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Database: UniProt
Entry: A0A173LV42_9MICO
LinkDB: A0A173LV42_9MICO
Original site: A0A173LV42_9MICO 
ID   A0A173LV42_9MICO        Unreviewed;       740 AA.
AC   A0A173LV42;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Copper-transporting P-type ATPase {ECO:0000313|EMBL:BAU98815.1};
GN   ORFNames=AUMI_12730 {ECO:0000313|EMBL:BAU98815.1};
OS   Aurantimicrobium minutum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Aurantimicrobium.
OX   NCBI_TaxID=708131 {ECO:0000313|EMBL:BAU98815.1, ECO:0000313|Proteomes:UP000243847};
RN   [1] {ECO:0000313|EMBL:BAU98815.1, ECO:0000313|Proteomes:UP000243847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNC {ECO:0000313|EMBL:BAU98815.1,
RC   ECO:0000313|Proteomes:UP000243847};
RA   Nakai R., Fujisawa T., Nakamura Y., Nishide H., Uchiyama I., Baba T.,
RA   Toyoda A., Fujiyama A., Naganuma T., Niki H.;
RT   "Complete Genome Sequence of Aurantimicrobium minutum Type Strain KNCT, a
RT   Planktonic Ultramicrobacterium Isolated from River Water.";
RL   Genome Announc. 4:e00616-16(2016).
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; AP017457; BAU98815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A173LV42; -.
DR   KEGG; amin:AUMI_12730; -.
DR   OrthoDB; 7059309at2; -.
DR   Proteomes; UP000243847; 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; 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; 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:UP000243847};
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        98..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        121..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        159..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        202..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        354..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        382..407
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        689..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        715..733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          7..71
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   740 AA;  77899 MW;  57BB564BA5990A8C CRC64;
     MAEKTTSTVV LGIEGMTCSS CVSRVEKSLG ELPGVHAAVN LATNSAKVEY PEGVSAEDLV
     KQVSKIGYTA TLPAADQHSH IHHEHGSKPG KISLLERLVI AIVLSVAVII LAMVPAWQFS
     YWQWISLLLT TPVVFFCGWP FHRSTFLNLR HGILTMDTLI TMGTFAAYFW SVYALFFGAA
     GMVGMHHTLE LFAWQSDPTH NIYFEAAAGV TTFLLLGRFL EERSQRSASA ALRALSELKA
     TEATILVDGV EKRIPADKLA VGDIFIVKPG EIIATDGEVI NGQAAVDESS LTGESLPVDK
     SPESAVTGST IVLDGRLTVR ATHVGQNTRM AQLATLVEDA QLHKAAVQKL ANRISAVFVP
     IVIGLAVITI LGWWIAGAPV TVGFTAAIAV LVIACPCALG LATPVALMVG TGRAAQMGII
     ISGPDAIESS ARIKTVVLDK TGTVTTGQMS VTSIHTTGAH HDVLRIIAAL ETHSEHPIAH
     AIVSKAEGLK LPAVSEFSSV AGQGVTGVVE GVIVFVGTQD WMEQHQLVLS DTQAVQLETA
     RHTGATTVLA GWDGKVQAIV AVADTIKDDS AAAITRINQM GLETILLTGD HEDAAHHIAA
     QVGISRVIAG ATPESKLQVI ADLQKRGGAV AMIGDGVNDA AALAQSDLGI AMGTGTDVAI
     AASDITLIRG TLTAAADALS LSRKTLRIIY GNLFWAFAYN VAAIPLAMLG FLNPMLAGAA
     MAFSSLFVVL NSLRLRRFAR
//
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