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Database: UniProt
Entry: A0A2U2RKC5_9MICO
LinkDB: A0A2U2RKC5_9MICO
Original site: A0A2U2RKC5_9MICO 
ID   A0A2U2RKC5_9MICO        Unreviewed;       771 AA.
AC   A0A2U2RKC5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:PWH06310.1};
GN   ORFNames=DEO23_04810 {ECO:0000313|EMBL:PWH06310.1};
OS   Brachybacterium endophyticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=2182385 {ECO:0000313|EMBL:PWH06310.1, ECO:0000313|Proteomes:UP000245590};
RN   [1] {ECO:0000313|EMBL:PWH06310.1, ECO:0000313|Proteomes:UP000245590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1HQ-2 {ECO:0000313|EMBL:PWH06310.1,
RC   ECO:0000313|Proteomes:UP000245590};
RA   Tuo L.;
RT   "Brachybacterium sp. M1HQ-2T, whole genome shotgun sequence.";
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:PWH06310.1}.
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DR   EMBL; QFKX01000002; PWH06310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2RKC5; -.
DR   OrthoDB; 7059309at2; -.
DR   Proteomes; UP000245590; 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; PR00120; HATPASE.
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; PS01229; COF_2; 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:UP000245590};
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        121..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        144..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        182..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        225..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        377..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        405..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        719..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        744..761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          17..81
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          78..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  79565 MW;  9EA7BC1C97D01EC7 CRC64;
     MSVTDAHERT GAEEPLRDVD LDIGGMTCAS CANRIERKLN RLDGVRASVN FATEAAHVSA
     PAAMDAQTLI GEVAKAGYTA TLPPDPDPED GVERGAGDDD ADDGSSAVAA DPELVDLRGR
     LLGAAVLGIP VILLSMIPAL QFTYWQWLVL ALAAPVVLWS GWPFHRAAAV NARHGAATMD
     TLISIGTVAA FLWSLYALFL GDAGIAGMRH EFSLRIARST EADAIYLEVA AGVTLFVLAG
     RYIEKRSKRR AGAALRALLH LGAKDVAVLR DGVETRIPVG RLAVGDRFVV RPGEKIATDG
     QVVAGRSAVD ASMLTGESVP QEVVPGDVVT GATVNQGGRI VVRASRVGAG TQLAQMARLV
     RDAQSGKAGV QRLADRISGV FVPIVLAIAL ITLIAWLLTG HGAEAAFTAA VAVLIIACPC
     ALGLATPTAL LVGTGRGAQL GILIKGPEVL ESTGGLDTVV LDKTGTVTTG RMSLVDVHVA
     DGVSGTELLR RAGAVEDASE HPIAQAIARG AGELVGDLPE ASDFEALPGR GVRGLVDGVE
     VSVGREVGEA AALEIPPALA AAVADAEADG RTAVAVAWGG AVRGVLTVAD AIRPTSAQAV
     ARLRELGLRP VLLTGDGRRV AETIASQAGI DEVIAGVMPE DKVAVVRRLQ YEGRRVAMVG
     DGVNDAAALA RADLGIAMGS GTDAAIQAAD ITLVRGDLRS AADAVRLARR TLRTIRGNLF
     WAFAYNVAAI PLAALGLLNP MLAGATMAFS SVFVVLSSLR LRTFRESGSG R
//
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