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COPK_CUPMC
ID   COPK_CUPMC              Reviewed;          94 AA.
AC   Q58AD3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Copper resistance protein K;
DE   Flags: Precursor;
GN   Name=copK; OrderedLocusNames=Rmet_6108;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OG   Plasmid pMOL30.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Monchy S., van der Lelie D., Vallaeys T., Taghavi S., Benotmane M.,
RA   McCorkle S., Dunn J., Lapidus A., Mergeay M.;
RT   "Sequence and features of the Ralstonia metallidurans CH34 heavy metals
RT   plasmids pMOL28 and pMOL30.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-38, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP   LOCATION, AND INDUCTION.
RX   PubMed=16735739; DOI=10.1099/mic.0.28593-0;
RA   Monchy S., Benotmane M.A., Wattiez R., van Aelst S., Auquier V.,
RA   Borremans B., Mergeay M., Taghavi S., van der Lelie D., Vallaeys T.;
RT   "Transcriptomic and proteomic analyses of the pMOL30-encoded copper
RT   resistance in Cupriavidus metallidurans strain CH34.";
RL   Microbiology 152:1765-1776(2006).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   CRYSTALLIZATION.
RX   PubMed=16511169; DOI=10.1107/s174430910502316x;
RA   Tricot C., van Aelst S., Wattiez R., Mergeay M., Stalon V., Wouters J.;
RT   "Overexpression, purification, crystallization and crystallographic
RT   analysis of CopK of Cupriavidus metallidurans.";
RL   Acta Crystallogr. F 61:825-827(2005).
RN   [5]
RP   STRUCTURE BY NMR OF 21-94, FUNCTION, SUBUNIT, INDUCTION, SUBCELLULAR
RP   LOCATION, AND MASS SPECTROMETRY.
RX   PubMed=18533181; DOI=10.1016/j.jmb.2008.05.017;
RA   Bersch B., Favier A., Schanda P., van Aelst S., Vallaeys T., Coves J.,
RA   Mergeay M., Wattiez R.;
RT   "Molecular structure and metal-binding properties of the periplasmic CopK
RT   protein expressed in Cupriavidus metallidurans CH34 during copper
RT   challenge.";
RL   J. Mol. Biol. 380:386-403(2008).
CC   -!- FUNCTION: Involved in resistance to copper. Can bind up to 2 copper
CC       ions. Has higher affinity for Cu(+) than for Cu(2+).
CC       {ECO:0000269|PubMed:18533181}.
CC   -!- SUBUNIT: Monomer in the copper-bound form. Homodimer as apoprotein.
CC       Dissociates into monomers upon copper binding.
CC       {ECO:0000269|PubMed:18533181}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16735739,
CC       ECO:0000269|PubMed:18533181}.
CC   -!- INDUCTION: By Cu(2+). Maximally expressed 30 minutes after induction
CC       with 0.4 mM copper. {ECO:0000269|PubMed:16735739,
CC       ECO:0000269|PubMed:18533181}.
CC   -!- MASS SPECTROMETRY: Mass=8279.58; Mass_error=0.06; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18533181};
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DR   EMBL; X71400; CAI11334.1; -; Genomic_DNA.
DR   EMBL; CP000354; ABF12967.1; -; Genomic_DNA.
DR   RefSeq; WP_008652571.1; NC_007971.2.
DR   RefSeq; YP_145685.1; NC_006466.1.
DR   PDB; 2K0Q; NMR; -; A=21-94.
DR   PDB; 2KM0; NMR; -; A=21-94.
DR   PDB; 2LEL; NMR; -; A=21-94.
DR   PDB; 3DSO; X-ray; 1.55 A; A=21-94.
DR   PDB; 3DSP; X-ray; 2.20 A; A=21-94.
DR   PDB; 3N7D; X-ray; 2.15 A; A/B=21-94.
DR   PDB; 3N7E; X-ray; 2.30 A; A/B=21-94.
DR   PDBsum; 2K0Q; -.
DR   PDBsum; 2KM0; -.
DR   PDBsum; 2LEL; -.
DR   PDBsum; 3DSO; -.
DR   PDBsum; 3DSP; -.
DR   PDBsum; 3N7D; -.
DR   PDBsum; 3N7E; -.
DR   AlphaFoldDB; Q58AD3; -.
DR   BMRB; Q58AD3; -.
DR   SMR; Q58AD3; -.
DR   EnsemblBacteria; ABF12967; ABF12967; Rmet_6108.
DR   KEGG; rme:Rmet_6108; -.
DR   HOGENOM; CLU_185099_0_0_4; -.
DR   OMA; DGQKIMM; -.
DR   OrthoDB; 2058115at2; -.
DR   EvolutionaryTrace; Q58AD3; -.
DR   Proteomes; UP000002429; Plasmid pMOL30.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.300; -; 1.
DR   InterPro; IPR021604; CopK.
DR   InterPro; IPR038644; CopK_sf.
DR   Pfam; PF11525; CopK; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Direct protein sequencing; Metal-binding; Periplasm;
KW   Plasmid; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:16735739"
FT   CHAIN           21..94
FT                   /note="Copper resistance protein K"
FT                   /id="PRO_0000344219"
FT   HELIX           23..25
FT                   /evidence="ECO:0007829|PDB:3DSO"
FT   STRAND          26..32
FT                   /evidence="ECO:0007829|PDB:3DSO"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:3DSO"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:3DSO"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:2LEL"
FT   STRAND          64..66
FT                   /evidence="ECO:0007829|PDB:3DSO"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:3DSO"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:3DSO"
FT   HELIX           84..87
FT                   /evidence="ECO:0007829|PDB:2K0Q"
FT   STRAND          90..92
FT                   /evidence="ECO:0007829|PDB:2LEL"
SQ   SEQUENCE   94 AA;  10269 MW;  0714E0E168DFFFE4 CRC64;
     MKQKLMVGAF IAAVSLSAAA VDMSNVVKTY DLQDGSKVHV FKDGKMGMEN KFGKSMNMPE
     GKVMETRDGT KIIMKGNEIF RLDEALRKGH SEGG
 
 
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