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Database: UniProt
Entry: A0A238W8B6_9RHOB
LinkDB: A0A238W8B6_9RHOB
Original site: A0A238W8B6_9RHOB 
ID   A0A238W8B6_9RHOB        Unreviewed;       249 AA.
AC   A0A238W8B6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:SNR42835.1};
GN   ORFNames=SAMN06265370_104259 {ECO:0000313|EMBL:SNR42835.1};
OS   Puniceibacterium sediminis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Puniceibacterium.
OX   NCBI_TaxID=1608407 {ECO:0000313|EMBL:SNR42835.1, ECO:0000313|Proteomes:UP000198417};
RN   [1] {ECO:0000313|EMBL:SNR42835.1, ECO:0000313|Proteomes:UP000198417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29052 {ECO:0000313|EMBL:SNR42835.1,
RC   ECO:0000313|Proteomes:UP000198417};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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; FZNN01000004; SNR42835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238W8B6; -.
DR   OrthoDB; 9780147at2; -.
DR   Proteomes; UP000198417; Unassembled WGS sequence.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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   Isomerase {ECO:0000313|EMBL:SNR42835.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198417};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..249
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013371438"
FT   DOMAIN          50..247
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   249 AA;  27234 MW;  EA249D818B558811 CRC64;
     MIKTLTAAAL ATCLSAPAWA FDVSAMTDGE RDAFRAEIRA YLLDNPEVIF EAVDIAEQRK
     AEAQTAGDEQ LLADNAAAIF DDGFSWVGGN PDGDITVVEF MDYRCGYCRK AHDEVAELVE
     RDGNIKFIVK EFPILGEASL TSTRFALAVR LVAGEEAYKP AYDALITMTS DMSEPVLRRL
     ANTLEVDADA VLARMNDPEI DRQISKTRAL AQVLKINGTP TFVMGTELVR GYVPLDTMQQ
     IVATERGEG
//
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