ID A5UXC7_ROSS1 Unreviewed; 197 AA.
AC A5UXC7;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:ABQ91280.1};
GN OrderedLocusNames=RoseRS_2912 {ECO:0000313|EMBL:ABQ91280.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ91280.1, ECO:0000313|Proteomes:UP000006554};
RN [1] {ECO:0000313|Proteomes:UP000006554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) 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; CP000686; ABQ91280.1; -; Genomic_DNA.
DR RefSeq; WP_011957624.1; NC_009523.1.
DR AlphaFoldDB; A5UXC7; -.
DR STRING; 357808.RoseRS_2912; -.
DR KEGG; rrs:RoseRS_2912; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_3_0_0; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000006554; Chromosome.
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; 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}.
FT DOMAIN 30..193
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 68
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 72
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 158
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 68..72
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 197 AA; 22049 MW; ABF6F48D1612A2EA CRC64;
MLRGFRVFVL LALVTVVSAC GRYEFRGVTL DPPKEAPDFT LTDFDGKPFR LSEQRGKIVI
LFFGFTNCPD MCPAALSDMA AARRKLGADA EKVQGVFVSL DPDRDTPERL KRYVTAFDPT
FIGLRGSEAE LSPVMQDYGV TSIRRELPDS ALKYTIDHST FIYVIDATGR WRLLFTHGMP
VDDIVSDLRY LVRQGGA
//
