COPD_PSEUB
ID COPD_PSEUB Reviewed; 310 AA.
AC P12377;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Copper resistance protein D;
GN Name=copD;
OS Pseudomonas syringae pv. tomato.
OG Plasmid pPT23D.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=323;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3372485; DOI=10.1128/jb.170.6.2879-2883.1988;
RA Mellano M.A., Cooksey D.A.;
RT "Nucleotide sequence and organization of copper resistance genes from
RT Pseudomonas syringae pv. tomato.";
RL J. Bacteriol. 170:2879-2883(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-310.
RX PubMed=8449873; DOI=10.1128/jb.175.6.1656-1664.1993;
RA Mills S.D., Jasalavich C.A., Cooksey D.A.;
RT "A two-component regulatory system required for copper-inducible expression
RT of the copper resistance operon of Pseudomonas syringae.";
RL J. Bacteriol. 175:1656-1664(1993).
CC -!- FUNCTION: Exact function not known. Involved in copper resistance.
CC Appears to be involved in copper uptake in conjunction with CopC.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: By copper.
CC -!- SIMILARITY: Belongs to the CopD family. {ECO:0000305}.
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DR EMBL; M19930; AAA25809.1; -; Genomic_DNA.
DR EMBL; L05176; AAA25802.1; -; Genomic_DNA.
DR PIR; D32018; D32018.
DR RefSeq; WP_015062131.1; NZ_SNVE01000046.1.
DR AlphaFoldDB; P12377; -.
DR TCDB; 9.B.62.1.2; the copper resistance (copd) family.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006825; P:copper ion transport; IEA:InterPro.
DR InterPro; IPR032694; CopC/D.
DR InterPro; IPR008457; Cu-R_CopD.
DR PANTHER; PTHR34820; PTHR34820; 1.
DR Pfam; PF05425; CopD; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Copper; Membrane; Plasmid;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..310
FT /note="Copper resistance protein D"
FT /id="PRO_0000218124"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 310 AA; 33089 MW; 6B47AEDAE189B0E4 CRC64;
MEDPLSIAVR FALYTDLMML FGLALFGLYS LRGAERRSGA VLPFRPLLSA TALIGLLLSV
VSIVLMAKAM SGASEWLEAV PHAEMMVTQT ELGTAWLIRM AALVGAAVTI AFNLRVPMAS
LLMVSLLGGV ALATLAWTGH GAMDEGSRRF WHFSADILHL WSSGGWFGAL VAFALMLRPN
KVETLQSVQV LSRTLSGFER AGAVIVAFIV LSGVVNYLFI VGPQVSGVVE STYGVLLLGK
LALFGLMVGL ASANRFVLSP AFERAVHRGE YARAARSIRY SMALELGAAV LVLGLIAWLG
TLSPEMEAGM