ID   CUTA_YERPY              Reviewed;         119 AA.
AC   B1JMR6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Divalent-cation tolerance protein CutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN   Name=cutA {ECO:0000255|HAMAP-Rule:MF_01160}; OrderedLocusNames=YPK_3827;
OS   Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YPIII;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT   "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
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; CP000950; ACA70093.1; -; Genomic_DNA.
DR   RefSeq; WP_002209122.1; NC_010465.1.
DR   AlphaFoldDB; B1JMR6; -.
DR   SMR; B1JMR6; -.
DR   EnsemblBacteria; ACA70093; ACA70093; YPK_3827.
DR   GeneID; 66843186; -.
DR   KEGG; ypy:YPK_3827; -.
DR   OMA; VYTTFPD; -.
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_1000137858"
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