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Database: UniProt
Entry: G5J2Z9_CROWT
LinkDB: G5J2Z9_CROWT
Original site: G5J2Z9_CROWT 
ID   G5J2Z9_CROWT            Unreviewed;       766 AA.
AC   G5J2Z9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Lead, cadmium, zinc and mercury transporting ATPase Copper-translocating P-type ATPase {ECO:0000313|EMBL:EHJ13436.1};
DE            EC=3.6.3.3 {ECO:0000313|EMBL:EHJ13436.1};
DE            EC=3.6.3.4 {ECO:0000313|EMBL:EHJ13436.1};
DE            EC=3.6.3.5 {ECO:0000313|EMBL:EHJ13436.1};
GN   ORFNames=CWATWH0003_1880 {ECO:0000313|EMBL:EHJ13436.1};
OS   Crocosphaera watsonii WH 0003.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=423471 {ECO:0000313|EMBL:EHJ13436.1, ECO:0000313|Proteomes:UP000003477};
RN   [1] {ECO:0000313|EMBL:EHJ13436.1, ECO:0000313|Proteomes:UP000003477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 0003 {ECO:0000313|EMBL:EHJ13436.1,
RC   ECO:0000313|Proteomes:UP000003477};
RX   PubMed=22232617;
RA   Bench S.R., Ilikchyan I.N., Tripp H.J., Zehr J.P.;
RT   "Two Strains of Crocosphaera watsonii with Highly Conserved Genomes are
RT   Distinguished by Strain-Specific Features.";
RL   Front. Microbiol. 2:261-261(2011).
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:EHJ13436.1}.
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DR   EMBL; AESD01000292; EHJ13436.1; -; Genomic_DNA.
DR   RefSeq; WP_007310219.1; NZ_AESD01000292.1.
DR   AlphaFoldDB; G5J2Z9; -.
DR   PATRIC; fig|423471.3.peg.1760; -.
DR   Proteomes; UP000003477; 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; TIGR01511; ATPase-IB1_Cu; 1.
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   PRINTS; PR00943; CUATPASE.
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; 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:EHJ13436.1};
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        112..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        145..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        178..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        212..230
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..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        712..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        740..759
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          17..83
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   766 AA;  82289 MW;  4509B870C35EC694 CRC64;
     MKNSLHPQSS PKNSSLTQEN LHLEGMGCAA CAIKVETVLN KVAGVKKCNV NFALERATVE
     YDSQVTNLGN IQAVISKAGY KSHVLEEQKN NQTEDSEQEK RKAKQQELTQ KVIVGGVISL
     ILMFGGLPMM TGLSLPFIPH WLHNAWLQLF LSIPVVFWCG KGFYMGAFKA FKGGTSDLNS
     LVTLGTGAAF LYSLFATFFP QFFIFQGLKA DVYYEAAVVI ITLILLGRLL ETRARSKTSE
     AIGNLMGLQA KTARVIRQGE GVDIAVEDVI IGDIVLVRPG EKIPVDGVII EGQSTLDESM
     ITGESIPVEK QTGDEVIGAT INKTGSFKFE ARKVGKDTTL SQIIKLVEEA QNSKAPIQKI
     ADQVTAWFVP AVMIIAVISF ICWLIFAQNL SLAMVTTVSV LIIACPCALG LATPTSIMVG
     TGKGAENGIL IKGADSLELA HKIKAIVLDK TGTLTQGKPI VTNYITVDGI ADNNELNILG
     IAAAIEENSE HPLAEAIVNY AKSQGIVNNY PKVENFEAMG GQGVQGKIEG KLVQIGTQKW
     LEKLGVNTKQ LVSQAREWEN QAKTTPWIAI DGEIKGLFAI ADAVKPSSIE AVKKLKKMGL
     EVIMLTGDNQ QTAQAIADEV GIYHVFAEVR PDEKANKIKE IQQSQGKIVA MVGDGINDAP
     ALAQADVGMA IGTGTDVAMS ASDITLISGD LQGIVTAIEL SRATMKNIRQ NLFFAFIYNT
     LGIPIAAGIL YPFFGMLLNP MIAGAAMAFS SVSVVSNALR LRNFSP
//
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