ID   Q5WCZ5_SHOC1            Unreviewed;       809 AA.
AC   Q5WCZ5;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE            EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE   AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE   AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN   OrderedLocusNames=ABC3231 {ECO:0000313|EMBL:BAD65765.1};
OS   Shouchella clausii (strain KSM-K16) (Alkalihalobacillus clausii).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=66692 {ECO:0000313|EMBL:BAD65765.1, ECO:0000313|Proteomes:UP000001168};
RN   [1] {ECO:0000313|EMBL:BAD65765.1, ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD65765.1,
RC   ECO:0000313|Proteomes:UP000001168};
RA   Hakamada Y., Kobayashi T., Hitomi J., Kawai S., Ito S.;
RT   "Molecular cloning and nucleotide sequence of the gene for an alkaline
RT   protease from the alkalophilic Bacillus sp. KSM-K16.";
RL   J. Ferment. Bioeng. 78:105-108(1994).
RN   [2] {ECO:0000313|EMBL:BAD65765.1, ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD65765.1,
RC   ECO:0000313|Proteomes:UP000001168};
RX   PubMed=7632397; DOI=10.1007/s002530050437;
RA   Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K.,
RA   Kawai S., Ito S.;
RT   "Purification and properties of an alkaline protease from alkalophilic
RT   Bacillus sp. KSM-K16.";
RL   Appl. Microbiol. Biotechnol. 43:473-481(1995).
RN   [3] {ECO:0000313|EMBL:BAD65765.1, ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD65765.1,
RC   ECO:0000313|Proteomes:UP000001168};
RX   PubMed=9278275; DOI=10.1093/protein/10.6.627;
RA   Shirai T., Suzuki A., Yamane T., Ashida T., Kobayashi T., Ito S.;
RT   "High-resolution crystal structure of M-protease: phylogeny aided analysis
RT   of the high-alkaline adaptation mechanism.";
RL   Protein Eng. 10:627-634(1997).
RN   [4] {ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|Proteomes:UP000001168};
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:BAD65765.1, ECO:0000313|Proteomes:UP000001168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16 {ECO:0000313|EMBL:BAD65765.1,
RC   ECO:0000313|Proteomes:UP000001168};
RX   PubMed=17429572; DOI=10.1007/s00792-007-0074-1;
RA   Kageyama Y., Takaki Y., Shimamura S., Nishi S., Nogi Y., Uchimura K.,
RA   Kobayashi T., Hitomi J., Ozaki K., Kawai S., Ito S., Horikoshi K.;
RT   "Intragenomic diversity of the V1 regions of 16S rRNA genes in high-
RT   alkaline protease-producing Bacillus clausii spp.";
RL   Extremophiles 11:597-603(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:456216; EC=7.2.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001390};
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}.
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DR   EMBL; AP006627; BAD65765.1; -; Genomic_DNA.
DR   RefSeq; WP_011248073.1; NC_006582.1.
DR   AlphaFoldDB; Q5WCZ5; -.
DR   STRING; 66692.ABC3231; -.
DR   KEGG; bcl:ABC3231; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_0_3_9; -.
DR   OrthoDB; 9813266at2; -.
DR   Proteomes; UP000001168; 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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; 2.
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   PRINTS; PR00943; CUATPASE.
DR   PRINTS; PR00942; CUATPASEI.
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; PS01229; COF_2; 1.
DR   PROSITE; PS01047; HMA_1; 2.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Hydrolase {ECO:0000313|EMBL:BAD65765.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001168};
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:ARBA00022448}.
FT   TRANSMEM        156..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        193..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        223..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        257..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        410..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        438..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        753..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        776..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          4..70
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          72..138
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   COILED          584..611
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   809 AA;  86804 MW;  2C3EFD12E3B3FB5F CRC64;
     MSEKKAAISI TGMTCAACAT RIEKGLNKIE GVSQATVNLA NEKATITYDS NKTEPSAFTE
     KIDKLGYGVR LEKAVFNVKG MTCAACATRI EKRLQKMPGV KEANVNLAIE RATVVYNEAE
     TNEQEMIRVV DKLGYQLERE AASSGNTKEE ESQKRFGLFL FSAILSLPLL WTMVTHFEFT
     SFLYVPDMFM NPWVQLALAT PVQLIVGAPF YKGAYKALAN KSANMDVLVA LGTSVAYVYS
     IFLGWEWYQN GQVGMPELYF EAAAVILTLI VLGKWFEARA KGRTSKAIST LLGLQAKTAR
     VIRNGNEVEL PIEEVKAGYE LIIRPGEKIP VDGYVKSGTS SVDESMITGE ALPVSKKADD
     SLIGATLNKQ GSLRMIATKV GKDTALAQIV KVVEEAQGSK ADIQRIADRV SGVFVPVVVL
     LAAATFLIWY TLIDPGNIRA AIVPFITILV IACPCALGLA TPTSIMAGSG RAAELGLLFR
     GGEHLENTRS ITTVVLDKTG TVTKGTPQLT DIVPAEGIDE NELLAIVASA EFESEHPLAN
     AIVQGAADRA ISLREAEAFE ALTGYGIRAK VDGVVIHIGT RKLMEQATIE YAILEERMEE
     LEQQGKTAML VSIGTDIAGL VAVADTVKET SKEAVERLHE LGLEVIMLTG DNERTAKAIA
     AEVGINHVIA GVLPEEKSNE VKRLQEDGKR VAMVGDGIND APALAVADVG MAMGTGADVA
     IETADVTLMR GDVNSVADAF LMSKKTMRNI KQNLFFAFFY NSAAIPIAAA GLLAPWVAGA
     AMAFSSVSVV ANALRLQRIR MPQRGAASQ
//