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Database: UniProt
Entry: A0A0N1KZE0_9PROT
LinkDB: A0A0N1KZE0_9PROT
Original site: A0A0N1KZE0_9PROT 
ID   A0A0N1KZE0_9PROT        Unreviewed;       747 AA.
AC   A0A0N1KZE0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=ATPase P {ECO:0000313|EMBL:KPF48797.1};
GN   ORFNames=IP80_09155 {ECO:0000313|EMBL:KPF48797.1};
OS   beta proteobacterium AAP65.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF48797.1, ECO:0000313|Proteomes:UP000037849};
RN   [1] {ECO:0000313|EMBL:KPF48797.1, ECO:0000313|Proteomes:UP000037849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP65 {ECO:0000313|EMBL:KPF48797.1,
RC   ECO:0000313|Proteomes:UP000037849};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPF48797.1}.
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DR   EMBL; LJHW01000014; KPF48797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1KZE0; -.
DR   STRING; 1523424.IP80_09155; -.
DR   PATRIC; fig|1523424.3.peg.434; -.
DR   Proteomes; UP000037849; 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   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   CDD; cd00371; HMA; 1.
DR   CDD; cd02079; P-type_ATPase_HM; 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; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
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; 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|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037849};
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        110..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        149..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        364..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        392..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        728..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          26..92
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   747 AA;  77699 MW;  93CCAE164305FA27 CRC64;
     MAVLDDPVEF GHGTRWVQGT QGQRLAETSL QLSGMYCAAC SGLIEGALGR VDGVQAASVS
     AASERATVRW DPARTRPSAL IQAVRSAGYD AVPDAAAPAR ALRSQAHRQA LWRLFVAAFC
     GMQVMMLATP SYVAGPGELE PDLRQLLNWG SWLLSLPVLA FSAGPFFRGA WVALRQRRIG
     MDVPVALGVA ITFVASTGAT FSPGGVFGHE VYFDSLTMFV SFLLGARYLE LRARHRAAEA
     LESSLARLPE VAWRVGAEGA VEAVSLQRLR PGDVLRVPLG QAFPADGVLV QGQTRADEAL
     LTGESAPVDK PAGAAVVAGS TNLGAPVLMQ VQRMGGDTRL ETIVAMMRSA SAQRPAAALL
     ADRWAAPFLW TVLLLAAGGA AVWSVIDPSR AVWVAVSVLI VTCPCALSLA APATLVAAAR
     GLARRGVLLQ RLDALERLAR VQQVFFDKTG TLTDDALQLT ATTRTAAGQA RFADDAQALG
     LAASLAAWSQ HPVSRAIAAA QGAAAGAAHD AGWQQVNEVP GQGVQALDAS GRPWRLGQAA
     WVGSSAPQPA GAAAGAHVAL GCDGEVLAWF GFDEALRAGA VAAVQALQAQ GLQLTLLTGD
     APERAQALAQ RLGLQHVLAR ATPEDKLAAV TQAQQAGRTV AMVGDGINDA PVLARADVSL
     AMGQGALVAR SQADAVITSN DLGDLVQARQ RAQHAVRIVR QNMVWAAAYN ATSIPLALMG
     WLPPWAAGLG MALSSLLVIG NALRAAR
//
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