ID   ZNUC_SALPA              Reviewed;         251 AA.
AC   Q5PIA5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=SPA0977;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(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; CP000026; AAV76952.1; -; Genomic_DNA.
DR   RefSeq; WP_000203023.1; NC_006511.1.
DR   AlphaFoldDB; Q5PIA5; -.
DR   SMR; Q5PIA5; -.
DR   EnsemblBacteria; AAV76952; AAV76952; SPA0977.
DR   KEGG; spt:SPA0977; -.
DR   HOGENOM; CLU_000604_1_11_6; -.
DR   OMA; GHDHVHP; -.
DR   Proteomes; UP000008185; 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_0000281547"
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;  27685 MW;  2A593FD47BE79160 CRC64;
     MTSLVSLENV SVSFGQRRVL SDVSLELSPG KILTLLGPNG AGKSTLVRVV LGLVAPDEGV
     IKRNGQLRIG YVPQKLYLDT TLPLTVNRFL RLRPGTQKTD ILPALKRVQA GHLIDAPMQK
     LSGGETQRVL LARALLNRPQ LLVLDEPTQG VDVNGQVALY DLIDQLRREL DCAVLMVSHD
     LHLVMAKTDE VLCLNHHICC SGAPEVVSMH PEFISMFGPR GAEQLGIYRH HHNHRHDLQG
     RIVLRRGNGH S