CUTA_ECOLI
ID CUTA_ECOLI Reviewed; 112 AA.
AC P69488; P36654; Q2M6G7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Divalent-cation tolerance protein CutA;
DE AltName: Full=C-type cytochrome biogenesis protein CycY;
GN Name=cutA; Synonyms=cutA1, cycY; OrderedLocusNames=b4137, JW4097;
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;
RX PubMed=7623667; DOI=10.1111/j.1365-2958.1995.tb02287.x;
RA Crooke H.R., Cole J.A.;
RT "The biogenesis of c-type cytochromes in Escherichia coli requires a
RT membrane-bound protein, DipZ, with a protein disulphide isomerase-like
RT domain.";
RL Mol. Microbiol. 15:1139-1150(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7623666; DOI=10.1111/j.1365-2958.1995.tb02286.x;
RA Fong S.-T., Camakaris J., Lee B.T.O.;
RT "Molecular genetics of a chromosomal locus involved in copper tolerance in
RT Escherichia coli K-12.";
RL Mol. Microbiol. 15:1127-1137(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
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 [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), COFACTOR, AND SUBUNIT.
RC STRAIN=LE392;
RX PubMed=12949080; DOI=10.1074/jbc.m304398200;
RA Arnesano F., Banci L., Benvenuti M., Bertini I., Calderone V., Mangani S.,
RA Viezzoli M.S.;
RT "The evolutionarily conserved trimeric structure of CutA1 proteins suggests
RT a role in signal transduction.";
RL J. Biol. Chem. 278:45999-46006(2003).
CC -!- FUNCTION: Involved in resistance toward heavy metals.
CC {ECO:0000269|PubMed:7623666}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000305|PubMed:12949080};
CC Note=Binds 1 copper ion per subunit. {ECO:0000305|PubMed:12949080};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12949080}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7623666}.
CC -!- SIMILARITY: Belongs to the CutA family. {ECO:0000305}.
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DR EMBL; X77707; CAA54780.1; -; Genomic_DNA.
DR EMBL; Z36905; CAA85374.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97036.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77097.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78139.1; -; Genomic_DNA.
DR PIR; I41027; I41027.
DR RefSeq; NP_418560.1; NC_000913.3.
DR RefSeq; WP_000883400.1; NZ_STEB01000014.1.
DR PDB; 1NAQ; X-ray; 1.70 A; A/B/C/D/E/F=1-112.
DR PDB; 3AA8; X-ray; 2.30 A; A/B/C=1-112.
DR PDB; 3AA9; X-ray; 2.30 A; A/B/C=1-112.
DR PDB; 3AH6; X-ray; 2.40 A; A/B/C/D/E/F=1-112.
DR PDB; 3X3U; X-ray; 2.09 A; A/B/C/D/E/F=1-112.
DR PDB; 4Y65; X-ray; 1.70 A; A/B/C=1-112.
DR PDB; 4Y6I; X-ray; 1.70 A; A/B/C/D/E/F=5-112.
DR PDBsum; 1NAQ; -.
DR PDBsum; 3AA8; -.
DR PDBsum; 3AA9; -.
DR PDBsum; 3AH6; -.
DR PDBsum; 3X3U; -.
DR PDBsum; 4Y65; -.
DR PDBsum; 4Y6I; -.
DR AlphaFoldDB; P69488; -.
DR SMR; P69488; -.
DR BioGRID; 4262693; 8.
DR BioGRID; 852952; 1.
DR DIP; DIP-47984N; -.
DR IntAct; P69488; 10.
DR STRING; 511145.b4137; -.
DR DrugBank; DB03975; Mercuribenzoic Acid.
DR jPOST; P69488; -.
DR PaxDb; P69488; -.
DR PRIDE; P69488; -.
DR EnsemblBacteria; AAC77097; AAC77097; b4137.
DR EnsemblBacteria; BAE78139; BAE78139; BAE78139.
DR GeneID; 66671951; -.
DR GeneID; 948660; -.
DR KEGG; ecj:JW4097; -.
DR KEGG; eco:b4137; -.
DR PATRIC; fig|1411691.4.peg.2563; -.
DR EchoBASE; EB2094; -.
DR eggNOG; COG1324; Bacteria.
DR HOGENOM; CLU_098807_3_0_6; -.
DR InParanoid; P69488; -.
DR OMA; VYTTFPD; -.
DR PhylomeDB; P69488; -.
DR BioCyc; EcoCyc:EG12177-MON; -.
DR EvolutionaryTrace; P69488; -.
DR PRO; PR:P69488; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0046688; P:response to copper ion; IMP:EcoCyc.
DR Gene3D; 3.30.70.120; -; 1.
DR HAMAP; MF_01160; CutA; 1.
DR InterPro; IPR023700; CutA_Enterobact.
DR InterPro; IPR004323; Ion_tolerance_CutA.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR PANTHER; PTHR23419; PTHR23419; 1.
DR Pfam; PF03091; CutA1; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Cytoplasm; Metal-binding; Reference proteome.
FT CHAIN 1..112
FT /note="Divalent-cation tolerance protein CutA"
FT /id="PRO_0000157118"
FT BINDING 16
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000305"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000305"
FT BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="A -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT TURN 4..6
FT /evidence="ECO:0007829|PDB:4Y65"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:1NAQ"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:1NAQ"
FT STRAND 38..52
FT /evidence="ECO:0007829|PDB:1NAQ"
FT STRAND 55..69
FT /evidence="ECO:0007829|PDB:1NAQ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1NAQ"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:1NAQ"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:4Y65"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1NAQ"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:1NAQ"
SQ SEQUENCE 112 AA; 12331 MW; 802145EF012DDB69 CRC64;
MLDEKSSNTA SVVVLCTAPD EATAQDLAAK VLAEKLAACA TLIPGATSLY YWEGKLEQEY
EVQMILKTTV SHQQALLECL KSHHPYQTPE LLVLPVTHGD TDYLSWLNAS LR
