PCOA_ECOLX
ID PCOA_ECOLX Reviewed; 605 AA.
AC Q47452;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Copper resistance protein A;
DE Flags: Precursor;
GN Name=pcoA;
OS Escherichia coli.
OG Plasmid pRJ1004.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8594334; DOI=10.1111/j.1365-2958.1995.mmi_17061153.x;
RA Brown N.L., Barrett S.R., Camakaris J., Lee B.T.O., Rouch D.A.;
RT "Molecular genetics and transport analysis of the copper-resistance
RT determinant (pco) from Escherichia coli plasmid pRJ1004.";
RL Mol. Microbiol. 17:1153-1166(1995).
CC -!- FUNCTION: Required for the copper-inducible expression of copper
CC resistance. May have oxidase activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CopA subfamily.
CC {ECO:0000305}.
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DR EMBL; X83541; CAA58525.1; -; Genomic_DNA.
DR PIR; S70159; S52253.
DR RefSeq; WP_000925242.1; NZ_WVVM01000015.1.
DR AlphaFoldDB; Q47452; -.
DR SMR; Q47452; -.
DR STRING; 481805.EcolC_3416; -.
DR GeneID; 61383275; -.
DR GeneID; 64297916; -.
DR GeneID; 67514213; -.
DR eggNOG; COG2132; Bacteria.
DR OMA; WNQMRMS; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd13848; CuRO_1_CopA; 1.
DR CDD; cd13874; CuRO_2_CopA; 1.
DR CDD; cd13896; CuRO_3_CopA; 1.
DR Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR006376; Cu-R_CopA.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR034284; CuRO_1_CopA.
DR InterPro; IPR034282; CuRO_2_CopA.
DR InterPro; IPR034279; CuRO_3_CopA.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR TIGRFAMs; TIGR01480; copper_res_A; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Copper; Metal-binding; Oxidoreductase; Periplasm; Plasmid; Repeat; Signal.
FT SIGNAL 1..41
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 42..605
FT /note="Copper resistance protein A"
FT /id="PRO_0000002950"
FT REPEAT 382..389
FT /note="1"
FT REPEAT 414..421
FT /note="2"
FT REPEAT 422..429
FT /note="3"
FT REGION 382..429
FT /note="3 X 8 AA tandem repeats of D-H-X-X-M-X-G-M"
FT BINDING 100
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 538
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000255"
FT BINDING 541
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000255"
FT BINDING 543
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000255"
FT BINDING 586
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000255"
FT BINDING 587
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000255"
FT BINDING 588
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000255"
FT BINDING 592
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000255"
FT BINDING 597
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000255"
SQ SEQUENCE 605 AA; 67307 MW; 8EECA182D56B27D8 CRC64;
MLLKTSRRTF LKGLTLSGVA GSLGVWSFNA RSSLSLPVAA SLQGTQFDLT IGETAVNITG
SERQAKTING GLPGPVLRWK EGDTITLKVK NRLNEQTSIH WHGIILPANM DGVPGLSFMG
IEPDDTYVYT FKVKQNGTYW YHSHSGLQEQ EGVYGAIIID AREPEPFAYD REHVVMLSDW
TDENPHSLLK KLKKQSDYYN FNKPTVGSFF RDVNTRGLSA TIADRKMWAE MKMNPTDLAD
VSGYTYTYLM NGQAPLKNWT GLFRPGEKIR LRFINGSAMT YFDIRIPGLK MTVVAADGQY
VNPVTVDEFR IAVAETYDVI VEPQGEAYTI FAQSMDRTGY ARGTLATREG LSAAVPPLDP
RPLLTMEDMG MGGMGHDMAG MDHSQMGGMD NSGEMMSMDG ADLPDSGTSS APMDHSSMAG
MDHSRMAGMP GMQSHPASET DNPLVDMQAM SVSPKLNDPG IGLRNNGRKV LTYADLKSRF
EDPDGREPGR TIELHLTGHM EKFAWSFNGI KFSDAAPVLL KYGERLRITL INDTMMTHPI
HLHGMWSDLE DENGNFMVRK HTIDVPPGTK RSYRVTADAL GRWAYHCHLL YHMEMGMFRE
VRVEE
