CUTA_PYRHO
ID CUTA_PYRHO Reviewed; 102 AA.
AC O58720;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Divalent-cation tolerance protein CutA;
GN Name=cutA; OrderedLocusNames=PH0992;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=15351719; DOI=10.1016/j.bbrc.2004.08.081;
RA Tanaka Y., Tsumoto K., Umetsu M., Nakanishi T., Yasutake Y., Sakai N.,
RA Yao M., Tanaka I., Arakawa T., Kumagai I.;
RT "Structural evidence for guanidine-protein side chain interactions: crystal
RT structure of CutA from Pyrococcus horikoshii in 3 M guanidine
RT hydrochloride.";
RL Biochem. Biophys. Res. Commun. 323:185-191(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RX PubMed=14706845; DOI=10.1016/s0014-5793(03)01402-9;
RA Tanaka Y., Tsumoto K., Nakanishi T., Yasutake Y., Sakai N., Yao M.,
RA Tanaka I., Kumagai I.;
RT "Structural implications for heavy metal-induced reversible assembly and
RT aggregation of a protein: the case of Pyrococcus horikoshii CutA.";
RL FEBS Lett. 556:167-174(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=14741340; DOI=10.1016/s0014-5793(03)01441-8;
RA Umetsu M., Tsumoto K., Ashish K., Nitta S., Tanaka Y., Adschiri T.,
RA Kumagai I.;
RT "Structural characteristics and refolding of in vivo aggregated
RT hyperthermophilic archaeon proteins.";
RL FEBS Lett. 557:49-56(2004).
CC -!- FUNCTION: Involved in resistance toward heavy metals.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000305};
CC Note=Binds 1 copper ion in the interface between two trimers.
CC {ECO:0000305};
CC -!- SUBUNIT: Homotrimer. The binding of the copper ion probably leads to
CC oligomerization.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the CutA family. {ECO:0000305}.
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DR EMBL; BA000001; BAA30089.1; -; Genomic_DNA.
DR PIR; C71091; C71091.
DR RefSeq; WP_010885081.1; NC_000961.1.
DR PDB; 1J2V; X-ray; 2.00 A; A=1-102.
DR PDB; 1UKU; X-ray; 1.45 A; A=1-102.
DR PDB; 1UMJ; X-ray; 1.60 A; A/B=1-102.
DR PDB; 2E66; X-ray; 2.00 A; A/B/C=1-102.
DR PDB; 4NYO; X-ray; 1.80 A; A/B/C/D/E/F=1-102.
DR PDB; 4NYP; X-ray; 2.00 A; A/B/C/D/E/F=1-102.
DR PDBsum; 1J2V; -.
DR PDBsum; 1UKU; -.
DR PDBsum; 1UMJ; -.
DR PDBsum; 2E66; -.
DR PDBsum; 4NYO; -.
DR PDBsum; 4NYP; -.
DR AlphaFoldDB; O58720; -.
DR SMR; O58720; -.
DR STRING; 70601.3257406; -.
DR EnsemblBacteria; BAA30089; BAA30089; BAA30089.
DR GeneID; 1443316; -.
DR KEGG; pho:PH0992; -.
DR eggNOG; arCOG04231; Archaea.
DR OMA; VYTTFPD; -.
DR OrthoDB; 110178at2157; -.
DR EvolutionaryTrace; O58720; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Copper; Cytoplasm; Metal-binding.
FT CHAIN 1..102
FT /note="Divalent-cation tolerance protein CutA"
FT /id="PRO_0000157129"
FT BINDING 48
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1UKU"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:1UKU"
FT STRAND 28..41
FT /evidence="ECO:0007829|PDB:1UKU"
FT STRAND 44..57
FT /evidence="ECO:0007829|PDB:1UKU"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1UKU"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:1UKU"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1UKU"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1UKU"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4NYO"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:1UKU"
SQ SEQUENCE 102 AA; 12348 MW; DC17341ECFDD8401 CRC64;
MIIVYTTFPD WESAEKVVKT LLKERLIACA NLREHRAFYW WEGKIEEDKE VGAILKTRED
LWEELKERIK ELHPYDVPAI IRIDVDDVNE DYLKWLIEET KK
