CADA_BACSU
ID CADA_BACSU Reviewed; 702 AA.
AC O32219;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cadmium, zinc and cobalt-transporting ATPase;
DE EC=7.2.2.12 {ECO:0000269|PubMed:11934502, ECO:0000269|PubMed:12779235};
DE EC=7.2.2.21 {ECO:0000269|PubMed:11934502, ECO:0000269|PubMed:12779235};
GN Name=cadA; Synonyms=yvgW; OrderedLocusNames=BSU33490;
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 DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=11267663; DOI=10.1016/s0167-4781(01)00182-8;
RA Yazgan A., Oezcengiz G., Marahiel M.A.;
RT "Tn10 insertional mutations of Bacillus subtilis that block the
RT biosynthesis of bacilysin.";
RL Biochim. Biophys. Acta 1518:87-94(2001).
RN [3]
RP CATALYTIC ACTIVITY.
RC STRAIN=168;
RX PubMed=11934502; DOI=10.1111/j.1574-6968.2002.tb11068.x;
RA Solovieva I.M., Entian K.D.;
RT "Investigation of the yvgW Bacillus subtilis chromosomal gene involved in
RT Cd(2+) ion resistance.";
RL FEMS Microbiol. Lett. 208:105-109(2002).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, AND INDUCTION.
RC STRAIN=168 / CU1065;
RX PubMed=12779235; DOI=10.1023/a:1023425321617;
RA Gaballa A., Helmann J.D.;
RT "Bacillus subtilis CPx-type ATPases: characterization of Cd, Zn, Co and Cu
RT efflux systems.";
RL BioMetals 16:497-505(2003).
RN [5]
RP DEVELOPMENTAL STAGE.
RC STRAIN=168 / PY79;
RX PubMed=16901659; DOI=10.1016/j.gene.2006.06.014;
RA Irigul O., Yazgan-Karatas A.;
RT "Sporulation-specific expression of the yvgW (cadA) gene and the effect of
RT blockage on spore properties in Bacillus subtilis.";
RL Gene 382:71-78(2006).
CC -!- FUNCTION: Couples the hydrolysis of ATP with the transport of cadmium,
CC zinc and cobalt out of the cell. Does not seem to transport copper.
CC {ECO:0000269|PubMed:12779235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out);
CC Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.12;
CC Evidence={ECO:0000269|PubMed:11934502, ECO:0000269|PubMed:12779235};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.21;
CC Evidence={ECO:0000269|PubMed:11934502, ECO:0000269|PubMed:12779235};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Expression increases rapidly at 5 hours and peaks
CC at 7 hours after onset of sporulation. {ECO:0000269|PubMed:16901659}.
CC -!- INDUCTION: By heat-shock, ethanol stress, zinc, cobalt and cadmium.
CC {ECO:0000269|PubMed:12779235}.
CC -!- DISRUPTION PHENOTYPE: Arrested in competence development and
CC sporulation. {ECO:0000269|PubMed:11267663}.
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; CAB15354.3; -; Genomic_DNA.
DR PIR; D70041; D70041.
DR RefSeq; NP_391229.2; NC_000964.3.
DR AlphaFoldDB; O32219; -.
DR SMR; O32219; -.
DR STRING; 224308.BSU33490; -.
DR TCDB; 3.A.3.6.10; the p-type atpase (p-atpase) superfamily.
DR jPOST; O32219; -.
DR PaxDb; O32219; -.
DR PRIDE; O32219; -.
DR EnsemblBacteria; CAB15354; CAB15354; BSU_33490.
DR GeneID; 936034; -.
DR KEGG; bsu:BSU33490; -.
DR eggNOG; COG2217; Bacteria.
DR InParanoid; O32219; -.
DR OMA; FAQPWET; -.
DR BioCyc; BSUB:BSU33490-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0015086; F:cadmium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008551; F:P-type cadmium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0016463; F:P-type zinc transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
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; 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; 1.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF55008; SSF55008; 1.
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 PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cadmium; Cadmium resistance; Cell membrane; Cobalt;
KW Cobalt transport; Copper; Copper transport; Ion transport; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response; Translocase; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..702
FT /note="Cadmium, zinc and cobalt-transporting ATPase"
FT /id="PRO_0000360852"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 108..116
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 137..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 164..166
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 187..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 321..339
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 340..345
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 346..363
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 364..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 649..670
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 671..678
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 679..694
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 695..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 4..72
FT /note="HMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT ACT_SITE 401
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 15
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 18
FT /ligand="Cd(2+)"
FT /ligand_id="ChEBI:CHEBI:48775"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 18
FT /ligand="Co(2+)"
FT /ligand_id="ChEBI:CHEBI:48828"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00280"
FT BINDING 595
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
SQ SEQUENCE 702 AA; 75405 MW; C149EDADA4C4297D CRC64;
MRLVKQEYVL DGLDCSNCAR KIENGVKGIK GINGCAVNFA ASTLTVSADG KEEQWVTNKV
EKKVKSIDPH VTVRQKHIKK SADDGYRNRM VNMLIRMAAA VILGAAAYLV QSGTIEFFLF
LGAYLIIGGD IIIRAVKNII RGQVFDEHFL MALATIGAFL IQQYPEGVAV MLFYQIGELF
QGAAVSRSRK SISALMDIRP DYANLKTKNG IEQVSSEDVQ TGDIIVVNPG ESIPLDGKVV
QGSAMVDTSA LTGESVPRKA AEGQDVMSGF INQNGVLHIE VTKGYQESAV SKILDLVQNA
SSRKARTENF ITKFAKYYTP AVVIIAVLLA FVPPLVLSGA ALSDWVYRAL IFLVISCPCA
LVVSIPLGFF GGIGAASKAG VLVKGSNYLE ALNQVKYAVF DKTGTLTKGS FEVTEIKPAE
GFTKDRLLEA AAYAELHSQH PIAESVRKAY GKMLSSDEIE SYEEISGHGI FAKVNGTEIL
AGNKKLMERE QIEDVPDENA GTIVHVAVDQ RYAGAIIIAD EIKEDAAQAV ADLKSLGIKQ
TAMLTGDSKQ TGEAVGKQLG IGEVYAELLP QDKVAQVEAL EAKLLPSEKL IFVGDGINDT
PVLARADIGV AMGGLGSDAA VEAADIVLMT DQPSKIAEAI RIAKRTRRIV WQNIGFALGV
KAIFLILGAF GIATMWEAVF SDVGVTLLAV ANAMRVMRLK NK
