ID   PCOC_ECOLX              Reviewed;         126 AA.
AC   Q47454;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Copper resistance protein C;
DE   Flags: Precursor;
GN   Name=pcoC;
OS   Escherichia coli.
OG   Plasmid pRJ1004.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8594334; DOI=10.1111/j.1365-2958.1995.mmi_17061153.x;
RA   Brown N.L., Barrett S.R., Camakaris J., Lee B.T.O., Rouch D.A.;
RT   "Molecular genetics and transport analysis of the copper-resistance
RT   determinant (pco) from Escherichia coli plasmid pRJ1004.";
RL   Mol. Microbiol. 17:1153-1166(1995).
CC   -!- FUNCTION: Required for the copper-inducible expression of copper
CC       resistance.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CopC family. {ECO:0000305}.
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DR   EMBL; X83541; CAA58527.1; -; Genomic_DNA.
DR   PIR; S70161; S52255.
DR   RefSeq; WP_000025662.1; NZ_WVVM01000015.1.
DR   PDB; 1IX2; X-ray; 1.55 A; A/B=23-126.
DR   PDB; 1LYQ; X-ray; 1.50 A; A/B=23-126.
DR   PDBsum; 1IX2; -.
DR   PDBsum; 1LYQ; -.
DR   AlphaFoldDB; Q47454; -.
DR   SMR; Q47454; -.
DR   DIP; DIP-16994N; -.
DR   STRING; 481805.EcolC_3414; -.
DR   GeneID; 61383277; -.
DR   GeneID; 64297918; -.
DR   GeneID; 67514215; -.
DR   eggNOG; COG2372; Bacteria.
DR   OMA; TEMPGMA; -.
DR   EvolutionaryTrace; Q47454; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0046688; P:response to copper ion; IEA:InterPro.
DR   Gene3D; 2.60.40.1220; -; 1.
DR   InterPro; IPR007348; CopC_dom.
DR   InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF04234; CopC; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Copper; Metal-binding; Periplasm; Plasmid; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..126
FT                   /note="Copper resistance protein C"
FT                   /id="PRO_0000006026"
FT   BINDING         24
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255"
FT   BINDING         115
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000255"
FT   STRAND          27..32
FT                   /evidence="ECO:0007829|PDB:1LYQ"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1LYQ"
FT   STRAND          44..50
FT                   /evidence="ECO:0007829|PDB:1LYQ"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:1LYQ"
FT   STRAND          58..66
FT                   /evidence="ECO:0007829|PDB:1LYQ"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:1IX2"
FT   STRAND          79..83
FT                   /evidence="ECO:0007829|PDB:1LYQ"
FT   STRAND          89..96
FT                   /evidence="ECO:0007829|PDB:1LYQ"
FT   STRAND          100..109
FT                   /evidence="ECO:0007829|PDB:1LYQ"
FT   STRAND          117..125
FT                   /evidence="ECO:0007829|PDB:1LYQ"
SQ   SEQUENCE   126 AA;  13256 MW;  A8C74B37F3489835 CRC64;
     MSILNKAILT GGLVMGVAFS AMAHPELKSS VPQADSAVAA PEKIQLNFSE NLTVKFSGAK
     LTMTGMKGMS SHSPMPVAAK VAPGADPKSM VIIPREPLPA GTYRVDWRAV SSDTHPITGN
     YTFTVK