRRTL
     ATIKSNLFWA FAYNIVLIPV AAMGLLNPMF AGAAMAFSSV FVVSNSLRLR GFTSAF
//
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