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Database: UniProt
Entry: A0A0D9A011_9CYAN
LinkDB: A0A0D9A011_9CYAN
Original site: A0A0D9A011_9CYAN 
ID   A0A0D9A011_9CYAN        Unreviewed;       806 AA.
AC   A0A0D9A011;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:KJH72796.1};
GN   ORFNames=UH38_04350 {ECO:0000313|EMBL:KJH72796.1};
OS   Aliterella atlantica CENA595.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC   Aliterellaceae; Aliterella.
OX   NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH72796.1, ECO:0000313|Proteomes:UP000032452};
RN   [1] {ECO:0000313|EMBL:KJH72796.1, ECO:0000313|Proteomes:UP000032452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CENA595 {ECO:0000313|EMBL:KJH72796.1,
RC   ECO:0000313|Proteomes:UP000032452};
RA   Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA   Fiore M.F.;
RT   "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT   from South Atlantic Ocean.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:KJH72796.1}.
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DR   EMBL; JYON01000003; KJH72796.1; -; Genomic_DNA.
DR   RefSeq; WP_045053410.1; NZ_JYON01000003.1.
DR   AlphaFoldDB; A0A0D9A011; -.
DR   STRING; 1618023.UH38_04350; -.
DR   PATRIC; fig|1618023.3.peg.738; -.
DR   OrthoDB; 438550at2; -.
DR   Proteomes; UP000032452; 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   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; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF19; COPPER-TRANSPORTING ATPASE PAA2, CHLOROPLASTIC; 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; 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   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01229; COF_2; 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:UP000032452};
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        120..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        180..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        371..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        437..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        753..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        778..802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          20..85
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   806 AA;  84990 MW;  96EB33C119CA25E4 CRC64;
     MQLVPKTVPL TASNSTLATK KITLDVGSMK CGGCVKTVER LILQQPGAIA ACVNLVTEVA
     VVECQADTDP LEIAAKLTNA GYPTKPRFAQ VPHLEEESTL ALEDPQQKQQ REMRSARRQI
     ITSAVLLILS SLGHLPESLL GFALLKNIWL HWGLATITLL LPGREIILDG WRGLKRNAPN
     MNTLVALGTL TAYTTSVVAL LFPQLGWECF FDEPVMLLGF ILLGRTLEQQ ARGKAAAAFK
     RLLALQPQVA RLIAQPQGEF AVSDRQSSVE IPADRVRVGE WLQVLPGEKI PVDGEVVAGQ
     TTVDESMLTG EAMPQVKQSG DVVTAGTLNK SGAIALRATR TGSDTTLAQI VDLVEAAQTR
     KAPVQKLADT VAGYFTYGVL AAALLTFLFW YFIGTHIWTD VLTIAHPAMS EHASLHTQHL
     ANAQILAPSP LLLSLKLAIS VMVVACPCAM GLATPTAILV GTGVGAEQGL LIKGGDVLER
     VHQLDTVVFD KTGTLTSGHP TVTDCILVAD DVLPSDLLQI AAAVESGTSH PLAAAIVQAA
     QKQNLSIPAA KDFYTEPGLG VSAQLKDGVT VLVGNAQWLS QNAVNISDTA SLQAQTLAAT
     GKTVVFVATG DCLIGLIAAS DTLRADASQV VESLRAGLGL KVMLLTGDKL TAAKAVAAQL
     GISDEDIIAD IRPAGKAAAI QQLQAQQQRV AMVGDGINDA PALSQADVGI ALKAGTDVAM
     EAAQIVLMRD RLTDVVAAIE LSKATFQKIR QNLFWAFAYN TLGIPIAAGV LLPSLDFVLS
     PAAAGALMAF SSVSVVTNSL LLRRFK
//
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