ID   CUTA_SALA4              Reviewed;         115 AA.
AC   B5F2K4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Divalent-cation tolerance protein CutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN   Name=cutA {ECO:0000255|HAMAP-Rule:MF_01160}; OrderedLocusNames=SeAg_B4602;
OS   Salmonella agona (strain SL483).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=454166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL483;
RX   PubMed=21602358; DOI=10.1128/jb.00297-11;
RA   Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA   Leclerc J.E., Ravel J., Cebula T.A.;
RT   "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT   CRISPR-mediated adaptive sublineage evolution.";
RL   J. Bacteriol. 193:3556-3568(2011).
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}.
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DR   EMBL; CP001138; ACH48938.1; -; Genomic_DNA.
DR   RefSeq; WP_000887832.1; NC_011149.1.
DR   AlphaFoldDB; B5F2K4; -.
DR   SMR; B5F2K4; -.
DR   EnsemblBacteria; ACH48938; ACH48938; SeAg_B4602.
DR   GeneID; 66758552; -.
DR   KEGG; sea:SeAg_B4602; -.
DR   HOGENOM; CLU_098807_3_0_6; -.
DR   OMA; VYTTFPD; -.
DR   Proteomes; UP000008819; 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..115
FT                   /note="Divalent-cation tolerance protein CutA"
FT                   /id="PRO_1000137847"
FT   BINDING         19
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT   BINDING         86
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT   BINDING         87
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
SQ   SEQUENCE   115 AA;  12681 MW;  468E359192E5E74B CRC64;
     MLDVKSQDIS IPEAVVVLCT APDEATAQDL AAKVLAEKLA ACATLLPGAT SLYYWEGKLE
     QEYEVQMILK TTVSHQQALI DCLKSHHPYQ TPELLVLPVT HGDTDYLSWL NASLR