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
//