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Database: UniProt
Entry: A0A1Y5SUP9_9PROT
LinkDB: A0A1Y5SUP9_9PROT
Original site: A0A1Y5SUP9_9PROT 
ID   A0A1Y5SUP9_9PROT        Unreviewed;       249 AA.
AC   A0A1Y5SUP9;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Disulfide bond formation protein D {ECO:0000313|EMBL:SLN48945.1};
GN   Name=bdbD_2 {ECO:0000313|EMBL:SLN48945.1};
GN   ORFNames=OCH7691_02134 {ECO:0000313|EMBL:SLN48945.1};
OS   Oceanibacterium hippocampi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sneathiellales;
OC   Sneathiellaceae; Oceanibacterium.
OX   NCBI_TaxID=745714 {ECO:0000313|EMBL:SLN48945.1, ECO:0000313|Proteomes:UP000193200};
RN   [1] {ECO:0000313|EMBL:SLN48945.1, ECO:0000313|Proteomes:UP000193200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7691 {ECO:0000313|EMBL:SLN48945.1,
RC   ECO:0000313|Proteomes:UP000193200};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be required for disulfide bond formation in some
CC       proteins. {ECO:0000256|ARBA:ARBA00003565}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
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DR   EMBL; FWFR01000001; SLN48945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5SUP9; -.
DR   InParanoid; A0A1Y5SUP9; -.
DR   OrthoDB; 9780147at2; -.
DR   Proteomes; UP000193200; Unassembled WGS sequence.
DR   CDD; cd03023; DsbA_Com1_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR041205; ScsC_N.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR13887:SF14; CLPXP ADAPTER PROTEIN SPXH; 1.
DR   PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR   Pfam; PF18312; ScsC_N; 1.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193200};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..249
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010999918"
FT   DOMAIN          65..247
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   249 AA;  26884 MW;  EDE103F0AA4918E7 CRC64;
     MTAIRTFLAA LALAVTLLGV TGAQAGESLD EAQEARIREI VREYLIEHPE VIVEALQALE
     AREQAARQDS LKDRVVAHAD GLFNDPTSPI LGNPDGDVTI VEFFDYRCPY CKRAHRALAE
     VLEADGNIRV VLKEFPVLGK DSVTAARAAL AAVHQDGYLA FHEAMMANEG NLGEDRVLAL
     AASVGLDTAK LQQDMASEEI VAVIRRSYAL AQALDITGTP AFVVGEKVYP GALTADQFRE
     IVRQARGDS
//
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