ID A0A059KLX0_9BURK Unreviewed; 227 AA.
AC A0A059KLX0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:KDB52467.1};
GN ORFNames=X805_19180 {ECO:0000313|EMBL:KDB52467.1};
OS Sphaerotilus natans subsp. natans DSM 6575.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Sphaerotilus.
OX NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB52467.1, ECO:0000313|Proteomes:UP000026714};
RN [1] {ECO:0000313|EMBL:KDB52467.1, ECO:0000313|Proteomes:UP000026714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB52467.1,
RC ECO:0000313|Proteomes:UP000026714};
RX PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA Park S., Kim D.H., Lee J.H., Hur H.G.;
RT "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL FEMS Microbiol. Ecol. 90:68-77(2014).
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:KDB52467.1}.
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DR EMBL; AZRA01000049; KDB52467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059KLX0; -.
DR STRING; 34103.SAMN05421778_11690; -.
DR PATRIC; fig|1286631.3.peg.1885; -.
DR eggNOG; COG1999; Bacteria.
DR Proteomes; UP000026714; 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; IPR006311; TAT_signal.
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; PS51318; TAT; 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 61..224
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 100
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 104
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 189
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 100..104
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 227 AA; 24288 MW; 4A35332D716BED51 CRC64;
MTATSDRRPE QHALPSSPCS SRRRLLRRAP AALALLGTAG GALLAGCERS ASPIAFKSLD
ITGADYARQL ALTDARTEQP FLLSNLKGKI AVVFFGFTQC PDVCPTTLGA LAETRQLLGA
EGDKLVGVFV TVDPKRDTAA LMKAYVGSFS PDWVPLRGSA DEVAAAAKEF KIFYREVPGK
TESSYTIDHT AASYVFDTQG QVRLYVRHNT PPADLAADIR TLLAQAG
//
