ID A9WGD0_CHLAA Unreviewed; 197 AA.
AC A9WGD0;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:ABY34051.1};
GN OrderedLocusNames=Caur_0813 {ECO:0000313|EMBL:ABY34051.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY34051.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; CP000909; ABY34051.1; -; Genomic_DNA.
DR RefSeq; WP_012256707.1; NC_010175.1.
DR RefSeq; YP_001634440.1; NC_010175.1.
DR AlphaFoldDB; A9WGD0; -.
DR STRING; 324602.Caur_0813; -.
DR EnsemblBacteria; ABY34051; ABY34051; Caur_0813.
DR KEGG; cau:Caur_0813; -.
DR PATRIC; fig|324602.8.peg.927; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_3_0_0; -.
DR InParanoid; A9WGD0; -.
DR Proteomes; UP000002008; 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; 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:UP000002008};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..197
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002743981"
FT DOMAIN 31..197
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 69
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 73
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 159
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 69..73
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 197 AA; 21881 MW; C3D3AFE25C8782E1 CRC64;
MRRFLFICWI VMICTACSAV SPPGTTTATI IDPPTVLSDF QLPASTGHDL RLSDLRGQPV
LLYFGYTRCP DYCPITLSEF RRTREQLGAD GEKVHFVLIS VDPAHDTPEV LAAYLRGFGE
GFIGLQGDDA TLRRISKEYG LTYRHGGGHQ QHGDAGVEHS TASYLIDQNG RLRIVYQYGT
AANVYVQDIR DLLKEAQ
//
