ID   ZNUC_BRUME              Reviewed;         298 AA.
AC   Q8YDJ8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=BMEII0177;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53418.1; -; Genomic_DNA.
DR   PIR; AG3531; AG3531.
DR   RefSeq; WP_004680954.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YDJ8; -.
DR   SMR; Q8YDJ8; -.
DR   STRING; 224914.BMEII0177; -.
DR   EnsemblBacteria; AAL53418; AAL53418; BMEII0177.
DR   GeneID; 29595304; -.
DR   KEGG; bme:BMEII0177; -.
DR   eggNOG; COG1121; Bacteria.
DR   OMA; GHDHVHP; -.
DR   PRO; PR:Q8YDJ8; -.
DR   Proteomes; UP000000419; Chromosome II.
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; Translocase; Transport; Zinc; Zinc transport.
FT   CHAIN           1..298
FT                   /note="Zinc import ATP-binding protein ZnuC"
FT                   /id="PRO_0000281497"
FT   DOMAIN          17..232
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
FT   REGION          273..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         49..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
SQ   SEQUENCE   298 AA;  32334 MW;  05BEA1EDACDA7714 CRC64;
     MDKKSSHPAG AARDILIELR NAGVYRDGRW LVRNVDLSVE RGEIVTLIGQ NGAGKSTAAK
     MALHILKPDE GMVSHKPGLR IGYVPQKINI DRTLPLSVER LMTLTGPLPR KEIDAALEAV
     GIAHLAKAET AHLSGGEFQR ALMARALARK PDIMVLDEPV QGVDFSGEAA LYELIARLRD
     DTSCGVLLIS HDLHLVMAAT DRVICLNGHV CCSGTPRDVT SSPEYVRLFG SRAVGPLAVY
     EHHHDHTHLP DGRVLYADGT TADPIAGSTM GPRGHCHVED GHHHDHEHHH HEGGQPRA