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Database: UniProt
Entry: A0A0U5BLT4_9MICO
LinkDB: A0A0U5BLT4_9MICO
Original site: A0A0U5BLT4_9MICO 
ID   A0A0U5BLT4_9MICO        Unreviewed;       751 AA.
AC   A0A0U5BLT4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:BAU31126.1};
GN   ORFNames=MalAC0309_0251 {ECO:0000313|EMBL:BAU31126.1};
OS   Microcella alkaliphila.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microcella.
OX   NCBI_TaxID=279828 {ECO:0000313|EMBL:BAU31126.1, ECO:0000313|Proteomes:UP000218965};
RN   [1] {ECO:0000313|Proteomes:UP000218965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM AC0309 {ECO:0000313|Proteomes:UP000218965};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAU31126.1, ECO:0000313|Proteomes:UP000218965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM AC0309 {ECO:0000313|EMBL:BAU31126.1,
RC   ECO:0000313|Proteomes:UP000218965};
RA   Kurata A., Hirose Y., Kishimoto N., Kobayashi T.;
RT   "Microcella alkaliphila JAM AC0309 whole genome shotgun sequence.";
RL   Submitted (JAN-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; AP017315; BAU31126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U5BLT4; -.
DR   KEGG; malk:MalAC0309_0251; -.
DR   OrthoDB; 7059309at2; -.
DR   Proteomes; UP000218965; Chromosome.
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; 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   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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   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        100..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        124..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        161..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        357..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        385..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        697..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        723..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          4..72
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   751 AA;  76956 MW;  4AAF517C091EC4A6 CRC64;
     MTTAPLQLEI GGMTCAACAG RVERSLSRLG GVTASVNYAT EKATVTLADD ADALPTIDEL
     VAAIEKAGYS ATPVAPPSEA RASTAQGDAP DPLADARRRL AIVVALTVPV LVLSMVPPLQ
     FPNWQWLVLA LSSPVAVWGA WPFHRAAFMN ARHGTATMDT LISVGVGAAF GWSLYTLFFG
     EAGMTGMVMS LQLFGSPDTG SHEIYLEVAA AVTAFMLAGR YLEAKAKRAS GEALRALLEL
     SATDATVLRD GVETRVAVDQ LVVGDRFIAR PGDTIATDGL VRDGATAVDT SVMTGESKPV
     EVAVDARVVG GTVNVGPGVI TVEATRIGAD TELARLGRLV EEAQTGKARV QRIADRVSAI
     FVPVVMVLSL LALLGWLLFG GTIEQAFTAA VTTLIIACPC ALGLATPTAL LVGTGRGSQL
     GILIRGPEVL EQTRRVDTIV LDKTGTLTTG RMRVTAVLPA AGIAEERVLA AAAGAESGSV
     HPVAAAIVEA AREAGAATGA VEGFQAHDGA GVSAVVDDRA VAVGRADWLT SAWSVEVGDD
     VRADIAHREN DGMTVVAVAI DGAYAGLIAI SDAVRPEAGA TIARLRALGL TPVLLTGDNA
     GAAARVAEQL GIDDVRSGVT PVGKLEAIRG LQADGHVVAM LGDGVNDAAA LAAADLGIAM
     GSGTDAAMAA SDLTIVSGDL SLVPDAVRLA RRTLRTIIGN LFWAFGYNTA AIPVAMMGLL
     SPVLAALAMA VSSLFVLGNS LRLRSFAPEP R
//
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