UniProtKB - O32219 (CADA_BACSU)
(max 400 entries)x
Your basket is currently empty. i
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
Protein
Cadmium, zinc and cobalt-transporting ATPase
Gene
cadA
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. Does not seem to transport copper.1 Publication
Catalytic activityi
ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out).2 Publications
ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out).2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 15 | Cadmium or zinc or cobaltPROSITE-ProRule annotation | 1 | |
Metal bindingi | 18 | Cadmium or zinc or cobaltPROSITE-ProRule annotation | 1 | |
Active sitei | 401 | 4-aspartylphosphate intermediateBy similarity | 1 | |
Metal bindingi | 595 | MagnesiumPROSITE-ProRule annotation | 1 | |
Metal bindingi | 599 | MagnesiumPROSITE-ProRule annotation | 1 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cadmium-exporting ATPase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
- zinc-exporting ATPase activity Source: UniProtKB-EC
GO - Biological processi
- cobalt ion transport Source: UniProtKB-KW
- copper ion transport Source: UniProtKB-KW
- response to cadmium ion Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase |
Biological process | Cadmium resistance, Cobalt transport, Copper transport, Ion transport, Stress response, Transport, Zinc transport |
Ligand | ATP-binding, Cadmium, Cobalt, Copper, Magnesium, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BioCyci | BSUB:BSU33490-MONOMER. |
Protein family/group databases
TCDBi | 3.A.3.6.10. the p-type atpase (p-atpase) superfamily. |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:cadA Synonyms:yvgW Ordered Locus Names:BSU33490 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 86 | CytoplasmicBy similarityAdd BLAST | 86 | |
Transmembranei | 87 – 107 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 108 – 116 | ExtracellularBy similarity | 9 | |
Transmembranei | 117 – 136 | HelicalBy similarityAdd BLAST | 20 | |
Topological domaini | 137 – 143 | CytoplasmicBy similarity | 7 | |
Transmembranei | 144 – 163 | HelicalBy similarityAdd BLAST | 20 | |
Topological domaini | 164 – 166 | ExtracellularBy similarity | 3 | |
Transmembranei | 167 – 186 | HelicalBy similarityAdd BLAST | 20 | |
Topological domaini | 187 – 320 | CytoplasmicBy similarityAdd BLAST | 134 | |
Transmembranei | 321 – 339 | HelicalBy similarityAdd BLAST | 19 | |
Topological domaini | 340 – 345 | ExtracellularBy similarity | 6 | |
Transmembranei | 346 – 363 | HelicalBy similarityAdd BLAST | 18 | |
Topological domaini | 364 – 648 | CytoplasmicBy similarityAdd BLAST | 285 | |
Transmembranei | 649 – 670 | HelicalBy similarityAdd BLAST | 22 | |
Topological domaini | 671 – 678 | ExtracellularBy similarity | 8 | |
Transmembranei | 679 – 694 | HelicalBy similarityAdd BLAST | 16 | |
Topological domaini | 695 – 702 | CytoplasmicBy similarity | 8 |
GO - Cellular componenti
- integral component of membrane Source: UniProtKB-KW
- plasma membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Disruption phenotypei
Arrested in competence development and sporulation.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000360852 | 1 – 702 | Cadmium, zinc and cobalt-transporting ATPaseAdd BLAST | 702 |
