COPA_BACSU
ID COPA_BACSU Reviewed; 802 AA.
AC O32220;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Copper-exporting P-type ATPase;
DE Short=Protein CopA;
DE EC=7.2.2.8;
DE AltName: Full=Copper-exporting P-type ATPase A;
DE AltName: Full=Cu(+)-exporting ATPase;
GN Name=copA; Synonyms=yvgX; OrderedLocusNames=BSU33500;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION IN COPPER EXPORT, INDUCTION BY COPPER, AND INTERACTION WITH COPZ.
RC STRAIN=168;
RX PubMed=12644235; DOI=10.1016/s0378-1097(03)00095-8;
RA Radford D.S., Kihlken M.A., Borrelly G.P.M., Harwood C.R., Le Brun N.E.,
RA Cavet J.S.;
RT "CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-
RT type ATPase CopA.";
RL FEMS Microbiol. Lett. 220:105-112(2003).
RN [3]
RP REGULATION.
RX PubMed=14663075; DOI=10.1099/mic.0.26225-0;
RA Gaballa A., Cao M., Helmann J.D.;
RT "Two MerR homologues that affect copper induction of the Bacillus subtilis
RT copZA operon.";
RL Microbiology 149:3413-3421(2003).
RN [4]
RP STRUCTURE BY NMR OF 1-150 IN COMPLEX WITH COPPER IONS.
RX PubMed=11922674; DOI=10.1006/jmbi.2002.5430;
RA Banci L., Bertini I., Ciofi-Baffoni S., D'Onofrio M., Gonnelli L.,
RA Marhuenda-Egea F.C., Ruiz-Duenas F.J.;
RT "Solution structure of the N-terminal domain of a potential copper-
RT translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I)
RT loaded states.";
RL J. Mol. Biol. 317:415-429(2002).
RN [5]
RP STRUCTURE BY NMR OF 1-150.
RX PubMed=14514665; DOI=10.1074/jbc.m307389200;
RA Banci L., Bertini I., Ciofi-Baffoni S., Gonnelli L., Su X.-C.;
RT "Structural basis for the function of the N-terminal domain of the ATPase
RT CopA from Bacillus subtilis.";
RL J. Biol. Chem. 278:50506-50513(2003).
RN [6]
RP STRUCTURE BY NMR OF 1-150.
RX PubMed=12590580; DOI=10.1021/bi027096p;
RA Banci L., Bertini I., Ciofi-Baffoni S., Del Conte R., Gonnelli L.;
RT "Understanding copper trafficking in bacteria: interaction between the
RT copper transport protein CopZ and the N-terminal domain of the copper
RT ATPase CopA from Bacillus subtilis.";
RL Biochemistry 42:1939-1949(2003).
RN [7]
RP STRUCTURE BY NMR OF 1-146 IN COMPLEX WITH COPPER IONS, AND SUBUNIT.
RC STRAIN=168 / BGSC1A1;
RX PubMed=18215122; DOI=10.1042/bj20071620;
RA Singleton C., Banci L., Ciofi-Baffoni S., Tenori L., Kihlken M.A.,
RA Boetzel R., Le Brun N.E.;
RT "Structure and Cu(I)-binding properties of the N-terminal soluble domains
RT of Bacillus subtilis CopA.";
RL Biochem. J. 411:571-579(2008).
CC -!- FUNCTION: Involved in copper export. {ECO:0000269|PubMed:12644235}.
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 -!- SUBUNIT: Monomer at sub-stoichiometric copper concentrations. Homodimer
CC at higher copper concentrations. Forms a heterodimer (electrostatic
CC interactions) with CopZ during the transfer of Cu(+).
CC {ECO:0000269|PubMed:11922674, ECO:0000269|PubMed:18215122}.
CC -!- INTERACTION:
CC O32220; O32220: copA; NbExp=2; IntAct=EBI-905041, EBI-905041;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By Cu(2+). {ECO:0000269|PubMed:12644235}.
CC -!- MISCELLANEOUS: The copZA operon is activated by CueR and indirectly
CC repressed by YfmP.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB15355.2; -; Genomic_DNA.
DR PIR; E70041; E70041.
DR RefSeq; NP_391230.2; NC_000964.3.
DR RefSeq; WP_003242925.1; NZ_JNCM01000033.1.
DR PDB; 1JWW; NMR; -; A=71-146.
DR PDB; 1KQK; NMR; -; A=72-146.
