ID   A0A1T5B4V9_9GAMM        Unreviewed;       205 AA.
AC   A0A1T5B4V9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Protein SCO1/2 {ECO:0000313|EMBL:SKB42256.1};
GN   ORFNames=SAMN05660880_00968 {ECO:0000313|EMBL:SKB42256.1};
OS   Luteibacter sp. 22Crub2.1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1283288 {ECO:0000313|EMBL:SKB42256.1, ECO:0000313|Proteomes:UP000191150};
RN   [1] {ECO:0000313|EMBL:SKB42256.1, ECO:0000313|Proteomes:UP000191150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22Crub2.1 {ECO:0000313|EMBL:SKB42256.1,
RC   ECO:0000313|Proteomes:UP000191150};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SCO1/2 family.
CC       {ECO:0000256|ARBA:ARBA00010996}.
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DR   EMBL; FUYT01000004; SKB42256.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5B4V9; -.
DR   Proteomes; UP000191150; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..205
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010574618"
FT   DOMAIN          36..203
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   BINDING         76
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         80
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         165
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        76..80
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   205 AA;  22489 MW;  19B26861C2C91D44 CRC64;
     MKPFLARRVL LTLLALVSLA ALSACQHEPQ PEWRLNDVSG HLPDLDFRLT DDNGKAVTGA
     DYRGKVTLMY FGYTHCPDVC PLTLTQLHVV LGRLGPAADK VRILFVSVDP ARDTPQIMHD
     YVNAFDKHAV GLVGSDADVE ALAKRYRSAF TREPDKGDGA YDVSHSSAIY FFDAQGKARL
     LATPSASQDD MVHDLTLLTS LEPHA
//