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | O32219. |
Expressioni
Developmental stagei
Expression increases rapidly at 5 hours and peaks at 7 hours after onset of sporulation.1 Publication
Inductioni
By heat-shock, ethanol stress, zinc, cobalt and cadmium.1 Publication
Structurei
3D structure databases
ProteinModelPortali | O32219. |
SMRi | O32219. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 5 – 73 | HMAPROSITE-ProRule annotationAdd BLAST | 69 |
Sequence similaritiesi
Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | ENOG4105C59. Bacteria. COG2217. LUCA. |
HOGENOMi | HOG000250399. |
InParanoidi | O32219. |
OMAi | AVVAKCC. |
Family and domain databases
CDDi | cd00371. HMA. 1 hit. |
Gene3Di | 3.40.1110.10. 1 hit. 3.40.50.1000. 2 hits. |
InterProi | View protein in InterPro IPR023299. ATPase_P-typ_cyto_dom_N. IPR018303. ATPase_P-typ_P_site. IPR023298. ATPase_P-typ_TM_dom_sf. IPR008250. ATPase_P-typ_transduc_dom_A_sf. IPR036412. HAD-like_sf. IPR023214. HAD_sf. IPR017969. Heavy-metal-associated_CS. IPR006121. HMA_dom. IPR036163. HMA_dom_sf. IPR027256. P-typ_ATPase_IB. IPR001757. P_typ_ATPase. |
Pfami | View protein in Pfam PF00403. HMA. 1 hit. |
PRINTSi | PR00941. CDATPASE. |
SUPFAMi | SSF55008. SSF55008. 1 hit. SSF56784. SSF56784. 2 hits. SSF81653. SSF81653. 1 hit. SSF81665. SSF81665. 3 hits. |
TIGRFAMsi | TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 1 hit. |
PROSITEi | View protein in PROSITE PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. 1 hit. PS50846. HMA_2. 1 hit. |
i Sequence
Sequence statusi: Complete.
O32219-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MRLVKQEYVL DGLDCSNCAR KIENGVKGIK GINGCAVNFA ASTLTVSADG
60 70 80 90 100
KEEQWVTNKV EKKVKSIDPH VTVRQKHIKK SADDGYRNRM VNMLIRMAAA
110 120 130 140 150
VILGAAAYLV QSGTIEFFLF LGAYLIIGGD IIIRAVKNII RGQVFDEHFL
160 170 180 190 200
MALATIGAFL IQQYPEGVAV MLFYQIGELF QGAAVSRSRK SISALMDIRP
210 220 230 240 250
DYANLKTKNG IEQVSSEDVQ TGDIIVVNPG ESIPLDGKVV QGSAMVDTSA
260 270 280 290 300
LTGESVPRKA AEGQDVMSGF INQNGVLHIE VTKGYQESAV SKILDLVQNA
310 320 330 340 350
SSRKARTENF ITKFAKYYTP AVVIIAVLLA FVPPLVLSGA ALSDWVYRAL
360 370 380 390 400
IFLVISCPCA LVVSIPLGFF GGIGAASKAG VLVKGSNYLE ALNQVKYAVF
410 420 430 440 450
DKTGTLTKGS FEVTEIKPAE GFTKDRLLEA AAYAELHSQH PIAESVRKAY
460 470 480 490 500
GKMLSSDEIE SYEEISGHGI FAKVNGTEIL AGNKKLMERE QIEDVPDENA
510 520 530 540 550
GTIVHVAVDQ RYAGAIIIAD EIKEDAAQAV ADLKSLGIKQ TAMLTGDSKQ
560 570 580 590 600
TGEAVGKQLG IGEVYAELLP QDKVAQVEAL EAKLLPSEKL IFVGDGINDT
610 620 630 640 650
PVLARADIGV AMGGLGSDAA VEAADIVLMT DQPSKIAEAI RIAKRTRRIV
660 670 680 690 700
WQNIGFALGV KAIFLILGAF GIATMWEAVF SDVGVTLLAV ANAMRVMRLK
NK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA. Translation: CAB15354.3. |
PIRi | D70041. |
Genome annotation databases
EnsemblBacteriai | CAB15354; CAB15354; BSU33490. |
Similar proteinsi
Entry informationi
Entry namei | CADA_BACSU | |
Accessioni | O32219Primary (citable) accession number: O32219 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 20, 2009 |
Last sequence update: | January 1, 1998 | |
Last modified: | February 28, 2018 | |
This is version 136 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |