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Database: UniProt
Entry: A0A2S8EXX9_9RHOB
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Original site: A0A2S8EXX9_9RHOB 
ID   A0A2S8EXX9_9RHOB        Unreviewed;       250 AA.
AC   A0A2S8EXX9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Disulfide bond formation protein DsbA {ECO:0000313|EMBL:PQO24494.1};
GN   ORFNames=C2I36_02335 {ECO:0000313|EMBL:PQO24494.1};
OS   Rhodobacteraceae bacterium WD3A24.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2086263 {ECO:0000313|EMBL:PQO24494.1, ECO:0000313|Proteomes:UP000237945};
RN   [1] {ECO:0000313|EMBL:PQO24494.1, ECO:0000313|Proteomes:UP000237945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WD3A24 {ECO:0000313|EMBL:PQO24494.1,
RC   ECO:0000313|Proteomes:UP000237945};
RA   Wang S.;
RT   "The draft genome sequence of Pararoseibaca halophilus WD3A24.";
RL   Submitted (JAN-2018) 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}.
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:PQO24494.1}.
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DR   EMBL; PUHN01000005; PQO24494.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8EXX9; -.
DR   OrthoDB; 9780147at2; -.
DR   Proteomes; UP000237945; 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; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR   PANTHER; PTHR35272:SF5; THIOREDOXIN-LIKE_FOLD DOMAIN-CONTAINING PROTEIN; 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:UP000237945};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..250
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015629520"
FT   DOMAIN          60..209
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   250 AA;  27980 MW;  6D7B6120BB83C481 CRC64;
     MIRTLLGLAL SAVLALPVAA FDVENMTNAE RQAFRAEIRD YLLDNPEVIL EAVQVLEERQ
     QSAQAEGDMN MVQANGREIF NDGHSWVGGD PEGDITLVEF SDYRCSFCRR AHPEVMDMIA
     DDGDIRYIVK EFPILGEQSE RASRYAISVL QLEGDAAYAR AHDTLMTYRG EITRRALASI
     SEDLGVDHDA ITARMDAPEV TEVIEQNRAL ATQLQINGTP TFVLEDQMLR GYLPRGQMEQ
     MIAQMRNPDG
//
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