ID A0A291QQT2_9BACT Unreviewed; 247 AA.
AC A0A291QQT2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=SCO family protein {ECO:0000313|EMBL:ATL46369.1};
GN ORFNames=COR50_03815 {ECO:0000313|EMBL:ATL46369.1};
OS Chitinophaga caeni.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2029983 {ECO:0000313|EMBL:ATL46369.1, ECO:0000313|Proteomes:UP000220133};
RN [1] {ECO:0000313|EMBL:ATL46369.1, ECO:0000313|Proteomes:UP000220133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 {ECO:0000313|EMBL:ATL46369.1,
RC ECO:0000313|Proteomes:UP000220133};
RA Jin D., Kong X., Deng Y., Bai Z.;
RT "Paenichitinophaga pekingensis gen. nov., sp. nov., isolated from activated
RT sludge.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SCO1/2 family.
CC {ECO:0000256|ARBA:ARBA00010996}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP023777; ATL46369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291QQT2; -.
DR KEGG; cbae:COR50_03815; -.
DR Proteomes; UP000220133; 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 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR603782-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000220133};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..226
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT BINDING 101
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 105
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT BINDING 191
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-1"
FT DISULFID 101..105
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR603782-2"
SQ SEQUENCE 247 AA; 27786 MW; 604B2DDCB0AB88E5 CRC64;
MIVNLNFTVI SKRALIGVAL AILVPLVGFL IVDHYSKNIV SIPRYYVAEG VDTVFKDGKT
TYDTVYHQVK NFQLTNQLGQ QVSLDDLDGK IVVVNLFFTH CPVVCPKLTK NIKSLQDAFV
KNDTLVQFLS LSVDPVRDSV SQLKRYADHF DIDPGNWWLM TGSKQEIYDL ARHELFVSAT
EGDGGPNDFI HSEKLIVLDK NRYIRGYYNG LDSTDLGRCA ADVAFLFLEK DHTKPGLLKR
IFSGGDH
//
