9.B.62 The Copper Resistance (CopD) Family

The CopD family consists of many homologues with 8 putative TMSs and sizes of about 300 residues from Gram-negative and Gram-positive bacteria. Some homologues from Gram-positive bacteria are larger (Listeria monocytogenes, 541 aas; Corynebacterium efficiens, 356 aas; Streptomyces coelicolor, 680 aas). Some of these proteins are multidomain proteins with extra soluble or membrane integrated domains of unknown function.

The E. coli homologue, PcoD, present in an operon (pcoABCDRS), has been characterized from plasmid pRJ1004 (Brown et al., 1995). It is homologous to the CopD protein of Pseudomonas syringae pv. tomato. The proteins in this operon appear to catalyze copper efflux in the logarithmic growth phase but allow accumulation in stationary phase (Brown et al., 1995). Other constituents present in the outer membrane (PcoB) and in the periplasm (PcoA and C) may be involved (Lee et al., 2002; Silver and Ji, 1994). Transcription of pco/cop operons may be controlled by two-component systems such as the PcoS/PcoR sensor kinase/response regulator system. The mechanism of copper resistance is not known but may involve either (1) copper efflux, (2) copper uptake plus periplasmic copper sequestration by CopA and CopC, or (3) copper uptake by a two component CopD-CopC system coupled to an unknown resistance mechanism.



This family belongs to the Copper Resistance Superfamily.

 

References:

Brown, N.L., S.R. Barrett, J. Camakaris, B.T. Lee, and D.A. Rouch. (1995). Molecular genetics and transport analysis of the copper-resistance determinant (pco) from Escherichia coli plasmid pRJ1004. Mol. Microbiol. 17: 1153-1166.

Lee, S.M., G. Grass, C. Rensing, S.R. Barrett, C.J.D. Yates, J.V. Stoyanov, and N.L. Brown. (2002). The Pco proteins are involved in periplasmic copper handling in Escherichia coli. Biochem. Biophys. Res. Commun. 295: 616-620.

Mills, S.D., C.A. Jasalavich, and D.A. Cooksey. (1993). A two-component regulatory system required for copper-inducible expression of the copper resistance operon of Pseudomonas syringae. J. Bacteriol. 175: 1656-1664.

Rehan, M., T. Furnholm, R.H. Finethy, F. Chu, G. El-Fadly, and L.S. Tisa. (2014). Copper tolerance in Frankia sp. strain EuI1c involves surface binding and copper transport. Appl. Microbiol. Biotechnol. 98: 8005-8015.

Silver, S. and G. Ji. (1994). Newer systems for bacterial resistances to toxic heavy metals. Environ Health Perspect 102Suppl3: 107-113.

Examples:

TC#NameOrganismal TypeExample
9.B.62.1.1

The PcoD copper resistance protein of 309 aas and 8 TMSs.

Gram-negative bacteriaPcoD of E. coli (S52256)
 
9.B.62.1.2

The CopD copper resistance protein of 310 aas and 8 TMSs.

Gram-negative bacteriaCopD of Pseudomonas syringae (P12377)
 
9.B.62.1.3

CopD homologue of 296 aas and 8 TMSs

Proteobacteria

CopD of Roseomonas cervicalis

 
9.B.62.1.4

Uncharacterized membrane protein of 290 aas and 8 TMSs, YebZ.

YebZ of E. coli

 
9.B.62.1.5

Copper (Cu2+) resistance system, CopC (high affinity periplasmic Cu2+ binding protein of 122 aas)/CopD (membrane protein of 291 aas and 8 TMSs) (Wijekoon et al. 2015).  May function with the periplasmic CopA protein and the outer membrane porin, CopB (see TC# 1.B.76.1.6).

CopCD of Pseudomonas fluorescens

 
Examples:

TC#NameOrganismal TypeExample
9.B.62.2.1

Copper resistance protein, CopC of 559 aas and 10 TMS in a 1 + 9 TMS arrangement.

Actinobacteria

CopC of Frankia sp.

 
9.B.62.2.2

Copper resistance protein CopCD of 551 aas and 9 TMSs

Actinobacteria

CopCD of Frankia symbiont subsp. Datisca glomerata

 
9.B.62.2.3
Copper resistance D domain protein, CopD of 410 aas and 9 TMSs; may function with the periplasmic CopC copper binding protein (Rehan et al. 2014).

Actinobacteria

CopCD of Frankia sp. strain EuI1c

 
9.B.62.2.4

CopCD of 659 aas and 8 TMSs.

Euryarchaea

CopCD of Natronomonas pharaonis

 
9.B.62.2.5

CopD homologue of 311 aas and 8 TMSs.

Proteobacteria

CopD of Acidiphilium multivorum

 
9.B.62.2.6

Uncharacterized protein of 157 aas and 4 TMSs.

Proteobacteria

UP of Tistrella mobilis

 
Examples:

TC#NameOrganismal TypeExample
9.B.62.3.1

Copper resistance protein, CopD of 736 aas and 16 TMSs in an apparent 8 + 8 TMS arrangement.

Actinobacteria

CopD of Frankia sp.

 
9.B.62.3.2

This protein has a cytochrome c oxidase caa3-type, assembly factor CtaG-related C-terminal protein domain (~475 - 725 aas) with an N-terminal CopD/PcoD copper sequestering domain (~150 - 375 aas). The protein is of 767 aas with 16 TMSs.

Actinobacteria

CtaG of Frankia sp.

 
9.B.62.3.3

Putative copper transporter of 249 aas.

Deinococcus/Thermus

Putative copper transporter of Deinococcus radiodurans

 
9.B.62.3.4

Putative copper transporter of 176 aas and 4 TMSs.

Actinobacteria

Putative copper transporter of Rhodococcus ruber

 
9.B.62.3.5

Uncharacterized protein of 223 aas and 5 TMSs

Planctomycetes

UP of Rhodopirellula baltica

 
9.B.62.3.6

CopD of 321 aas and 9 TMSs.

Actinobacteria

CopD of Mycobacterium smegmatis

 
9.B.62.3.7

CopD of 270 aas and 7 TMSs.

Actinobacteria

copD of Tsukamurella paurometabola

 
9.B.62.3.8

Uncharacterized protein of 191 aas and 6 TMSs

UP of Sagittula stellata

 
Examples:

TC#NameOrganismal TypeExample
9.B.62.4.1

Uncharacterized protein of 303 aas and 7 TMSs

Chloroflexi

UP of Caldilinea aerophila

 
Examples:

TC#NameOrganismal TypeExample
9.B.62.5.1

Uncharacterized protein of 150 aas and 4 TMSs

Aquificae

UP of Hydrogenobacter thermophilus

 
9.B.62.5.2

Uncharacterized protein of 183 aas and 4 TMSs.

Proteobacteria

UP of Komagataeibacter hansenii (Gluconacetobacter hansenii)

 
9.B.62.5.3

Uncharacterized protein of 153 aas and 3 TMSs

Euryarchaea

UP of Halomicrobium mukohataei (Haloarcula mukohataei)

 
Examples:

TC#NameOrganismal TypeExample