ID   ZNUC_BACSU              Reviewed;         231 AA.
AC   O34946; Q797R5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=High-affinity zinc uptake system ATP-binding protein ZnuC;
DE            EC=7.2.2.20;
GN   Name=znuC; Synonyms=adcC, ycdI; OrderedLocusNames=BSU02860;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9274031; DOI=10.1099/00221287-143-8-2775;
RA   Kumano M., Tamakoshi A., Yamane K.;
RT   "A 32 kb nucleotide sequence from the region of the lincomycin-resistance
RT   gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and
RT   identification of the site of the lin-2 mutation.";
RL   Microbiology 143:2775-2782(1997).
RN   [2]
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   [3]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=9811636; DOI=10.1128/jb.180.22.5815-5821.1998;
RA   Gaballa A., Helmann J.D.;
RT   "Identification of a zinc-specific metalloregulatory protein, Zur,
RT   controlling zinc transport operons in Bacillus subtilis.";
RL   J. Bacteriol. 180:5815-5821(1998).
RN   [4]
RP   INDUCTION.
RC   STRAIN=168;
RX   PubMed=12426338; DOI=10.1128/jb.184.23.6508-6514.2002;
RA   Gaballa A., Wang T., Ye R.W., Helmann J.D.;
RT   "Functional analysis of the Bacillus subtilis Zur regulon.";
RL   J. Bacteriol. 184:6508-6514(2002).
RN   [5]
RP   FUNCTION IN COMPETENCE DEVELOPMENT, DISRUPTION PHENOTYPE, AND GENE NAME.
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: Part of the high-affinity ABC transporter complex ZnuABC
CC       involved in zinc import (Probable). Responsible for energy coupling to
CC       the transport system (By similarity). ZnuABC-mediated zinc transport is
CC       required for comF expression and competence development. {ECO:0000250,
CC       ECO:0000269|PubMed:21813502, ECO:0000269|PubMed:9811636, ECO:0000305}.
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   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ZnuC),
CC       two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- INDUCTION: Repressed by zinc via the metallo-regulatory protein Zur.
CC       {ECO:0000269|PubMed:12426338, ECO:0000269|PubMed:9811636}.
CC   -!- DISRUPTION PHENOTYPE: Disruption results in low transformability.
CC       {ECO:0000269|PubMed:21813502}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB000617; BAA22247.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12080.1; -; Genomic_DNA.
DR   PIR; B69756; B69756.
DR   RefSeq; NP_388168.1; NC_000964.3.
DR   RefSeq; WP_003234730.1; NZ_JNCM01000030.1.
DR   AlphaFoldDB; O34946; -.
DR   SMR; O34946; -.
DR   STRING; 224308.BSU02860; -.
DR   TCDB; 3.A.1.15.11; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O34946; -.
DR   PRIDE; O34946; -.
DR   EnsemblBacteria; CAB12080; CAB12080; BSU_02860.
DR   GeneID; 938374; -.
DR   KEGG; bsu:BSU02860; -.
DR   PATRIC; fig|224308.179.peg.297; -.
DR   eggNOG; COG1121; Bacteria.
DR   InParanoid; O34946; -.
DR   OMA; GHDHVHP; -.
DR   PhylomeDB; O34946; -.
DR   BioCyc; BSUB:BSU02860-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR   GO; GO:0015633; F:ABC-type zinc transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Ion transport; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport; Zinc; Zinc transport.
FT   CHAIN           1..231
FT                   /note="High-affinity zinc uptake system ATP-binding protein
FT                   ZnuC"
FT                   /id="PRO_0000360808"
FT   DOMAIN          4..230
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   231 AA;  26319 MW;  61A4A615633C6A0F CRC64;
     MNLVSLKDIV FGYSHTPVLD KVSLDIESGE FVGITGPNGA SKSTLIKVML GMLKPWEGTV
     TISKRNTEGK RLTIGYVPQQ ISSFNAGFPS TVLELVQSGR YTKGKWFKRL NEEDHLEVEK
     ALKMVEMWDL RHRKIGDLSG GQKQKICIAR MLASNPDLLM LDEPTTAVDY DSRKGFYEFM
     HHLVKNHNRT VVMVTHEQNE VQQFLDKVIR LERGEKGGWK CLTWNSCDEL F