ID   CUTA_YERPB              Reviewed;         119 AA.
AC   B2K1X9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Divalent-cation tolerance protein CutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN   Name=cutA {ECO:0000255|HAMAP-Rule:MF_01160}; OrderedLocusNames=YPTS_0426;
OS   Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=502801;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB1/+;
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 PB1/+.";
RL   Submitted (APR-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}.
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DR   EMBL; CP001048; ACC87414.1; -; Genomic_DNA.
DR   RefSeq; WP_002209122.1; NC_010634.1.
DR   AlphaFoldDB; B2K1X9; -.
DR   SMR; B2K1X9; -.
DR   GeneID; 66843186; -.
DR   KEGG; ypb:YPTS_0426; -.
DR   OMA; VYTTFPD; -.
DR   BioCyc; YPSE502801:YPTS_RS02220-MON; -.
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_1000137856"
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