COPR_PSEUB
ID COPR_PSEUB Reviewed; 227 AA.
AC Q02540;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Transcriptional activator protein CopR;
GN Name=copR;
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=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).
RN [2]
RP PROTEIN SEQUENCE OF 1-8, AND CHARACTERIZATION.
RX PubMed=8078459; DOI=10.1007/bf00286685;
RA Mills S.D., Lim C.-K., Cooksey D.A.;
RT "Purification and characterization of CopR, a transcriptional activator
RT protein that binds to a conserved domain (cop box) in copper-inducible
RT promoters of Pseudomonas syringae.";
RL Mol. Gen. Genet. 244:341-351(1994).
CC -!- FUNCTION: Member of the two-component regulatory system CopS/CopR.
CC Involved in the activation of copper resistance gene operon CopABCD.
CC Phosphorylation of CopR by CopS would convert it into an active state
CC to induce expression of the cop operon by binding to a specific site on
CC the cop operon promoter (cop box) and possibly by facilitating the
CC binding of RNA polymerase to the cop promoter. CopR also binds to the
CC chromosomally encoded cop operon promoter. May also be involved in
CC basic copper metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by CopS. {ECO:0000305}.
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DR EMBL; L05176; AAA25803.1; -; Genomic_DNA.
DR PIR; B47080; B47080.
DR RefSeq; WP_015062132.1; NZ_SNVE01000046.1.
DR AlphaFoldDB; Q02540; -.
DR SMR; Q02540; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR006291; PcoR.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR TIGRFAMs; TIGR01387; cztR_silR_copR; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW Activator; Copper; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Phosphoprotein; Plasmid; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..227
FT /note="Transcriptional activator protein CopR"
FT /id="PRO_0000081076"
FT DOMAIN 2..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 125..223
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 51
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 227 AA; 25470 MW; EB505F0BD8A9F13B CRC64;
MKLLVAEDEP KTGIYLQQGL REAGFNVDRV VTGTDAVDQA LNEAYDLLIL DVMMPGLDGW
EVIRRLRTAG QPVPVLFLTA RDGVDDRVKG LELGADDYLV KPFALSELLA RVRTLLRRGS
SLQVQTSLQI GDLQVDLLKR RATRGGKRIE LTAKEFALLE LLMRRQGEVL SKSLIASQVW
DMNFDSDTNV IEVAIRRLRA KIDDDFEVKL LHTCRGMGYM LEAQDEG