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Database: UniProt
Entry: A0A318IUF7_9BURK
LinkDB: A0A318IUF7_9BURK
Original site: A0A318IUF7_9BURK 
ID   A0A318IUF7_9BURK        Unreviewed;       246 AA.
AC   A0A318IUF7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA {ECO:0000256|ARBA:ARBA00013831};
GN   ORFNames=DFR42_1118 {ECO:0000313|EMBL:PXX38643.1};
OS   Undibacterium pigrum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Undibacterium.
OX   NCBI_TaxID=401470 {ECO:0000313|EMBL:PXX38643.1, ECO:0000313|Proteomes:UP000247792};
RN   [1] {ECO:0000313|EMBL:PXX38643.1, ECO:0000313|Proteomes:UP000247792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19792 {ECO:0000313|EMBL:PXX38643.1,
RC   ECO:0000313|Proteomes:UP000247792};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:PXX38643.1}.
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DR   EMBL; QJKB01000011; PXX38643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318IUF7; -.
DR   OrthoDB; 9784896at2; -.
DR   Proteomes; UP000247792; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..246
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016375249"
FT   DOMAIN          15..170
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          227..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   246 AA;  27227 MW;  8EB846DC81E82C26 CRC64;
     MQFFSQIKRR MFMLAGLSLV AGAVSASPAA PQAGVEYQVL KRPQPVEGGK KIEVIEFFGY
     FCPHCYALEP LLAEWVKKQG DNISFKRIHV NFHELIPQQK LYFSMEAMGK ADEYHMKAFQ
     AFHVNRNRLQ TDADVMEFVS KSGLDKQKFA DVYNSFSINS KLSRATQLAN AYQIDGVPSI
     AIDGRYVTSP VMAAATMTRV TEESQNRAAI EVLDYIVAKV QQGRNAPAAT APATPAASAN
     APVKKK
//
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