ID   ZNUC_ECOK1              Reviewed;         251 AA.
AC   A1AC19;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Ecok1_17150;
GN   ORFNames=APECO1_908;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ01209.1; -; Genomic_DNA.
DR   RefSeq; WP_000202996.1; NC_008563.1.
DR   AlphaFoldDB; A1AC19; -.
DR   SMR; A1AC19; -.
DR   EnsemblBacteria; ABJ01209; ABJ01209; APECO1_908.
DR   GeneID; 66674252; -.
DR   KEGG; ecv:APECO1_908; -.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; GHDHVHP; -.
DR   Proteomes; UP000008216; 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; 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; 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..251
FT                   /note="Zinc import ATP-binding protein ZnuC"
FT                   /id="PRO_0000281506"
FT   DOMAIN          5..220
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
SQ   SEQUENCE   251 AA;  27867 MW;  F4BF845AC3C7904C CRC64;
     MTSLVSLENV SVSFGQRRVL SDVSLELKPG KILTLLGPNG AGKSTLVRVV LGLVTPDEGV
     IKRNGKLRIG YVPQKLYLDT TLPLTVNRFL RLRPGTHKED ILPALKRVQA GHLINAPMQK
     LSGGETQRVL LARALLNRPQ LLVLDEPTQG VDVNGQVALY DLIDQLRREL DCGVLMVSHD
     LHLVMAKTDE VLCLNHHICC SGTPEVVSLH PEFISMFGPR GAEQLGIYRH HHNHRHDLQG
     RIVLRRGNDR S