ID D1C5G1_SPHTD Unreviewed; 232 AA.
AC D1C5G1;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:ACZ37477.1};
GN OrderedLocusNames=Sthe_0038 {ECO:0000313|EMBL:ACZ37477.1};
OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales;
OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter.
OX NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ37477.1, ECO:0000313|Proteomes:UP000002027};
RN [1] {ECO:0000313|Proteomes:UP000002027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC {ECO:0000313|Proteomes:UP000002027};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F.,
RA Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R.,
RA Goeker M., Klenk H.P., Eisen J.A.;
RT "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ37477.1, ECO:0000313|Proteomes:UP000002027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49802 / DSM 20745 / S 6022
RC {ECO:0000313|Proteomes:UP000002027};
RX PubMed=21304676;
RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C.,
RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Desulfohalobium retbaense type strain
RT (HR(100)).";
RL Stand. Genomic Sci. 2:38-48(2010).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; CP001823; ACZ37477.1; -; Genomic_DNA.
DR RefSeq; WP_012870526.1; NC_013523.1.
DR AlphaFoldDB; D1C5G1; -.
DR STRING; 479434.Sthe_0038; -.
DR KEGG; sti:Sthe_0038; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_3_0_0; -.
DR InParanoid; D1C5G1; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000002027; Chromosome 1.
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:SF5; AT19154P; 1.
DR PANTHER; PTHR12151; ELECTRON TRANSPORT PROTIN SCO1/SENC FAMILY MEMBER; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002027}.
FT DOMAIN 40..232
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 165..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 82
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 78..82
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 232 AA; 25040 MW; F0D005258F340FAB CRC64;
MPTRPASRRR IGPTLTLVLF LGLVTLLAAC GGSRELTGTD LGQEPAPDFT LTDHRGQTVS
LSQLRGKAVA LTFIYTHCPD ICPLITQHLR QAYEQLPEDA QERVALVAIT VDPARDTPEV
LQEYSERHGL AENPAWFALT ADAATLEPVW ASYYVDSGAM MADDHAGADA HGGQGEHGDH
ADHEATPAAG DGQQFTHTDA IFLIDRDGNW RVLLRSGTPP EEIADNLEIL AG
//
