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Protein

Cadmium, zinc and cobalt-transporting ATPase

Gene

cadA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi15 – 151Cadmium or zinc or cobaltPROSITE-ProRule annotation
Metal bindingi18 – 181Cadmium or zinc or cobaltPROSITE-ProRule annotation
Active sitei401 – 40114-aspartylphosphate intermediateBy similarity
Metal bindingi595 – 5951MagnesiumPROSITE-ProRule annotation
Metal bindingi599 – 5991MagnesiumPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cadmium resistance, Cobalt transport, Copper transport, Ion transport, Stress response, Transport, Zinc transport

Keywords - Ligandi

ATP-binding, Cadmium, Cobalt, Copper, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU33490-MONOMER.

Protein family/group databases

TCDBi3.A.3.6.10. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadmium, zinc and cobalt-transporting ATPase (EC:3.6.3.32 Publications, EC:3.6.3.52 Publications)
Gene namesi
Name:cadA
Synonyms:yvgW
Ordered Locus Names:BSU33490
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8686CytoplasmicBy similarityAdd
BLAST
Transmembranei87 – 10721HelicalBy similarityAdd
BLAST
Topological domaini108 – 1169ExtracellularBy similarity
Transmembranei117 – 13620HelicalBy similarityAdd
BLAST
Topological domaini137 – 1437CytoplasmicBy similarity
Transmembranei144 – 16320HelicalBy similarityAdd
BLAST
Topological domaini164 – 1663ExtracellularBy similarity
Transmembranei167 – 18620HelicalBy similarityAdd
BLAST
Topological domaini187 – 320134CytoplasmicBy similarityAdd
BLAST
Transmembranei321 – 33919HelicalBy similarityAdd
BLAST
Topological domaini340 – 3456ExtracellularBy similarity
Transmembranei346 – 36318HelicalBy similarityAdd
BLAST
Topological domaini364 – 648285CytoplasmicBy similarityAdd
BLAST
Transmembranei649 – 67022HelicalBy similarityAdd
BLAST
Topological domaini671 – 6788ExtracellularBy similarity
Transmembranei679 – 69416HelicalBy similarityAdd
BLAST
Topological domaini695 – 7028CytoplasmicBy similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Arrested in competence development and sporulation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 702702Cadmium, zinc and cobalt-transporting ATPasePRO_0000360852Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO32219.

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

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018181.

Structurei

3D structure databases

ProteinModelPortaliO32219.
SMRiO32219. Positions 4-74, 190-302, 377-650.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 7369HMAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HMA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250399.
InParanoidiO32219.
OMAiFAMGGMH.
OrthoDBiEOG6742RM.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
[Graphical view]
PRINTSiPR00941. CDATPASE.
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O32219-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:702
Mass (Da):75,405
Last modified:January 1, 1998 - v1
Checksum:iC149EDADA4C4297D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15354.3.
PIRiD70041.

Genome annotation databases

EnsemblBacteriaiCAB15354; CAB15354; BSU33490.
PATRICi18978700. VBIBacSub10457_3513.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15354.3.
PIRiD70041.

3D structure databases

ProteinModelPortaliO32219.
SMRiO32219. Positions 4-74, 190-302, 377-650.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018181.

Protein family/group databases

TCDBi3.A.3.6.10. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbiO32219.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15354; CAB15354; BSU33490.
PATRICi18978700. VBIBacSub10457_3513.

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250399.
InParanoidiO32219.
OMAiFAMGGMH.
OrthoDBiEOG6742RM.

Enzyme and pathway databases

BioCyciBSUB:BSU33490-MONOMER.

Family and domain databases

Gene3Di2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HMA_dom.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
[Graphical view]
PRINTSiPR00941. CDATPASE.
SUPFAMiSSF55008. SSF55008. 1 hit.
SSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Tn10 insertional mutations of Bacillus subtilis that block the biosynthesis of bacilysin."
    Yazgan A., Oezcengiz G., Marahiel M.A.
    Biochim. Biophys. Acta 1518:87-94(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
    Strain: 168 / PY79.
  3. "Investigation of the yvgW Bacillus subtilis chromosomal gene involved in Cd(2+) ion resistance."
    Solovieva I.M., Entian K.D.
    FEMS Microbiol. Lett. 208:105-109(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
    Strain: 168.
  4. "Bacillus subtilis CPx-type ATPases: characterization of Cd, Zn, Co and Cu efflux systems."
    Gaballa A., Helmann J.D.
    BioMetals 16:497-505(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, INDUCTION.
    Strain: 168 / CU1065.
  5. "Sporulation-specific expression of the yvgW (cadA) gene and the effect of blockage on spore properties in Bacillus subtilis."
    Irigul O., Yazgan-Karatas A.
    Gene 382:71-78(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
    Strain: 168 / PY79.

Entry informationi

Entry nameiCADA_BACSU
AccessioniPrimary (citable) accession number: O32219
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.