ID L7CNJ7_RHOBT Unreviewed; 208 AA.
AC L7CNJ7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Copper chaperone SCO1/SenC {ECO:0000313|EMBL:ELP35864.1};
GN ORFNames=RBSWK_00271 {ECO:0000313|EMBL:ELP35864.1};
OS Rhodopirellula baltica SWK14.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=993516 {ECO:0000313|EMBL:ELP35864.1, ECO:0000313|Proteomes:UP000010959};
RN [1] {ECO:0000313|EMBL:ELP35864.1, ECO:0000313|Proteomes:UP000010959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWK14 {ECO:0000313|EMBL:ELP35864.1,
RC ECO:0000313|Proteomes:UP000010959};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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:ELP35864.1}.
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DR EMBL; AMWG01000006; ELP35864.1; -; Genomic_DNA.
DR AlphaFoldDB; L7CNJ7; -.
DR PATRIC; fig|993516.3.peg.295; -.
DR Proteomes; UP000010959; 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:SF25; SCO1 PROTEIN HOMOLOG; 1.
DR Pfam; PF02630; SCO1-SenC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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}.
FT DOMAIN 30..200
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 86
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 163
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 82..86
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 208 AA; 23438 MW; A9EF0068208BEDD4 CRC64;
MRHSTAPSDG PGPDEVIYGN DNAVVDNATL RPEDVANDTP SKPPEDAEWL SEFELLERSG
EMVSTADLKG APYVVSFFFS TCPSICVSQN QKLKELQDEF EGQGVRFVAI SVDPENDTPE
VLREYAARFG ADPDQWLFLT GELNYIRRIG AEIFQQPVNK QFHTERFVLV DPDGKIEGFY
NWPEKRQLEA LKESIESMLQ EEASSKKS
//
