ZOSA_BACSU
ID ZOSA_BACSU Reviewed; 637 AA.
AC O31688;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc-transporting ATPase;
DE EC=7.2.2.20 {ECO:0000269|PubMed:12180919};
DE AltName: Full=ABC-type Zn(2+) transporter {ECO:0000305};
DE AltName: Full=Zn(2+)-translocating P-type ATPase;
GN Name=zosA; Synonyms=ykvW; OrderedLocusNames=BSU13850;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND GENE NAME.
RC STRAIN=168 / CU1065;
RX PubMed=12180919; DOI=10.1046/j.1365-2958.2002.03068.x;
RA Gaballa A., Helmann J.D.;
RT "A peroxide-induced zinc uptake system plays an important role in
RT protection against oxidative stress in Bacillus subtilis.";
RL Mol. Microbiol. 45:997-1005(2002).
RN [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN COMPETENCE DEVELOPMENT.
RC STRAIN=168;
RX PubMed=21813502; DOI=10.1093/jb/mvr098;
RA Ogura M.;
RT "ZnuABC and ZosA zinc transporters are differently involved in competence
RT development in Bacillus subtilis.";
RL J. Biochem. 150:615-625(2011).
CC -!- FUNCTION: Couples the hydrolysis of ATP with the transport of zinc into
CC the cell. Plays an important role in protecting cells against oxidative
CC stress. ZosA-mediated zinc transport is required for post-
CC transcriptional control of comK and competence development.
CC {ECO:0000269|PubMed:12180919, ECO:0000269|PubMed:21813502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) +
CC phosphate(in) + Zn(2+)(in); Xref=Rhea:RHEA:29795, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29105, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.20;
CC Evidence={ECO:0000269|PubMed:12180919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29796;
CC Evidence={ECO:0000269|PubMed:12180919};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By hydrogen peroxide. Repressed by PerR.
CC {ECO:0000269|PubMed:12180919}.
CC -!- DISRUPTION PHENOTYPE: Disruption results in low transformability, which
CC can be rescued by the addition of excess zinc.
CC {ECO:0000269|PubMed:21813502}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000305}.
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DR EMBL; AL009126; CAB13258.1; -; Genomic_DNA.
DR PIR; F69869; F69869.
DR RefSeq; NP_389268.1; NC_000964.3.
DR RefSeq; WP_003245873.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31688; -.
DR SMR; O31688; -.
DR STRING; 224308.BSU13850; -.
DR TCDB; 3.A.3.6.9; the p-type atpase (p-atpase) superfamily.
DR PaxDb; O31688; -.
DR PRIDE; O31688; -.
DR EnsemblBacteria; CAB13258; CAB13258; BSU_13850.
DR GeneID; 939268; -.
DR KEGG; bsu:BSU13850; -.
DR PATRIC; fig|224308.179.peg.1509; -.
DR eggNOG; COG2217; Bacteria.
DR InParanoid; O31688; -.
DR OMA; HLHLMET; -.
DR PhylomeDB; O31688; -.
DR BioCyc; BSUB:BSU13850-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015633; F:ABC-type zinc transporter activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..637
FT /note="Zinc-transporting ATPase"
FT /id="PRO_0000360853"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 337
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 637 AA; 68566 MW; 62DBA8089CC83322 CRC64;
MNEQVIVQRD PHEPLKTDKR EKNWAQHAEL IAALVSGALI LAGWLLSGYQ VLSIILFLLA
FVIGGFAKAK EGIEETLESK TLNVELLMIF AAIGSALIGY WAEGAILIFI FSLSGALETY
TMNKSSRDLT SLMQLEPEEA TLMVNGETKR VPVSDLQAGD MIVIKPGERV AADGIIESGS
TSLDESALTG ESMPVEKNTG DTVFTGTVNR NGSLTVRVTK ANEDSLFRKI IKLVESAQNS
VSPAQAFIER FENAYVKGVL IAVALLLFVP HFALGWSWSE TFYRAMVFMV VASPCALVAS
IMPAALSLIS NGARNGMLVK GSVFLEQLGS VQMIAFDKTG TVTKGQPAVE TIRIAEGFSE
AEVLEAVYAI ETQSSHPLAQ AITAYAESRG VNQSGYISIE ETSGFGVMAE VSGAKWKVGK
AGFIGEEMAA QFMKQTASDV IQSGHTIVFV KKDDQIAGCI ALKDQIRPEA KEVMEELNRL
GIKTAMLTGD HEDTAQAIAK EAGMTTVVAE CLPDQKVNEI KRLKEEFGTI AMVGDGINDA
PALKAADVGI AMGGGTDVAL ETADMVLMKN DLKKLVNMCR LSRKMNRIIK QNIVFSLAVI
CLLICANFLQ AMELPFGVIG HEGSTILVIL NGLRLLK
