ID   CUTA_PECAS              Reviewed;         110 AA.
AC   Q6D9J5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Divalent-cation tolerance protein CutA;
GN   Name=cutA; OrderedLocusNames=ECA0619;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
CC   -!- FUNCTION: Involved in resistance toward heavy metals. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CutA family. {ECO:0000305}.
CC   -!- CAUTION: Gln-81 is present instead of the conserved His which is
CC       expected to be a metal-binding residue. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG73535.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX950851; CAG73535.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_014914061.1; NC_004547.2.
DR   AlphaFoldDB; Q6D9J5; -.
DR   SMR; Q6D9J5; -.
DR   STRING; 218491.ECA0619; -.
DR   EnsemblBacteria; CAG73535; CAG73535; ECA0619.
DR   GeneID; 61410870; -.
DR   KEGG; eca:ECA0619; -.
DR   eggNOG; COG1324; Bacteria.
DR   HOGENOM; CLU_098807_3_1_6; -.
DR   OMA; VYTTFPD; -.
DR   OrthoDB; 1801957at2; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
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; Reference proteome.
FT   CHAIN           1..110
FT                   /note="Divalent-cation tolerance protein CutA"
FT                   /id="PRO_0000157121"
FT   BINDING         14
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   110 AA;  12212 MW;  C88A63E79C82480E CRC64;
     MSDRPLCDAV VILCTAPDDA CAQRLANSLL ETRLAACVTL LPGARSLYYW EGKLEQQSEV
     QMLIKSDTSH QQALLTHLKQ QHPYDTPELL VLPVSGGDSD YLTWLNASLR