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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
 
 
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