ID   D5CSV6_SIDLE            Unreviewed;       212 AA.
AC   D5CSV6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Electron transport protein SCO1/SenC {ECO:0000313|EMBL:ADE12042.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Slit_1813 {ECO:0000313|EMBL:ADE12042.1};
OS   Sideroxydans lithotrophicus (strain ES-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Sideroxydans.
OX   NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE12042.1, ECO:0000313|Proteomes:UP000001625};
RN   [1] {ECO:0000313|EMBL:ADE12042.1, ECO:0000313|Proteomes:UP000001625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-1 {ECO:0000313|EMBL:ADE12042.1,
RC   ECO:0000313|Proteomes:UP000001625};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT   "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL   Submitted (MAR-2010) 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; CP001965; ADE12042.1; -; Genomic_DNA.
DR   RefSeq; WP_013029940.1; NC_013959.1.
DR   AlphaFoldDB; D5CSV6; -.
DR   STRING; 580332.Slit_1813; -.
DR   KEGG; slt:Slit_1813; -.
DR   eggNOG; COG1999; Bacteria.
DR   HOGENOM; CLU_050131_4_2_4; -.
DR   OrthoDB; 8550465at2; -.
DR   Proteomes; UP000001625; 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   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.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001625};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..212
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003069577"
FT   BINDING         93
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   BINDING         97
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT   DISULFID        93..97
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ   SEQUENCE   212 AA;  23499 MW;  3E5AA9D99E6DE841 CRC64;
     MQSNLTILAA ALAIGLSGAA ATSAYAHDGM HMEMMDMSGS ADVHHAVQKV VRKTMNYNVP
     RVELVRDDNR TVLLPDEMND GRPVIMNFIY TTCTSACPLT SHTFQELQAK LGSERNKVHM
     ISISIDPEQD TPRQLAEYAH KYDAKSQWQF YTGTSEASLA AQRAFGVYYG DKMDHTPVTL
     LRAAPGKAWL RIDGFASADD LLLEYRKLVS TP
//