COPC_PSEUB
ID COPC_PSEUB Reviewed; 126 AA.
AC P12376;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Copper resistance protein C;
DE Flags: Precursor;
GN Name=copC;
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 CHARACTERIZATION, AND PROTEIN SEQUENCE OF 25-29.
RC STRAIN=PT23.2;
RX PubMed=1924351; DOI=10.1073/pnas.88.20.8915;
RA Cha J.-S., Cooksey D.A.;
RT "Copper resistance in Pseudomonas syringae mediated by periplasmic and
RT outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:8915-8919(1991).
CC -!- FUNCTION: Mediates copper resistance by sequestration of copper in the
CC periplasm along with the copper-binding protein CopA.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: By copper.
CC -!- SIMILARITY: Belongs to the CopC family. {ECO:0000305}.
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DR EMBL; M19930; AAA25808.1; -; Genomic_DNA.
DR PIR; C32018; C32018.
DR RefSeq; WP_003317555.1; NZ_SNVE01000046.1.
DR PDB; 1M42; NMR; -; A=25-126.
DR PDB; 1NM4; NMR; -; A=25-126.
DR PDB; 1OT4; NMR; -; A=25-126.
DR PDB; 2C9P; X-ray; 2.25 A; A/B/C=25-126.
DR PDB; 2C9Q; X-ray; 1.60 A; A=25-126.
DR PDB; 2C9R; X-ray; 2.00 A; A=25-126.
DR PDBsum; 1M42; -.
DR PDBsum; 1NM4; -.
DR PDBsum; 1OT4; -.
DR PDBsum; 2C9P; -.
DR PDBsum; 2C9Q; -.
DR PDBsum; 2C9R; -.
DR AlphaFoldDB; P12376; -.
DR SMR; P12376; -.
DR EvolutionaryTrace; P12376; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0006825; P:copper ion transport; IEA:InterPro.
DR GO; GO:0046688; P:response to copper ion; IEA:InterPro.
DR Gene3D; 2.60.40.1220; -; 1.
DR InterPro; IPR032694; CopC/D.
DR InterPro; IPR007348; CopC_dom.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR34820; PTHR34820; 1.
DR Pfam; PF04234; CopC; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Metal-binding; Periplasm;
KW Plasmid; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:1924351"
FT CHAIN 25..126
FT /note="Copper resistance protein C"
FT /id="PRO_0000006025"
FT BINDING 25
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 28..33
FT /evidence="ECO:0007829|PDB:2C9Q"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2C9Q"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:2C9Q"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:2C9Q"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:2C9Q"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:2C9Q"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2C9Q"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:2C9Q"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:2C9Q"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:2C9Q"
SQ SEQUENCE 126 AA; 13042 MW; 132CBB3347EEE4D5 CRC64;
MLLNRTSFVT LFAAGMLVSA LAQAHPKLVS STPAEGSEGA APAKIELHFS ENLVTQFSGA
KLVMTAMPGM EHSPMAVKAA VSGGGDPKTM VITPASPLTA GTYKVDWRAV SSDTHPITGS
VTFKVK
