CUTA_SHIFL
ID CUTA_SHIFL Reviewed; 112 AA.
AC Q83P43; Q7UAM2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Divalent-cation tolerance protein CutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN Name=cutA {ECO:0000255|HAMAP-Rule:MF_01160};
GN OrderedLocusNames=SF4291, S4558;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN45709.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP19495.1; -; Genomic_DNA.
DR RefSeq; NP_710002.2; NC_004337.2.
DR RefSeq; WP_000883409.1; NZ_WPGW01000108.1.
DR AlphaFoldDB; Q83P43; -.
DR SMR; Q83P43; -.
DR STRING; 198214.SF4291; -.
DR EnsemblBacteria; AAN45709; AAN45709; SF4291.
DR EnsemblBacteria; AAP19495; AAP19495; S4558.
DR GeneID; 1027771; -.
DR KEGG; sfl:SF4291; -.
DR KEGG; sft:NCTC1_04660; -.
DR KEGG; sfx:S4558; -.
DR PATRIC; fig|198214.7.peg.5061; -.
DR HOGENOM; CLU_098807_3_0_6; -.
DR OMA; VYTTFPD; -.
DR OrthoDB; 1801957at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome.
FT CHAIN 1..112
FT /note="Divalent-cation tolerance protein CutA"
FT /id="PRO_0000157125"
FT BINDING 16
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT BINDING 83
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
FT BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01160"
SQ SEQUENCE 112 AA; 12361 MW; D02145EF103CC6C2 CRC64;
MLDEKSSNTT SVVVLCTAPD EATAQDLAAK VLAEKLAACA TLIPGATSLY YWEGKLEQEY
EVQMILKTTV SHQQALLECL KSHHPYQTPE LLVLPVTHGD TDYLSWLNAS LR