CUTA_ECOUT
ID CUTA_ECOUT Reviewed; 112 AA.
AC Q1R3C3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Divalent-cation tolerance protein CutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN Name=cutA {ECO:0000255|HAMAP-Rule:MF_01160}; OrderedLocusNames=UTI89_C4734;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC -!- FUNCTION: Involved in resistance toward heavy metals.
CC {ECO:0000255|HAMAP-Rule:MF_01160}.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01160};
CC Note=Binds 1 copper ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01160};
CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01160}.
CC -!- SIMILARITY: Belongs to the CutA family. {ECO:0000255|HAMAP-
CC Rule:MF_01160}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE10141.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000243; ABE10141.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000883409.1; NC_007946.1.
DR AlphaFoldDB; Q1R3C3; -.
DR SMR; Q1R3C3; -.
DR EnsemblBacteria; ABE10141; ABE10141; UTI89_C4734.
DR KEGG; eci:UTI89_C4734; -.
DR HOGENOM; CLU_098807_3_0_6; -.
DR OMA; VYTTFPD; -.
DR Proteomes; UP000001952; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0010038; P:response to metal ion; IEA:InterPro.
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 3: Inferred from homology;
KW Copper; Cytoplasm; Metal-binding.
FT CHAIN 1..112
FT /note="Divalent-cation tolerance protein CutA"
FT /id="PRO_0000280483"
FT BINDING 16
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
SQ SEQUENCE 112 AA; 12361 MW; D02145EF103CC6C2 CRC64;
MLDEKSSNTT SVVVLCTAPD EATAQDLAAK VLAEKLAACA TLIPGATSLY YWEGKLEQEY
EVQMILKTTV SHQQALLECL KSHHPYQTPE LLVLPVTHGD TDYLSWLNAS LR