CUTA_SALTY
ID CUTA_SALTY Reviewed; 115 AA.
AC Q7CPA2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Divalent-cation tolerance protein CutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN Name=cutA {ECO:0000255|HAMAP-Rule:MF_01160}; OrderedLocusNames=STM4324;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL23147.1; -; Genomic_DNA.
DR RefSeq; NP_463188.1; NC_003197.2.
DR RefSeq; WP_000887832.1; NC_003197.2.
DR PDB; 3OPK; X-ray; 1.90 A; A/B/C=1-115.
DR PDBsum; 3OPK; -.
DR AlphaFoldDB; Q7CPA2; -.
DR SMR; Q7CPA2; -.
DR STRING; 99287.STM4324; -.
DR PaxDb; Q7CPA2; -.
DR EnsemblBacteria; AAL23147; AAL23147; STM4324.
DR GeneID; 1255850; -.
DR GeneID; 66758552; -.
DR KEGG; stm:STM4324; -.
DR PATRIC; fig|99287.12.peg.4549; -.
DR HOGENOM; CLU_098807_3_0_6; -.
DR OMA; VYTTFPD; -.
DR PhylomeDB; Q7CPA2; -.
DR BioCyc; SENT99287:STM4324-MON; -.
DR EvolutionaryTrace; Q7CPA2; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Copper; Cytoplasm; Metal-binding; Reference proteome.
FT CHAIN 1..115
FT /note="Divalent-cation tolerance protein CutA"
FT /id="PRO_0000157124"
FT BINDING 19
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT BINDING 86
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:3OPK"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:3OPK"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:3OPK"
FT STRAND 41..55
FT /evidence="ECO:0007829|PDB:3OPK"
FT STRAND 58..72
FT /evidence="ECO:0007829|PDB:3OPK"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3OPK"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:3OPK"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3OPK"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3OPK"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:3OPK"
SQ SEQUENCE 115 AA; 12681 MW; 468E359192E5E74B CRC64;
MLDVKSQDIS IPEAVVVLCT APDEATAQDL AAKVLAEKLA ACATLLPGAT SLYYWEGKLE
QEYEVQMILK TTVSHQQALI DCLKSHHPYQ TPELLVLPVT HGDTDYLSWL NASLR