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Database: UniProt
Entry: C3JWT2_RHOER
LinkDB: C3JWT2_RHOER
Original site: C3JWT2_RHOER 
ID   C3JWT2_RHOER            Unreviewed;       753 AA.
AC   C3JWT2;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   SubName: Full=Copper-exporting ATPase {ECO:0000313|EMBL:EEN84029.1};
DE            EC=3.6.3.4 {ECO:0000313|EMBL:EEN84029.1};
GN   ORFNames=RHOER0001_3553 {ECO:0000313|EMBL:EEN84029.1};
OS   Rhodococcus erythropolis SK121.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN84029.1, ECO:0000313|Proteomes:UP000005836};
RN   [1] {ECO:0000313|EMBL:EEN84029.1, ECO:0000313|Proteomes:UP000005836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK121 {ECO:0000313|EMBL:EEN84029.1,
RC   ECO:0000313|Proteomes:UP000005836};
RA   Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (APR-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:EEN84029.1}.
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DR   EMBL; ACNO01000116; EEN84029.1; -; Genomic_DNA.
DR   RefSeq; WP_003946240.1; NZ_ACNO01000116.1.
DR   AlphaFoldDB; C3JWT2; -.
DR   GeneID; 64142214; -.
DR   Proteomes; UP000005836; 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; 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: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   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; PS01229; COF_2; 1.
DR   PROSITE; PS01047; HMA_1; 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:EEN84029.1};
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   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        108..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        132..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        169..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        396..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        706..723
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        729..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          14..78
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   753 AA;  78183 MW;  E41DD75BE5E50F5E CRC64;
     MTSPTAVDNA ANSSSVELAI TGMTCASCAS RIEKKLNKID GVTATVNYAT EKAKVTFPDG
     VPVEDLVTAV ENAGYSAALP KPPSAPDTVD PDAETPQDRD LRELRTRLII STLLSVPVIA
     MAMIPALQFD NWQWLSLTLA APVIVWAALP FHRAAWVNLR HGAATMDTLI SLGTISAFVW
     SLYALFFGTA GEAGMKHAFR LTVDRMDGSA NIYLEVAAGV ITFVLAGRYF EHKSKRTSGA
     ALRALMELGA KDVAVLRNGV EVRIPAEELA AGDSFIVRPG EKIATDGIIT EGRSAVDMSM
     LTGESVPEEV GVGDTVVGAT VNVGGTLTVE ATRVGSDTQL AQMAALVEDA QNGKAEVQRL
     ADRIAGIFVP VVIAIAVATL GYWLGTGNPI EMAFTAAVAV LIIACPCALG LATPTALLVG
     TGRGAQMGIL IKGPEVLEST RAVDTVVLDK TGTVTTGQMT LLDTVVGEGT TVDEVLRLAG
     ALEHRSEHPI AAAIAKGATE AVGELPTVED FVNVAGRGVQ GMVDGHAVVA GRDALLADWS
     MPLPENLREA KAAAEKAGRT AIAVGWDGKA HGILVIADAV KDTSAEAIAQ LKALGLEPVL
     LTGDNATVAR TVADQVGIST VFAEVMPADK VDAVKKLQAE GRVVAMVGDG VNDAAALAQA
     DLGLAMGTGT DVAIEASDIT LVRGDLRSAA DAIRLSRKTL KTIKGNLFWA FAYNTAAIPL
     AAAGLLNPML AGAAMAFSSV FVVSNSLRLR RFK
//
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