ZNUC_HYDCU
ID ZNUC_HYDCU Reviewed; 258 AA.
AC Q31I51;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Tcr_0576;
OS Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) (Thiomicrospira
OS crunogena).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=317025;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25203 / XCL-2;
RX PubMed=17105352; DOI=10.1371/journal.pbio.0040383;
RA Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A.,
RA Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F.,
RA Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L.,
RA Hauser L.J., Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M.,
RA Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E.,
RA Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H.,
RA Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P.,
RA Tinkham L.E., Zeruth G.T.;
RT "The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena
RT XCL-2.";
RL PLoS Biol. 4:1-17(2006).
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; CP000109; ABB41172.1; -; Genomic_DNA.
DR RefSeq; WP_011369997.1; NC_007520.2.
DR AlphaFoldDB; Q31I51; -.
DR SMR; Q31I51; -.
DR STRING; 317025.Tcr_0576; -.
DR EnsemblBacteria; ABB41172; ABB41172; Tcr_0576.
DR KEGG; tcx:Tcr_0576; -.
DR eggNOG; COG1121; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR OMA; GHDHVHP; -.
DR OrthoDB; 1721927at2; -.
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..258
FT /note="Zinc import ATP-binding protein ZnuC"
FT /id="PRO_0000281558"
FT DOMAIN 7..233
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
SQ SEQUENCE 258 AA; 28732 MW; 4992D310CCDBC4B8 CRC64;
MTTSPLITAK NINHAYGNKT VLNDISLTLH SNEIVTLIGP NGAGKSTLLK ILLNLIQPTS
GEVTRKTGLR IGFMPQKIQV DASMPLSVQR FLELGLARQS QTLFNKKTND TTELHEVIND
LKLNDLLTHP IQQVSGGEMQ RILLARALLR NPELLILDEP VQGVDLQGQT ELYHYISEIR
DKYGCGILMV SHDLHIVMRS TNKVLCLNQH LCCSGLPQTV SGSPAFQELF GQGFEEVAFY
EHHHDDRVCT HTHGHTET