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O31688 (ZOSA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. 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:
Zinc-transporting ATPase
EC=3.6.3.5
Alternative name(s):
Zn(2+)-translocating P-type ATPase
Gene names
Name:zosA
Synonyms:ykvW
Ordered Locus Names:BSU13850
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Couples the hydrolysis of ATP with the transport of zinc into the cell. Ref.2

Catalytic activity

ATP + H2O + Zn2+(In) = ADP + phosphate + Zn2+(Out). Ref.2

Subcellular location

Cell membrane; Multi-pass membrane protein.

Induction

By hydrogen peroxide. Repressed by PerR. Ref.2

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637Zinc-transporting ATPase
PRO_0000360853

Regions

Transmembrane28 – 4518Helical; Potential
Transmembrane51 – 6919Helical; Potential
Transmembrane81 – 10020Helical; Potential
Transmembrane106 – 12318Helical; Potential
Transmembrane259 – 27921Helical; Potential
Transmembrane285 – 30925Helical; Potential
Transmembrane593 – 61220Helical; Potential
Transmembrane618 – 63619Helical; Potential

Sites

Active site33714-aspartylphosphate intermediate Probable
Metal binding5351Magnesium By similarity
Metal binding5391Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
O31688 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 62DBA8089CC83322

FASTA63768,566
        10         20         30         40         50         60 
MNEQVIVQRD PHEPLKTDKR EKNWAQHAEL IAALVSGALI LAGWLLSGYQ VLSIILFLLA 

        70         80         90        100        110        120 
FVIGGFAKAK EGIEETLESK TLNVELLMIF AAIGSALIGY WAEGAILIFI FSLSGALETY 

       130        140        150        160        170        180 
TMNKSSRDLT SLMQLEPEEA TLMVNGETKR VPVSDLQAGD MIVIKPGERV AADGIIESGS 

       190        200        210        220        230        240 
TSLDESALTG ESMPVEKNTG DTVFTGTVNR NGSLTVRVTK ANEDSLFRKI IKLVESAQNS 

       250        260        270        280        290        300 
VSPAQAFIER FENAYVKGVL IAVALLLFVP HFALGWSWSE TFYRAMVFMV VASPCALVAS 

       310        320        330        340        350        360 
IMPAALSLIS NGARNGMLVK GSVFLEQLGS VQMIAFDKTG TVTKGQPAVE TIRIAEGFSE 

       370        380        390        400        410        420 
AEVLEAVYAI ETQSSHPLAQ AITAYAESRG VNQSGYISIE ETSGFGVMAE VSGAKWKVGK 

       430        440        450        460        470        480 
AGFIGEEMAA QFMKQTASDV IQSGHTIVFV KKDDQIAGCI ALKDQIRPEA KEVMEELNRL 

       490        500        510        520        530        540 
GIKTAMLTGD HEDTAQAIAK EAGMTTVVAE CLPDQKVNEI KRLKEEFGTI AMVGDGINDA 

       550        560        570        580        590        600 
PALKAADVGI AMGGGTDVAL ETADMVLMKN DLKKLVNMCR LSRKMNRIIK QNIVFSLAVI 

       610        620        630 
CLLICANFLQ AMELPFGVIG HEGSTILVIL NGLRLLK

« 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]"A peroxide-induced zinc uptake system plays an important role in protection against oxidative stress in Bacillus subtilis."
Gaballa A., Helmann J.D.
Mol. Microbiol. 45:997-1005(2002) [PubMed: 12180919] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB13258.1.
PIRF69869.
RefSeqNP_389268.1. NC_000964.3.

3D structure databases

ProteinModelPortalO31688.
SMRO31688. Positions 127-238, 313-589.
ModBaseSearch...

Protein family/group databases

TCDB3.A.3.6.9. P-type ATPase (P-ATPase) superfamily.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000002485; EBBACP00000002485; EBBACG00000002480.
GeneID939268.
GenomeReviewsGene locus BSU13850 in contig AL009126_GR.
KEGGbsu:BSU13850.
NMPDRfig|224308.1.peg.1387.
PATRIC18974551. VBIBacSub10457_1467.

Organism-specific databases

GenoListBSU13850. [Micado]

Phylogenomic databases

GeneTreeEBGT00070000031791.
HOGENOMHBG507745.
OMAPGWGVQA.
PhylomeDBO31688.
ProtClustDBCLSK872812.

Enzyme and pathway databases

BioCycBSUB:BSU13850-MONOMER.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
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.
IPR000150. Hypothet_cof.
[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.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00941. CDATPASE.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01512. ATPase-IB2_Cd. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameZOSA_BACSU
AccessionPrimary (citable) accession number: O31688
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 93 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