CUTA_THEMA
ID CUTA_THEMA Reviewed; 101 AA.
AC Q9X0E6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Divalent-cation tolerance protein CutA;
GN Name=cutA; OrderedLocusNames=TM_1056;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX PubMed=14705033; DOI=10.1002/prot.10585;
RA Savchenko A., Skarina T., Evdokimova E., Watson J.D., Laskowski R.,
RA Arrowsmith C.H., Edwards A.M., Joachimiak A., Zhang R.-G.;
RT "X-ray crystal structure of CutA from Thermotoga maritima at 1.4 A
RT resolution.";
RL Proteins 54:162-165(2004).
CC -!- FUNCTION: Involved in resistance toward heavy metals. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the CutA family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36133.1; -; Genomic_DNA.
DR PIR; B72302; B72302.
DR RefSeq; NP_228862.1; NC_000853.1.
DR RefSeq; WP_004080448.1; NZ_CP011107.1.
DR PDB; 1KR4; X-ray; 1.40 A; A=1-101.
DR PDB; 1O5J; X-ray; 1.95 A; A=1-101.
DR PDB; 1VHF; X-ray; 1.54 A; A=2-101.
DR PDBsum; 1KR4; -.
DR PDBsum; 1O5J; -.
DR PDBsum; 1VHF; -.
DR AlphaFoldDB; Q9X0E6; -.
DR SMR; Q9X0E6; -.
DR STRING; 243274.THEMA_09080; -.
DR EnsemblBacteria; AAD36133; AAD36133; TM_1056.
DR KEGG; tma:TM1056; -.
DR eggNOG; COG1324; Bacteria.
DR InParanoid; Q9X0E6; -.
DR OMA; VYTTFPD; -.
DR OrthoDB; 1801957at2; -.
DR EvolutionaryTrace; Q9X0E6; -.
DR Proteomes; UP000008183; 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 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; Cytoplasm; Reference proteome.
FT CHAIN 1..101
FT /note="Divalent-cation tolerance protein CutA"
FT /id="PRO_0000157131"
FT STRAND 1..10
FT /evidence="ECO:0007829|PDB:1KR4"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:1KR4"
FT STRAND 28..41
FT /evidence="ECO:0007829|PDB:1KR4"
FT STRAND 44..58
FT /evidence="ECO:0007829|PDB:1KR4"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1KR4"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:1KR4"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1KR4"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1KR4"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:1KR4"
SQ SEQUENCE 101 AA; 12177 MW; DB2039392BC83777 CRC64;
MILVYSTFPN EEKALEIGRK LLEKRLIACF NAFEIRSGYW WKGEIVQDKE WAAIFKTTEE
KEKELYEELR KLHPYETPAI FTLKVENVLT EYMNWLRESV L
