ID   CUTA_YERPS              Reviewed;         119 AA.
AC   Q66FE0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Divalent-cation tolerance protein CutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN   Name=cutA {ECO:0000255|HAMAP-Rule:MF_01160}; OrderedLocusNames=YPTB0400;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH19640.1; -; Genomic_DNA.
DR   RefSeq; WP_002209122.1; NC_006155.1.
DR   AlphaFoldDB; Q66FE0; -.
DR   SMR; Q66FE0; -.
DR   EnsemblBacteria; CAH19640; CAH19640; YPTB0400.
DR   GeneID; 66843186; -.
DR   KEGG; yps:YPTB0400; -.
DR   OMA; VYTTFPD; -.
DR   Proteomes; UP000001011; 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_0000157127"
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