ID   CUTA_YERP3              Reviewed;         119 AA.
AC   A7FN06;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Divalent-cation tolerance protein CutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN   Name=cutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN   OrderedLocusNames=YpsIP31758_3680;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT   causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS49887.1; -; Genomic_DNA.
DR   RefSeq; WP_002209122.1; NC_009708.1.
DR   AlphaFoldDB; A7FN06; -.
DR   SMR; A7FN06; -.
DR   EnsemblBacteria; ABS49887; ABS49887; YpsIP31758_3680.
DR   GeneID; 66843186; -.
DR   KEGG; ypi:YpsIP31758_3680; -.
DR   HOGENOM; CLU_098807_3_0_6; -.
DR   OMA; VYTTFPD; -.
DR   Proteomes; UP000002412; 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..119
FT                   /note="Divalent-cation tolerance protein CutA"
FT                   /id="PRO_1000065599"
FT   BINDING         23
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT   BINDING         90
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT   BINDING         91
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
SQ   SEQUENCE   119 AA;  13173 MW;  59CB1DD130D2A815 CRC64;
     MSDSDAMTDP NAVSYSNAIV VLCTAPDEAS AQNLAAQVLG EKLAACVTLL PGATSLYYWE
     GKLEQEYEVQ LLFKSNTDHQ QALLTYIKQH HPYQTPELLV LPVRDGDKDY LSWLNASLL