ZNUC_ECOLI
ID ZNUC_ECOLI Reviewed; 251 AA.
AC P0A9X1; P52648; P76285;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
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, ECO:0000269|PubMed:9680209};
GN Name=znuC {ECO:0000255|HAMAP-Rule:MF_01725}; Synonyms=yebM;
GN OrderedLocusNames=b1858, JW1847;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / EMG2;
RA Robison K., O'Keeffe T., Church G.M.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN ZINC TRANSPORT, INDUCTION, ATPASE ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12;
RX PubMed=9680209; DOI=10.1046/j.1365-2958.1998.00883.x;
RA Patzer S.I., Hantke K.;
RT "The ZnuABC high-affinity zinc uptake system and its regulator Zur in
RT Escherichia coli.";
RL Mol. Microbiol. 28:1199-1210(1998).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16159766; DOI=10.1128/jb.187.18.6333-6340.2005;
RA Yamamoto K., Ishihama A.;
RT "Transcriptional response of Escherichia coli to external zinc.";
RL J. Bacteriol. 187:6333-6340(2005).
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, ECO:0000269|PubMed:9680209}.
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 ECO:0000269|PubMed:9680209};
CC -!- ACTIVITY REGULATION: Inhibited by arsenate.
CC {ECO:0000269|PubMed:9680209}.
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 -!- INDUCTION: Transcriptionally repressed by zur (zinc uptake regulator),
CC in response to high extracellular zinc concentrations.
CC {ECO:0000269|PubMed:16159766, ECO:0000269|PubMed:9680209}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Zinc importer
CC (TC 3.A.1.15.5) family. {ECO:0000255|HAMAP-Rule:MF_01725}.
CC -!- SEQUENCE CAUTION:
CC Sequence=U38702; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U38702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U00096; AAC74928.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15666.1; -; Genomic_DNA.
DR PIR; B64948; B64948.
DR RefSeq; NP_416372.1; NC_000913.3.
DR RefSeq; WP_000202996.1; NZ_STEB01000009.1.
DR AlphaFoldDB; P0A9X1; -.
DR SMR; P0A9X1; -.
DR BioGRID; 4263224; 5.
DR ComplexPortal; CPX-4407; Zinc ABC transporter complex.
DR DIP; DIP-48234N; -.
DR IntAct; P0A9X1; 13.
DR STRING; 511145.b1858; -.
DR TCDB; 3.A.1.15.5; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0A9X1; -.
DR PRIDE; P0A9X1; -.
DR EnsemblBacteria; AAC74928; AAC74928; b1858.
DR EnsemblBacteria; BAA15666; BAA15666; BAA15666.
DR GeneID; 66674252; -.
DR GeneID; 946374; -.
DR KEGG; ecj:JW1847; -.
DR KEGG; eco:b1858; -.
DR PATRIC; fig|1411691.4.peg.390; -.
DR EchoBASE; EB2931; -.
DR eggNOG; COG1121; Bacteria.
DR HOGENOM; CLU_000604_1_11_6; -.
DR InParanoid; P0A9X1; -.
DR OMA; GHDHVHP; -.
DR PhylomeDB; P0A9X1; -.
DR BioCyc; EcoCyc:ZNUC-MON; -.
DR BioCyc; MetaCyc:ZNUC-MON; -.
DR PRO; PR:P0A9X1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0015633; F:ABC-type zinc transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central.
DR GO; GO:0055069; P:zinc ion homeostasis; IC:ComplexPortal.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IC:ComplexPortal.
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 1: Evidence at protein level;
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..251
FT /note="Zinc import ATP-binding protein ZnuC"
FT /id="PRO_0000093130"
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"
FT CONFLICT 80..83
FT /note="TTLP -> STLS (in Ref. 1; U38702)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="L -> W (in Ref. 1; U38702)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="V -> A (in Ref. 1; U38702)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="G -> W (in Ref. 1; U38702)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..176
FT /note="VLM -> ALL (in Ref. 1; U38702)"
FT /evidence="ECO:0000305"
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
