ID A0A2V5JE90_9MICC Unreviewed; 764 AA.
AC A0A2V5JE90;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:PYI37667.1};
GN ORFNames=CVS30_14160 {ECO:0000313|EMBL:PYI37667.1};
OS Arthrobacter psychrolactophilus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=92442 {ECO:0000313|EMBL:PYI37667.1, ECO:0000313|Proteomes:UP000247980};
RN [1] {ECO:0000313|EMBL:PYI37667.1, ECO:0000313|Proteomes:UP000247980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:PYI37667.1,
RC ECO:0000313|Proteomes:UP000247980};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-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:PYI37667.1}.
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DR EMBL; QJVC01000018; PYI37667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5JE90; -.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000247980; 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; 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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 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 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:UP000247980};
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 124..142
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 401..427
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 716..733
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 739..757
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 16..80
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 82..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 764 AA; 78523 MW; E6F78121BD5D6E9A CRC64;
MSASEILTQT ATPGPRMVEI DIEGMTCASC VSRVERKLGK LEGVSAAVNL PLETAQVTVP
AGISDQQILD TVNATGYTAR LKNPPPLKHD GGHHHEQESH PSATPEHTDH MAHGGTAATL
RPRLVLAAIL TVPVFLISMF PALQFPHWGW VVGILTLPVV TWAAWPFHRA AAINARHLAS
TMDTLVSIGV SAAFLFSAVE LGLDPTMTAH GMAMDGAHAR LYFEVSAVVV TFLLLGRYLE
ARAKSKAGDA LKALLSLGAK EATVLRNGVE VKIPATDLAV AEIFVVRPGE KIATDGIITD
GSSAIDTALI TGESMPVDVA VGDAVTGATI NTSGRLLVRA TRVGSETTLA QMGKLVSAAQ
ASKAPIARLA DRISAVFVPI VLAIAVLTFA LWLLFSGDIQ AAFTAAVAVL IIACPCALGL
ATPVGLLTGT GRAAQLGILI KGPQVLEDTR TVDTILLDKT GTVTEGKLSV VDVVALAGLP
ASEVLSFAGA VESRSEHPIA HAIAEHARNW GTLPDVEDFT SSPGGGVRAN IEGRTVLAGR
TGWLEDNGVE LTGPHRAAQT AQQNLGTTAI WVAVDGEVAG LIALKDTIKA GSAAAIATLK
ELGLRPILLT GDNAAVAAQV AAAVGIAPED VYADVLPEGK VSAVKALQAA GATVAMAGDG
VNDAAALAQA DLGIAMGSGT DVAIEAADLT VMGNDLGQVA TAIALSRKTL GTIKTNLFWA
FFYNAIGIPV AALGLLNPMI AGAAMAASSV LVVANSLRLR RFGR
//
