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Database: UniProt
Entry: V7PWH4_9BACT
LinkDB: V7PWH4_9BACT
Original site: V7PWH4_9BACT 
ID   V7PWH4_9BACT            Unreviewed;       746 AA.
AC   V7PWH4;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   13-SEP-2023, entry version 47.
DE   RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN   ORFNames=O210_OD1C00001G0447 {ECO:0000313|EMBL:ETB63969.1};
OS   Parcubacteria bacterium RAAC4_OD1_1.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1394712 {ECO:0000313|EMBL:ETB63969.1, ECO:0000313|Proteomes:UP000018547};
RN   [1] {ECO:0000313|EMBL:ETB63969.1, ECO:0000313|Proteomes:UP000018547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA   Castelle C.J., Thomas B.C., Banfield J.F.;
RT   "Small genomes and sparse metabolisms of sediment-associated bacteria from
RT   four candidate phyla.";
RL   Submitted (NOV-2013) 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}.
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:ETB63969.1}.
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DR   EMBL; AWSN01000001; ETB63969.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7PWH4; -.
DR   STRING; 1394712.O210_OD1C00001G0447; -.
DR   PATRIC; fig|1394712.3.peg.419; -.
DR   Proteomes; UP000018547; 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; TIGR01512; ATPase-IB2_Cd; 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; 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:UP000018547};
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        96..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        166..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        197..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        353..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        383..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        692..715
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        721..739
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          2..68
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   746 AA;  81124 MW;  2DFA5F18BEAB5EAF CRC64;
     MKNKIFKIEG MHCASCATII SKEVSKLPGI NKVNVNFANE KAKIDFDENK TNLEIMNSSI
     EKLGYHIVDQ EGSTPYNQMK TKSDIEEINN KSKTKFIMPI SIIVFFIMMW DILAKTSSLV
     PNIPIPMELL NTIMMIISTI VLFYIGKPFL KGVTRFIRYG KANMDTLIGI GTLTAYIYSS
     IITLFPQVNM AMNLPDYTYF DVVIVVIGFI TFGKYLESRS KKKTGEAIEK LIKLGAKTAI
     VKRDGKEIEI EVSEVKVGDM IIVKPGMKIP VDGKITEGTT SIDESMITGE SMPVDKKVGD
     IVTGATINKQ GSIVFEATKV GEETVLSSII KMVENAQGSK APIEALADRV SNIFVPTVLI
     VAFITLILWM IIGIPILGKS IAISYGLLSF VGILVIACPC ALGLATPTAI IVGVGKGAEH
     GILIKDAESL EKLSKVDTIV LDKTGTITKG KPEVTNIVSL DSIYKETDII KITASLEALS
     EHPLGLAIKN YALSQNIILN KVDDFAALEG IGVKGKIKDL NVFIHKPEDK DINEELRELQ
     NEGKTVIIIE VENKKIGLMA LSDTIKDNAK ETINKLHKKG IKVIMLTGDN HLAAKYIADQ
     VNIDNVYSEV LPKDKIDKII SLQKEGRIVA MAGDGINDAP ALTEADVGIA MATGSDIAIE
     SAGITLLNGD IHKLSEAIIL SKKTFATVKQ NLFWAFIYNV IGIPIAAGIL FPIWGIILNP
     IFAGLAMALS SVSVVGNSLR LKVKKI
//
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