ID A0A1I1CIV0_9PSEU Unreviewed; 761 AA.
AC A0A1I1CIV0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Cation-transporting ATPase V/Cu+-exporting ATPase {ECO:0000313|EMBL:SFB62601.1};
GN ORFNames=SAMN05216266_13120 {ECO:0000313|EMBL:SFB62601.1};
OS Amycolatopsis marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=490629 {ECO:0000313|EMBL:SFB62601.1, ECO:0000313|Proteomes:UP000243799};
RN [1] {ECO:0000313|Proteomes:UP000243799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3568 {ECO:0000313|Proteomes:UP000243799};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOKG01000031; SFB62601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1CIV0; -.
DR STRING; 490629.SAMN05216266_13120; -.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000243799; 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:UP000243799};
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 101..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 160..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 342..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 370..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 679..696
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 702..720
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 13..79
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 727..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 80256 MW; 17FE83A7555862E2 CRC64;
MTLQQERSET DRQRLVFGVG GMHCASCAGR IERTLARQER VASAEVNFGS AQAVVEFEGP
APDSEALEAA VSDQGYTLSP HQPEAPPEAV TDAHRREQHS WGWRVLLAWP LGIAVMVLAL
AYGDSPTAGY LEWILTTPVQ FVLAWPILTD AAARARHRQL NMNSLIALGT LTAYTFSLVQ
LLRDPGSDLY FETAALILAF ILLGRYFEAR AKGRASRAIT ALLELGAKQA RVRRDDGTEE
LVDVDEVEPG QLLVVRPGEK VPTDGVVVEG ASAVDESMLT GESVPVDKAV GDTVIGATVN
AGGLLVVRAT NVGSDTALAQ IVRVVEQAQG GKPAIQRLAD RVAAVFVPVV AAVAALAFLG
WATIGGAPVH GLVAAVAVLI IACPCAVGLA TPMAIMVGTG RGAALGVLIK GGEVLEQSRR
VDTVVFDKTG TLTHGAMRLV GTVGDPETLE LAAGVESGSE HPVGQAVVEA AKEQEITVPW
VTEFAAVAGR GVAGTVHGRR VVVGRAILLS DEDWAIPAEL TAEAERFEQE AATAFYVGWD
GQARGVLAVA DTVKEQAVEV VRDLHGMGLQ TVMITGDNRR TAEAIAKEVG IDRVLAEVLP
EDKLSEVARL QDEGRRVAMV GDGVNDAPAL VQADLGIAIG TGTDVAIESS DLTLIGGSLD
GVVTAIELSR RTYRTIMQNL FWAFAYNTLL IPVAALGFLS PIFAGAAMAI SSVTVVTNSL
RLTRFGRRRG NGSGQVRARA TSGSDRKDTD DEQLPADRLS R
//
