ID   ZNUC_ACIAD              Reviewed;         259 AA.
AC   Q6FFL0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Zinc import ATP-binding protein ZnuC {ECO:0000255|HAMAP-Rule:MF_01725};
DE            EC=7.2.2.20 {ECO:0000255|HAMAP-Rule:MF_01725};
GN   Name=znuC {ECO:0000255|HAMAP-Rule:MF_01725}; OrderedLocusNames=ACIAD0175;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Part of the ABC transporter complex ZnuABC involved in zinc
CC       import. Responsible for energy coupling to the transport system.
CC       {ECO:0000255|HAMAP-Rule:MF_01725}.
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:0000255|HAMAP-Rule:MF_01725};
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:0000255|HAMAP-Rule:MF_01725}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01725}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01725}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Zinc importer
CC       (TC 3.A.1.15.5) family. {ECO:0000255|HAMAP-Rule:MF_01725}.
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DR   EMBL; CR543861; CAG67147.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6FFL0; -.
DR   SMR; Q6FFL0; -.
DR   STRING; 62977.ACIAD0175; -.
DR   EnsemblBacteria; CAG67147; CAG67147; ACIAD0175.
DR   KEGG; aci:ACIAD0175; -.
DR   eggNOG; COG1121; Bacteria.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; GHDHVHP; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015633; F:ABC-type zinc transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   InterPro; IPR017882; ZnuC.
DR   PANTHER; PTHR42734:SF9; PTHR42734:SF9; 1.
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.
DR   PROSITE; PS51298; ZNUC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport; Zinc;
KW   Zinc transport.
FT   CHAIN           1..259
FT                   /note="Zinc import ATP-binding protein ZnuC"
FT                   /id="PRO_0000281488"
FT   DOMAIN          11..225
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
SQ   SEQUENCE   259 AA;  29372 MW;  A6059CFB4B9A77EC CRC64;
     MQISPIAPEL IRLENIYVHR DERDILKNID FSLHQNEIVT LIGPNGAGKS TLIKILLGII
     FPNKGKVIAK KKLKMAYVPQ KFNPSHSLPL RVCDLLDLEK CSATLREEII QDTGISKLQT
     AKVQQLSGGE RQRVLLARAL LRQPDILVLD EPMQGLDIQS EAELYEYVRS LPERYGCAIL
     MVSHDLQWVM QGTQRVVCLN KHICCSGLPE SVQQHPEYLA IFGGQRVPYQ HHHDHCAHGD
     HVEQCNHIDH PHIHPEPEA