ID H6KZF1_SAPGL Unreviewed; 211 AA.
AC H6KZF1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Electron transport protein sco1/senc {ECO:0000313|EMBL:AFC25727.1};
GN OrderedLocusNames=SGRA_2999 {ECO:0000313|EMBL:AFC25727.1};
OS Saprospira grandis (strain Lewin).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC25727.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC25727.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC25727.1,
RC ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
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DR EMBL; CP002831; AFC25727.1; -; Genomic_DNA.
DR RefSeq; WP_015693328.1; NC_016940.1.
DR AlphaFoldDB; H6KZF1; -.
DR STRING; 984262.SGRA_2999; -.
DR KEGG; sgn:SGRA_2999; -.
DR eggNOG; COG1999; Bacteria.
DR HOGENOM; CLU_050131_2_0_10; -.
DR OrthoDB; 9811998at2; -.
DR Proteomes; UP000007519; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007519}.
FT DOMAIN 46..209
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 84
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 88
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 172
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 84..88
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 211 AA; 23746 MW; 1E2C7F294B593E77 CRC64;
MNTKFFIFLL AIATLGACSS SPQKKLPVLG QPEVTEKTVD GKTVYDSTEH KIPDFSLYNQ
EGENITQATV EGKVYVADFF FTSCPTICPK VKANLKKVYK EYKDRDDFLL LSHSIDVKHD
TIGRLAWYAD KFNIDAKSWH LLTGKHEDIY KLSPEYLIAA LVDEGAPGGF DHSGALALVD
RHRRIRGMYD GTDPEKMEDL IKDIAILLAE K
//
