ID A0ZAE8_NODSP Unreviewed; 812 AA.
AC A0ZAE8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Lead, cadmium, zinc and mercury transporting ATPase Copper-translocating P-type ATPase {ECO:0000313|EMBL:AHJ26423.1};
DE EC=3.6.3.3 {ECO:0000313|EMBL:AHJ26423.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:AHJ26423.1};
GN ORFNames=NSP_660 {ECO:0000313|EMBL:AHJ26423.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ26423.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ26423.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ26423.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
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}.
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DR EMBL; CP007203; AHJ26423.1; -; Genomic_DNA.
DR RefSeq; WP_006194389.1; NZ_CP007203.1.
DR AlphaFoldDB; A0ZAE8; -.
DR STRING; 313624.NSP_660; -.
DR GeneID; 78015462; -.
DR PATRIC; fig|313624.11.peg.66; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_3; -.
DR Proteomes; UP000019325; 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; 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 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 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 Hydrolase {ECO:0000313|EMBL:AHJ26423.1};
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 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 113..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 145..164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 432..459
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 756..775
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 787..805
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 18..84
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 79..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 86342 MW; BE1BA70A37810708 CRC64;
MQLAPKNQLT PEPAPTSEKI ILDVGGMKCA GCVSAVERQL TQYPGVKSAC VNLATEVAVV
ESETGAVDPQ TLAQRLTSAG FPSQPRQARE KLANESTLQD PEERKRREMR SSFGQLIIAG
VLLVLSGIGH FGSMGGQILP ILNNIWFHCG LATVAILIPG RPILVDGWRG WRRNAPNMNT
LVGLGTLTAY TASLIALLFP QMGWECFFDE PVMMLGFILL GRTLEQQARG RASAAFRELL
SLQPQIARLI PNPNPEKLGL GTNIVEIPAE NVRVGEWLQV LPGDKIPVDG EVRFGKTTVN
ESMLTGEAVP VIKQPGDLVA AGTLNESGAI AIIATRTGSD TTLAQIVTLV ETAQTRKAPV
QKLADTVAGY FTYGVLTASV LTFVFWFFFG THIWNDVSMS GGMDMMSHAP LSSPEAMERV
STHSPLLTSL KLAIAVMVVA CPCALGLATP TAILVGTAIG AERGLLIKGG DVLERVHELD
TVVFDKTGTL TTGNPTVTDC LPFEEWEDNK PYSLLQLAAA VESGTYHPLA KAIQQAAQEQ
KLSIPDAVDF HTEPGLGVSA IVEGLSVLLG NWDWLSKHGV FASEAAQQIA LHLAENGKTV
VGVAVGGNLA GLIAVEDPLR PDAEATVNQL REMGLRVMLL SGDRLEAAHA IAKQLGLDSA
DVMAGILPGK KADVIKSLQL QGKSQSPTPH SVVAMVGDGI NDAPALSQAD VGIALYSGTD
VAMETAEIVL MRDRLNDVVA SIKLSRATFN KIRQNLFWAF AYNTIGIPLA AGVLLPNFGF
VLSPSGAAAL MAFSSVSVVT NSILLRRIAH RL
//
