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Protein

Zinc-transporting ATPase

Gene

zosA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Couples the hydrolysis of ATP with the transport of zinc into the cell. Plays an important role in protecting cells against oxidative stress. ZosA-mediated zinc transport is required for post-transcriptional control of comK and competence development.2 Publications

Catalytic activityi

ATP + H2O + Zn2+(Out) = ADP + phosphate + Zn2+(In).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei337 – 33714-aspartylphosphate intermediateBy similarity
Metal bindingi535 – 5351MagnesiumBy similarity
Metal bindingi539 – 5391MagnesiumBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Ion transport, Transport, Zinc transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU13850-MONOMER.

Protein family/group databases

TCDBi3.A.3.6.9. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc-transporting ATPase (EC:3.6.3.-)
Alternative name(s):
Zn(2+)-translocating P-type ATPase
Gene namesi
Name:zosA
Synonyms:ykvW
Ordered Locus Names:BSU13850
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei43 – 6321HelicalSequence analysisAdd
BLAST
Transmembranei89 – 10921HelicalSequence analysisAdd
BLAST
Transmembranei258 – 27821HelicalSequence analysisAdd
BLAST
Transmembranei286 – 30621HelicalSequence analysisAdd
BLAST
Transmembranei599 – 61921HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Disruption results in low transformability, which can be rescued by the addition of excess zinc.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Zinc-transporting ATPasePRO_0000360853Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO31688.

Expressioni

Inductioni

By hydrogen peroxide. Repressed by PerR.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007681.

Structurei

3D structure databases

ProteinModelPortaliO31688.
SMRiO31688. Positions 127-238, 313-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250399.
InParanoidiO31688.
KOiK01534.
OMAiRQTRSII.
OrthoDBiEOG6742RM.
PhylomeDBiO31688.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
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.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00941. CDATPASE.
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEQVIVQRD PHEPLKTDKR EKNWAQHAEL IAALVSGALI LAGWLLSGYQ
60 70 80 90 100
VLSIILFLLA FVIGGFAKAK EGIEETLESK TLNVELLMIF AAIGSALIGY
110 120 130 140 150
WAEGAILIFI FSLSGALETY TMNKSSRDLT SLMQLEPEEA TLMVNGETKR
160 170 180 190 200
VPVSDLQAGD MIVIKPGERV AADGIIESGS TSLDESALTG ESMPVEKNTG
210 220 230 240 250
DTVFTGTVNR NGSLTVRVTK ANEDSLFRKI IKLVESAQNS VSPAQAFIER
260 270 280 290 300
FENAYVKGVL IAVALLLFVP HFALGWSWSE TFYRAMVFMV VASPCALVAS
310 320 330 340 350
IMPAALSLIS NGARNGMLVK GSVFLEQLGS VQMIAFDKTG TVTKGQPAVE
360 370 380 390 400
TIRIAEGFSE AEVLEAVYAI ETQSSHPLAQ AITAYAESRG VNQSGYISIE
410 420 430 440 450
ETSGFGVMAE VSGAKWKVGK AGFIGEEMAA QFMKQTASDV IQSGHTIVFV
460 470 480 490 500
KKDDQIAGCI ALKDQIRPEA KEVMEELNRL GIKTAMLTGD HEDTAQAIAK
510 520 530 540 550
EAGMTTVVAE CLPDQKVNEI KRLKEEFGTI AMVGDGINDA PALKAADVGI
560 570 580 590 600
AMGGGTDVAL ETADMVLMKN DLKKLVNMCR LSRKMNRIIK QNIVFSLAVI
610 620 630
CLLICANFLQ AMELPFGVIG HEGSTILVIL NGLRLLK
Length:637
Mass (Da):68,566
Last modified:January 1, 1998 - v1
Checksum:i62DBA8089CC83322
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13258.1.
PIRiF69869.
RefSeqiNP_389268.1. NC_000964.3.
WP_003245873.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13258; CAB13258; BSU13850.
GeneIDi939268.
KEGGibsu:BSU13850.
PATRICi18974551. VBIBacSub10457_1467.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13258.1.
PIRiF69869.
RefSeqiNP_389268.1. NC_000964.3.
WP_003245873.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO31688.
SMRiO31688. Positions 127-238, 313-589.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007681.

Protein family/group databases

TCDBi3.A.3.6.9. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PaxDbiO31688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13258; CAB13258; BSU13850.
GeneIDi939268.
KEGGibsu:BSU13850.
PATRICi18974551. VBIBacSub10457_1467.

Phylogenomic databases

eggNOGiENOG4105C59. Bacteria.
COG2217. LUCA.
HOGENOMiHOG000250399.
InParanoidiO31688.
KOiK01534.
OMAiRQTRSII.
OrthoDBiEOG6742RM.
PhylomeDBiO31688.

Enzyme and pathway databases

BioCyciBSUB:BSU13850-MONOMER.

Family and domain databases

Gene3Di2.70.150.10. 1 hit.
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.
IPR027256. P-typ_ATPase_IB.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00941. CDATPASE.
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEiPS00154. ATPASE_E1_E2. 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. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION, GENE NAME.
    Strain: 168 / CU1065.
  3. "ZnuABC and ZosA zinc transporters are differently involved in competence development in Bacillus subtilis."
    Ogura M.
    J. Biochem. 150:615-625(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION IN COMPETENCE DEVELOPMENT.
    Strain: 168.

Entry informationi

Entry nameiZOSA_BACSU
AccessioniPrimary (citable) accession number: O31688
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 122 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.