MT_SYNE7
ID MT_SYNE7 Reviewed; 56 AA.
AC P30331; Q31NP9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Metallothionein;
DE Short=MT;
GN Name=smtA; OrderedLocusNames=Synpcc7942_1290;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8446025; DOI=10.1111/j.1365-2958.1993.tb01109.x;
RA Huckle J.W., Morby A.P., Turner J.S., Robinson N.J.;
RT "Isolation of a prokaryotic metallothionein locus and analysis of
RT transcriptional control by trace metal ions.";
RL Mol. Microbiol. 7:177-187(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP CHARACTERIZATION.
RX PubMed=1607014; DOI=10.1016/0014-5793(92)80509-f;
RA Shi J., Lindsay W.P., Huckle J.W., Morby A.P., Robinson N.J.;
RT "Cyanobacterial metallothionein gene expressed in Escherichia coli. Metal-
RT binding properties of the expressed protein.";
RL FEBS Lett. 303:159-163(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:1JJD}
RP STRUCTURE BY NMR OF 2-56 IN COMPLEX WITH ZINC.
RX PubMed=11493688; DOI=10.1073/pnas.171120098;
RA Blindauer C.A., Harrison M.D., Parkinson J.A., Robinson A.K., Cavet J.S.,
RA Robinson N.J., Sadler P.J.;
RT "A metallothionein containing a zinc finger within a four-metal cluster
RT protects a bacterium from zinc toxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9593-9598(2001).
CC -!- FUNCTION: May play a role in essential metal ion homeostasis
CC (especially zinc homeostasis) and resistance to certain non-essential
CC metal ions. Binds four zinc ions (PubMed:11493688).
CC {ECO:0000269|PubMed:11493688}.
CC -!- INDUCTION: Upon exposure to a range of metals, particularly cadmium,
CC zinc, copper and mercury.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 14 family.
CC {ECO:0000305}.
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DR EMBL; X64585; CAA45873.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB57320.1; -; Genomic_DNA.
DR PIR; S31198; S31198.
DR RefSeq; WP_011377964.1; NC_007604.1.
DR PDB; 1JJD; NMR; -; A=2-56.
DR PDBsum; 1JJD; -.
DR AlphaFoldDB; P30331; -.
DR SMR; P30331; -.
DR STRING; 1140.Synpcc7942_1290; -.
DR PRIDE; P30331; -.
DR EnsemblBacteria; ABB57320; ABB57320; Synpcc7942_1290.
DR KEGG; syf:Synpcc7942_1290; -.
DR eggNOG; ENOG50330JR; Bacteria.
DR HOGENOM; CLU_192999_1_0_3; -.
DR OMA; TQMKCAC; -.
DR OrthoDB; 2014524at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1290-MON; -.
DR EvolutionaryTrace; P30331; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017854; Metalthion_dom_sf.
DR InterPro; IPR000518; Metalthion_fam14_prok.
DR Pfam; PF02069; Metallothio_Pro; 1.
DR PRINTS; PR00859; MTPROKARYOTE.
DR SUPFAM; SSF57868; SSF57868; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cadmium; Copper; Direct protein sequencing; Mercury;
KW Metal-binding; Metal-thiolate cluster; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..56
FT /note="Metallothionein"
FT /id="PRO_0000197371"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT BINDING 54
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:11493688,
FT ECO:0007744|PDB:1JJD"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:1JJD"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1JJD"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1JJD"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:1JJD"
SQ SEQUENCE 56 AA; 5741 MW; E76846D6086F2524 CRC64;
MTSTTLVKCA CEPCLCNVDP SKAIDRNGLY YCSEACADGH TGGSKGCGHT GCNCHG
