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Entry: A0A1Q2SK08_9GAMM
LinkDB: A0A1Q2SK08_9GAMM
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ID   A0A1Q2SK08_9GAMM        Unreviewed;       818 AA.
AC   A0A1Q2SK08;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:BAW79459.1};
GN   ORFNames=TAO_0089 {ECO:0000313|EMBL:BAW79459.1};
OS   Candidatus Nitrosoglobus terrae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Candidatus Nitrosoglobus.
OX   NCBI_TaxID=1630141 {ECO:0000313|EMBL:BAW79459.1, ECO:0000313|Proteomes:UP000243679};
RN   [1] {ECO:0000313|EMBL:BAW79459.1, ECO:0000313|Proteomes:UP000243679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAO100 {ECO:0000313|EMBL:BAW79459.1,
RC   ECO:0000313|Proteomes:UP000243679};
RX   PubMed=28072419; DOI=10.1038/ismej.2016.191;
RA   Hayatsu M., Tago K., Uchiyama I., Toyoda A., Wang Y., Shimomura Y.,
RA   Okubo T., Kurisu F., Hirono Y., Nonaka K., Akiyama H., Itoh T., Takami H.;
RT   "An acid-tolerant ammonia-oxidizing ?-proteobacterium from soil.";
RL   ISME J. 11:1130-1141(2017).
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; AP014836; BAW79459.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q2SK08; -.
DR   KEGG; ntt:TAO_0089; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000243679; 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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   CDD; cd00371; HMA; 2.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 2.
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; IPR006122; HMA_Cu_ion-bd.
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   NCBIfam; TIGR00003; copper ion binding protein; 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; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
DR   PRINTS; PR00942; CUATPASEI.
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; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 1.
DR   PROSITE; PS01047; HMA_1; 2.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022796};
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:UP000243679};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT   TRANSMEM        189..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        216..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        249..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        273..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        429..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        460..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        767..784
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        790..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          26..92
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          94..160
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   818 AA;  87298 MW;  80AECFA15B821A9F CRC64;
     MPKTSALNAI KTPISQDSAK LEEKIQTLTL PIKGMTCASC SNRLERVLSK QFGIIQSQVN
     LALEQAHIHF NPKLISTQAI YQLITQAGFT VPMETLDFNI DGMTCTACTV RLEKVLDRLS
     GVSKVAIHLA TEKAMITAPT GVLSSDTVIT AVQQAGFTAK PLLSVADREA QEKAQTSAKD
     RYELRQLQLA ALLTFPLTLP MLMMPFGIHI DLAPWIQFLL ATPVQFWIGR HFYVGAYKSL
     RGGIGNMDVL VSLGTSAAWG LSTWNILISS NDYLYFEASA MVITLVLLGR RLEGRAKRSA
     ASAIRALMAL RPATAQIERA GKIITIPAEQ VVTDDIVLVR PGEHIPVDGV IIEGSSQLDE
     SMITGESLPV ARGKGEAITG GSVNGEGLLR IQATTVGAES TLARIIQLVE NAQSSKAPVQ
     KLVDQVTHIF VPVVVTIAFL TFAGWWLLEG STETAFKAAI SVLVIACPCA LGLATPTALM
     VGTGTAARHG ILIRDAIALE RAQNSDTVVF DKTGTLTEGQ PAVDLVLPVE DSAETLLQLV
     ASAQQGSEHP LAKAVLAKAQ GMALSPPQNF RNFPGKGFST QIQERTILVG NRRLMEENQI
     DISLLQAQAA TFEKTGHTII WVAEINSPSR LLGILTATDP IKAVTSQAIS SLQSRGLTVV
     MLTGDNSGAA QAVADKIGIK QVIAEVLPED KTNQIQTLQA QGRRVIMVGD GVNDAPALAT
     ADVGMAMGTG TDVAMETAGI ILMRGDPSLV TAALSISRAT YQKIRQNLFW AFVYNILAIP
     LAAFGMLNPV VAGAAMAMSS VSVVSNSLLL RRWQPKLI
//
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