ID C7JE29_ACEP3 Unreviewed; 260 AA.
AC C7JE29;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Electron transport transmembrane protein Sco1/SenC/PrrC {ECO:0000313|EMBL:BAI00213.1};
GN Name=sco1 {ECO:0000313|EMBL:BAI00213.1};
GN Synonyms=senC {ECO:0000313|EMBL:BAI00213.1};
GN OrderedLocusNames=APA01_20910 {ECO:0000313|EMBL:BAI00213.1};
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAI00213.1, ECO:0000313|Proteomes:UP000000948};
RN [1] {ECO:0000313|EMBL:BAI00213.1, ECO:0000313|Proteomes:UP000000948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; AP011121; BAI00213.1; -; Genomic_DNA.
DR AlphaFoldDB; C7JE29; -.
DR STRING; 634452.APA01_20910; -.
DR KEGG; apt:APA01_20910; -.
DR PATRIC; fig|634452.3.peg.2179; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_3_1_5; -.
DR BioCyc; APAS634452:APA01_RS10630-MONOMER; -.
DR Proteomes; UP000000948; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|PIRSR:PIRSR603782-1};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603782-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR603782-1};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:BAI00213.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 68..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 130
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 134
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 218
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 130..134
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 260 AA; 28564 MW; A210E5BD531419BD CRC64;
MDKTCSYPIP KYTCCFTPNR SYIMKRQCIA ASICAVCYNM PMTQKSSRTT ISDRSKPRSP
HKQNWKTIFP VAGILFALLI GATGLRVVLT SRSHTQIGGP YALTDENGHV VSQAAFQGHY
TLIYFGYTHC VDVCPLTLAT VSAALDELGS QGKNITPIFI SVDPARDTPA VVKEYIQRFS
SRIVGLTGTE AQLQPIMTAF HVSARRRAIT GDGYLMDHSS LLYLMDGQNH LAGMIPVDSS
AHQITVELKQ LLPPSKNHPS
//
