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O32219 (CADA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cadmium, zinc and cobalt-transporting ATPase
EC=3.6.3.3
EC=3.6.3.5
Gene names
Name:cadA
Synonyms:yvgW
Ordered Locus Names:BSU33490
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length702 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. Does not seem to transport copper. Ref.4

Catalytic activity

ATP + H2O + Cd2+(In) = ADP + phosphate + Cd2+(Out). Ref.3 Ref.4

ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out). Ref.3 Ref.4

Subcellular location

Cell membrane; Multi-pass membrane protein.

Developmental stage

Expression increases rapidly at 5 hours and peaks at 7 hours after onset of sporulation. Ref.5

Induction

By heat-shock, ethanol stress, zinc, cobalt and cadmium. Ref.4

Disruption phenotype

Arrested in competence development and sporulation. Ref.2

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 1 HMA domain.

Sequence caution

The sequence CAB15354.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 702702Cadmium, zinc and cobalt-transporting ATPase
PRO_0000360852

Regions

Topological domain1 – 8686Cytoplasmic By similarity
Transmembrane87 – 10721Helical; By similarity
Topological domain108 – 1169Extracellular By similarity
Transmembrane117 – 13620Helical; By similarity
Topological domain137 – 1437Cytoplasmic By similarity
Transmembrane144 – 16320Helical; By similarity
Topological domain164 – 1663Extracellular By similarity
Transmembrane167 – 18620Helical; By similarity
Topological domain187 – 320134Cytoplasmic By similarity
Transmembrane321 – 33919Helical; By similarity
Topological domain340 – 3456Extracellular By similarity
Transmembrane346 – 36318Helical; By similarity
Topological domain364 – 648285Cytoplasmic By similarity
Transmembrane649 – 67022Helical; By similarity
Topological domain671 – 6788Extracellular By similarity
Transmembrane679 – 69416Helical; By similarity
Topological domain695 – 7028Cytoplasmic By similarity
Domain5 – 7369HMA

Sites

Active site40114-aspartylphosphate intermediate By similarity
Metal binding151Cadmium or zinc or cobalt Potential
Metal binding181Cadmium or zinc or cobalt Potential
Metal binding5951Magnesium By similarity
Metal binding5991Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
O32219 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C149EDADA4C4297D

FASTA70275,405
        10         20         30         40         50         60 
MRLVKQEYVL DGLDCSNCAR KIENGVKGIK GINGCAVNFA ASTLTVSADG KEEQWVTNKV 

        70         80         90        100        110        120 
EKKVKSIDPH VTVRQKHIKK SADDGYRNRM VNMLIRMAAA VILGAAAYLV QSGTIEFFLF 

       130        140        150        160        170        180 
LGAYLIIGGD IIIRAVKNII RGQVFDEHFL MALATIGAFL IQQYPEGVAV MLFYQIGELF 

       190        200        210        220        230        240 
QGAAVSRSRK SISALMDIRP DYANLKTKNG IEQVSSEDVQ TGDIIVVNPG ESIPLDGKVV 

       250        260        270        280        290        300 
QGSAMVDTSA LTGESVPRKA AEGQDVMSGF INQNGVLHIE VTKGYQESAV SKILDLVQNA 

       310        320        330        340        350        360 
SSRKARTENF ITKFAKYYTP AVVIIAVLLA FVPPLVLSGA ALSDWVYRAL IFLVISCPCA 

       370        380        390        400        410        420 
LVVSIPLGFF GGIGAASKAG VLVKGSNYLE ALNQVKYAVF DKTGTLTKGS FEVTEIKPAE 

       430        440        450        460        470        480 
GFTKDRLLEA AAYAELHSQH PIAESVRKAY GKMLSSDEIE SYEEISGHGI FAKVNGTEIL 

       490        500        510        520        530        540 
AGNKKLMERE QIEDVPDENA GTIVHVAVDQ RYAGAIIIAD EIKEDAAQAV ADLKSLGIKQ 

       550        560        570        580        590        600 
TAMLTGDSKQ TGEAVGKQLG IGEVYAELLP QDKVAQVEAL EAKLLPSEKL IFVGDGINDT 

       610        620        630        640        650        660 
PVLARADIGV AMGGLGSDAA VEAADIVLMT DQPSKIAEAI RIAKRTRRIV WQNIGFALGV 

       670        680        690        700 
KAIFLILGAF GIATMWEAVF SDVGVTLLAV ANAMRVMRLK NK

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 9384377] [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: 11267663] [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: 11934502] [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: 12779235] [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: 16901659] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
Strain: 168 / PY79.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB15354.2. Different initiation.
PIRD70041.
RefSeqNP_391229.2. NC_000964.3.

3D structure databases

HSSPHSSP built from PDB template 2AJ1 based on UniProtKB Q60048.
ProteinModelPortalO32219.
SMRO32219. Positions 4-74, 190-302, 377-650.
ModBaseSearch...

Protein family/group databases

TCDB3.A.3.6.10. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003445; EBBACP00000003445; EBBACG00000003438.
GeneID936034.
GenomeReviewsGene locus BSU33490 in contig AL009126_GR.
KEGGbsu:BSU33490.
NMPDRfig|224308.1.peg.3355.
PATRIC18978700. VBIBacSub10457_3513.

Organism-specific databases

GenoListBSU33490. [Micado]

Phylogenomic databases

GeneTreeEBGT00070000031791.
HOGENOMHBG507745.
OMAARSIMEA.
PhylomeDBO32219.
ProtClustDBCLSK887878.

Enzyme and pathway databases

BioCycBSUB:BSU33490-MONOMER.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR001366. ATPase_P-typ_Cd-transp.
IPR006404. ATPase_P-typ_Cd/Co/Hg/Pb/Zn.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK01534.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00403. HMA. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00941. CDATPASE.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
SSF55008. HeavyMe_transpt. 1 hit.
TIGRFAMsTIGR01512. ATPase-IB2_Cd. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCADA_BACSU
AccessionPrimary (citable) accession number: O32219
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents