ID A0A095ZCL1_9BURK Unreviewed; 203 AA.
AC A0A095ZCL1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Electron transporter {ECO:0000313|EMBL:KGF32490.1};
GN ORFNames=HMPREF2130_00665 {ECO:0000313|EMBL:KGF32490.1};
OS Oligella urethralis DNF00040.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Oligella.
OX NCBI_TaxID=1401065 {ECO:0000313|EMBL:KGF32490.1, ECO:0000313|Proteomes:UP000029629};
RN [1] {ECO:0000313|EMBL:KGF32490.1, ECO:0000313|Proteomes:UP000029629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00040 {ECO:0000313|EMBL:KGF32490.1,
RC ECO:0000313|Proteomes:UP000029629};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGF32490.1}.
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DR EMBL; JRNI01000003; KGF32490.1; -; Genomic_DNA.
DR RefSeq; WP_018026598.1; NZ_JRNI01000003.1.
DR AlphaFoldDB; A0A095ZCL1; -.
DR GeneID; 61260908; -.
DR eggNOG; COG1999; Bacteria.
DR OrthoDB; 9790194at2; -.
DR Proteomes; UP000029629; Unassembled WGS sequence.
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:UP000029629};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..203
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001914198"
FT DOMAIN 35..203
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 75
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 79
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 168
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 75..79
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 203 AA; 22801 MW; 87A023D50D80453F CRC64;
MIKRLKKSSL AFALSLACLG MATPIDSALA ETQFYSTRSH LPDLKFELQH TDEQRLSEQQ
FKQKVVLVYF GYTYCPDVCP TTMAELALMK SMLSEQQQAQ VQVIFISVDP HRDTPARLEK
YLEAFGLGAI GLSGTEKEIA AIAKRYRVAY QIEKPKNPNN PELYDVMHAE GIYVFDTNGK
AAFLASNSHD IEGLHQRVVA LLK
//
