ID G4M997_9BURK Unreviewed; 196 AA.
AC G4M997;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Cytochrome oxidase biogenesis protein Sco1/SenC/PrrC, putative copper metallochaperone {ECO:0000313|EMBL:CCD37726.1};
GN ORFNames=BKIR_c2_4701 {ECO:0000313|EMBL:CCD37726.1};
OS Candidatus Paraburkholderia kirkii UZHbot1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1055526 {ECO:0000313|EMBL:CCD37726.1, ECO:0000313|Proteomes:UP000003511};
RN [1] {ECO:0000313|EMBL:CCD37726.1, ECO:0000313|Proteomes:UP000003511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD37726.1,
RC ECO:0000313|Proteomes:UP000003511};
RA Carlier A.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCD37726.1, ECO:0000313|Proteomes:UP000003511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD37726.1,
RC ECO:0000313|Proteomes:UP000003511};
RA Carlier A.L., Eberl L.;
RT "Draft genome sequence of Candidatus Burkholderia kirkii.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCD37726.1}.
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DR EMBL; CAFE01000117; CCD37726.1; -; Genomic_DNA.
DR AlphaFoldDB; G4M997; -.
DR STRING; 1055526.BKIR_c2_4701; -.
DR HOGENOM; CLU_050131_3_0_4; -.
DR BioCyc; CBUR1055526:G10QW-210-MONOMER; -.
DR Proteomes; UP000003511; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02968; SCO; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003782; SCO1/SenC.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 1.
DR PANTHER; PTHR12151:SF27; PUTATIVE-RELATED; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003511};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..196
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003465231"
FT DOMAIN 18..196
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 71
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 71..75
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 196 AA; 21617 MW; AF973F8067A1AEB2 CRC64;
MTTVLRRLLA LLVFAALLSA CEKAPDFKNL DITGNKQFGS DFSLPDTQGK TRTLADFKGK
AVVLFFGYTH CPDVCPTTLA ELSQAMQPLG DKSKDVQVLM VTVDPARDTP ELLGQYVAAF
NSSYIGLRPA NDAQLAQLAK DFRVYYAKST GKTPDDYTMD HTAASYVFDK DGKLRLFARD
GQGVEPWVHD LKLLID
//
