ID A0A1M5EYM5_9GAMM Unreviewed; 802 AA.
AC A0A1M5EYM5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Cu+-exporting ATPase {ECO:0000313|EMBL:SHF84246.1};
GN ORFNames=SAMN02745148_03663 {ECO:0000313|EMBL:SHF84246.1};
OS Halomonas ilicicola DSM 19980.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1121942 {ECO:0000313|EMBL:SHF84246.1, ECO:0000313|Proteomes:UP000184346};
RN [1] {ECO:0000313|EMBL:SHF84246.1, ECO:0000313|Proteomes:UP000184346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19980 {ECO:0000313|EMBL:SHF84246.1,
RC ECO:0000313|Proteomes:UP000184346};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
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; FQUJ01000028; SHF84246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5EYM5; -.
DR STRING; 1121942.SAMN02745148_03663; -.
DR Proteomes; UP000184346; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd02094; P-type_ATPase_Cu-like; 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; IPR045800; HMBD.
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; PF19335; HMBD; 2.
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:UP000184346};
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 146..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 211..238
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 250..269
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 408..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 432..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 748..767
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 773..795
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 38..64
FT /note="Heavy metal binding"
FT /evidence="ECO:0000259|Pfam:PF19335"
FT DOMAIN 100..124
FT /note="Heavy metal binding"
FT /evidence="ECO:0000259|Pfam:PF19335"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 84179 MW; D81EB6126DEFCE84 CRC64;
MTQHQHDHCH GHASHEAPTR GSGDTDQHAA GSQGGAQYTC PMHPEVVSDQ PGDCPKCGMH
LVPVGSDDSQ THDGHGHGAS APAHGGKYDK VPAGHAGAIY TCPMHPEVRQ TDPGACPLCG
MGLELESAAV GDEGPNPELV DFTRRFWVAA VLTLPVLILT MSPYLGLGAI RDFFGERNAM
WIELVLSTPV ILWSGWPFFV RGYNSFRTMN LNMFSLIGMG VGAAYLFSIV AVLVPGVFPD
GFRREDGSVG VYFEAAAVIV TLVLLGQVME LRAREGTGKA IRALLDMAAK TARVIRPDGS
EEEIPLEDVQ VGDHLRVRPG DKVPVDGMVV EGRSSIDESM ISGEPVPVEK VQGDQVTGAT
INGTGSLVME ATRVGADTML SQIVEMVAAA QRSRAPIQKF ADKVAGKFVP AVIGVAILSF
ISWAIWGPAP ALSYALVSAV AVLIIACPCA LGLATPMSIM TATGRGAQAG VLIKNAEALE
RFAKVDTLMV DKTGTLTEGK PKLVAVLPEE GHDEAEVLRL AASLEKGSEH PLAEAIVAGA
EERGVSLADA TDFEAVTGMG VKGVVDGKSV ALGNAKLMAE LGLDGGRISE TANARRDEGE
TVMFVVLDGQ IAGLVSVADP VKATTPDALK ALHRLGFRII MATGDNERTA KAVAGRLGID
EIRADVMPED KARIIKELQA EGRKVAMAGD GVNDAPALAQ ADVGIAMGTG ADVAIESAGF
TLVKGNLDGI VRARKLSLAT MRNIKQNLFF ALIYNGAGVP IAAGILYPFL GILISPMFAA
FAMTASSLSV VLNALRLRRV RI
//
