ID A0A366IJJ7_9MICO Unreviewed; 737 AA.
AC A0A366IJJ7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Cu2+-exporting ATPase {ECO:0000313|EMBL:RBP72321.1};
GN ORFNames=DFO65_104279 {ECO:0000313|EMBL:RBP72321.1};
OS Brevibacterium celere.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=225845 {ECO:0000313|EMBL:RBP72321.1, ECO:0000313|Proteomes:UP000253509};
RN [1] {ECO:0000313|EMBL:RBP72321.1, ECO:0000313|Proteomes:UP000253509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3b_TX {ECO:0000313|EMBL:RBP72321.1,
RC ECO:0000313|Proteomes:UP000253509};
RA Lamendella R.;
RT "Freshwater and sediment microbial communities from various areas in North
RT America, analyzing microbe dynamics in response to fracking.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:RBP72321.1}.
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DR EMBL; QNSB01000004; RBP72321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366IJJ7; -.
DR Proteomes; UP000253509; 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 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; 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; 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 PROSITE; PS00154; ATPASE_E1_E2; 1.
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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000253509};
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 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 120..138
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 186..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 337..359
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 365..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 677..695
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 701..722
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 76745 MW; BA9B6AD4B798D471 CRC64;
MADQVERDAH EHHSEDSSNA GPAGHTDHAG HSHHPGHGDH EGHPGHSAGH SGHSGHAGHS
GHGDHVGQFR RLFWIMLVFA IPVIGFSPMF AHLVGYEIPG AAGAAGAPAT GAEHGGDTPL
GWLAWISPLL GTVMYVWGGR PFLTGGWSET RSRKPGMMLL ISLAITVALL SSWGASLGLL
HPELEFWWEL ALLIVIMLAG HWIEMRSLAQ TTSALDSLAA LLPDEAETVV GDEVVTVSPA
DLRVGDIVIV RPGSAVPADG RIIDGSASMD ESMITGESRT VRRGHGDGVV AGTVATDSGV
RIEVTATGDD TALAGIRKLV SDAQSSTSRA QRIADTAAAW LFWFALGVAV VTALVWSVLG
LPDDAVVRTI TVLVIACPHA LGLAIPLVVS IATERAARAG ILIKDRLALE TMRTVDTVLF
DKTGTLTKGE PTVTAVEAAD DAEARAEAVL ALAAAAESDS EHPLAKAIVR AAADRELEIP
RAADFSSSPA VGVRARVDGA EVEVGGPHLL SSRGVSELSI AEDWREEGAI ILHVLRDSTV
IGALRLADEI RPESREAVDA LHAAGSQVVM ITGDAEAVAQ SVADELGIDR VFAGVRPEAK
AAKVRQLQDE GRRVAMVGDG VNDAPALAQA DVGIAIGAGT DVAIGSAGVI LASDDPRAVL
SVGELSRATY RKMKQNLWWA AGYNLISVPL AAGILAPVGF ILPMSVGAIL MSASTVVVAI
NAQMLRRLDL RPESLAS
//