DR PDB; 1OPZ; NMR; -; A=2-71.
DR PDB; 1OQ3; NMR; -; A=2-71.
DR PDB; 1OQ6; NMR; -; A=2-71.
DR PDB; 1P6T; NMR; -; A=2-146.
DR PDB; 2RML; NMR; -; A=2-146.
DR PDB; 2VOY; EM; 18.00 A; A=71-146.
DR PDBsum; 1JWW; -.
DR PDBsum; 1KQK; -.
DR PDBsum; 1OPZ; -.
DR PDBsum; 1OQ3; -.
DR PDBsum; 1OQ6; -.
DR PDBsum; 1P6T; -.
DR PDBsum; 2RML; -.
DR PDBsum; 2VOY; -.
DR AlphaFoldDB; O32220; -.
DR BMRB; O32220; -.
DR SMR; O32220; -.
DR IntAct; O32220; 2.
DR MINT; O32220; -.
DR STRING; 224308.BSU33500; -.
DR TCDB; 3.A.3.5.18; the p-type atpase (p-atpase) superfamily.
DR PaxDb; O32220; -.
DR PRIDE; O32220; -.
DR EnsemblBacteria; CAB15355; CAB15355; BSU_33500.
DR GeneID; 937985; -.
DR KEGG; bsu:BSU33500; -.
DR PATRIC; fig|224308.179.peg.3635; -.
DR eggNOG; COG2217; Bacteria.
DR InParanoid; O32220; -.
DR OMA; HWMLPAW; -.
DR PhylomeDB; O32220; -.
DR BioCyc; BSUB:BSU33500-MON; -.
DR BRENDA; 7.2.2.8; 658.
DR EvolutionaryTrace; O32220; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR CDD; cd00371; HMA; 2.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00403; HMA; 2.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 2.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR TIGRFAMs; TIGR00003; TIGR00003; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Copper; Copper transport;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..802
FT /note="Copper-exporting P-type ATPase"
FT /id="PRO_0000046330"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..796
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..71
FT /note="HMA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT DOMAIN 73..139
FT /note="HMA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 499
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 19
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 84
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 87
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 698
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 702
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:1OPZ"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1OPZ"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1OPZ"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1OPZ"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1OPZ"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1OPZ"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:1OPZ"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1OPZ"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:1JWW"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:1JWW"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1JWW"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:1JWW"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:1JWW"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:1JWW"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1JWW"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1JWW"
SQ SEQUENCE 802 AA; 85912 MW; 8D6EC2B203E11E38 CRC64;
MSEQKEIAMQ VSGMTCAACA ARIEKGLKRM PGVTDANVNL ATETSNVIYD PAETGTAAIQ
EKIEKLGYHV VTEKAEFDIE GMTCAACANR IEKRLNKIEG VANAPVNFAL ETVTVEYNPK
EASVSDLKEA VDKLGYKLKL KGEQDSEAAA KKKEERKQTA RLIFSAVLSF PLLWAMVSHF
TFTSFIWVPD IFLNPWMQFA LATPVQFLIG WPFYVGAYKA LRNKSANMDV LVALGTTAAY
AYSLYLTFQS IGSHGHTDGL YYETSAILLT LILLGKLFET KAKGRSSDAI KKLMKLQAKT
ATVVRDGQEQ IIPIDEVLVN DIVYVKPGER IPVDGEVVEG RSAVDESMIT GESLPVDKNP
GDSVTGSTVN ANGFLKIKAV NVGKDTALSH IIKIVEEAQG SKAPIQRLAD QISGIFVPIV
LGIAVLTFLI WYLWAAPGDF AEAISKFIAV LVIACPCALG LATPTSIMAG SGRAAEFGIL
FKGGEHLEKT HRLDTIVLDK TGTVTNGKPR LTDAIPFGRF EEKDLLQFAA AAETGSEHPL
GEAIIAGVKD KGLEIPKLTR FEAKVGAGIL AEAGGKSILV GTRKLMESEQ VEHGALLAQM
EELEAEGKTV MLVSIDGEAA GLVAVADTIK DTSRKAVARL KELGLDVIMM TGDNRRTAEA
IAKEAGIANI IAEVLPEQKA AEIARLQKEG RQTAMVGDGI NDAPALATAD IGMAIGTGTD
IAMETADITL IRGDLNSIAD AIRMSRLTMK NIKQNLFWAL GYNSLGIPIA ALGFLAPWIA
GAAMAFSSVS VVLNALRLQK VK
