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Database: UniProt
Entry: A0A0C9PVV9_9BACT
LinkDB: A0A0C9PVV9_9BACT
Original site: A0A0C9PVV9_9BACT 
ID   A0A0C9PVV9_9BACT        Unreviewed;       833 AA.
AC   A0A0C9PVV9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Cation transport ATPase {ECO:0000313|EMBL:GAN31622.1};
GN   ORFNames=BROSI_A0123 {ECO:0000313|EMBL:GAN31622.1};
OS   Candidatus Brocadia sinica JPN1.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Brocadia.
OX   NCBI_TaxID=1197129 {ECO:0000313|EMBL:GAN31622.1, ECO:0000313|Proteomes:UP000032309};
RN   [1] {ECO:0000313|EMBL:GAN31622.1, ECO:0000313|Proteomes:UP000032309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPN1 {ECO:0000313|EMBL:GAN31622.1,
RC   ECO:0000313|Proteomes:UP000032309};
RA   Oshiki M., Shinyako-Hata K., Satoh H., Okabe S.;
RT   "Draft Genome Sequence of an Anaerobic Ammonium-Oxidizing Bacterium,
RT   "Candidatus Brocadia sinica".";
RL   Genome Announc. 3:e00267-15(2015).
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:GAN31622.1}.
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DR   EMBL; BAFN01000001; GAN31622.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9PVV9; -.
DR   Proteomes; UP000032309; 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:0005507; F:copper ion binding; IEA:InterPro.
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   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; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
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:UP000032309};
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        111..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        139..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        173..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        354..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        387..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        699..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        724..744
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          23..89
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          755..821
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   833 AA;  91247 MW;  D9F0F4AE1B7FEB99 CRC64;
     MAVVSECYII KMLVETEIEK QNKKLQVKVG GISCSFCAES IRKAYRRIDA VKDVNVSLAH
     EEVLIQYDPE KITETELKNT VRQLGYTVRD PKKARTYEEE EAELQREKWR LIIAAGFTGT
     AALLMNSMWV GYYQSWFKWL MMRLAFATIF GPGWYIFTMA VHSLRRRILN QHVLLESGAF
     AGLFGGFAGF FLKNFPITDF FQVAVSLTTY HILSGYLSLR VRTRVSQAVR KLLALQPPIA
     RVIRNGREEE VPIENVQVGD RVRVRPGEQI PVDGEVVDGV SVVDESLVTG ESMPVEKSVG
     NEVIGGSLNQ AGTLIVKVMR VGEESFLQQV ARHIEEARAL KPGIIQLVDK ILKYYVPGVL
     ICAILGITIW TLGAWLVTGE VNLTRGIFAA LAVLVMGYPC ALGMATPLAM IYGGGVAARK
     GILIRSSEAF QALKDTRVVV LDKTGTITEG KPKVVDVIPI RTFDDREVLQ IAASAEKPSE
     HPLARAIVNH AQTLDITLTD IGQFQAVPGK GARAMMNGRA VCVGSLRYFA EEDVEVDKGY
     NEAKAFEEQG KTVVGVSIDK EFLGLITVAD TLKEDALETV HQMKEIGLRP VMITGDNQRT
     AQAVARQVGI DEVIAEAMPD EKVTQVRKLQ AQGYRVAMVG DGINDAPALM QADVGIAIGA
     GTDIAIESAD VILIGNRLGG VLDAYLIGRN SYKKTQQNLI LAFIFNGIGV PAAATGFFHP
     GWAMIAMVAS VSTVLLNSFG SRLLSAKKMK AKERQVVTFD IPNMHCEGCL DTIRTALEKR
     IGVAEVKADL EKHLLEIISY NKDISPEGIK ELLTEAGFKP SELTKNLPAP ISN
//
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