ID A0A1X7A3Y0_9RHOB Unreviewed; 210 AA.
AC A0A1X7A3Y0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=DSBA-like thioredoxin domain protein {ECO:0000313|EMBL:SLN69798.1};
DE SubName: Full=Protein-disulfide isomerase {ECO:0000313|EMBL:PSK80844.1};
GN ORFNames=CLV79_11931 {ECO:0000313|EMBL:PSK80844.1}, LOS8367_03519
GN {ECO:0000313|EMBL:SLN69798.1};
OS Limimaricola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1343159 {ECO:0000313|EMBL:SLN69798.1, ECO:0000313|Proteomes:UP000193495};
RN [1] {ECO:0000313|EMBL:SLN69798.1, ECO:0000313|Proteomes:UP000193495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8367 {ECO:0000313|EMBL:SLN69798.1,
RC ECO:0000313|Proteomes:UP000193495};
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.
RN [2] {ECO:0000313|EMBL:PSK80844.1, ECO:0000313|Proteomes:UP000240624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29956 {ECO:0000313|EMBL:PSK80844.1,
RC ECO:0000313|Proteomes:UP000240624};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-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}.
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DR EMBL; PYGB01000019; PSK80844.1; -; Genomic_DNA.
DR EMBL; FWFY01000017; SLN69798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7A3Y0; -.
DR OrthoDB; 9780147at2; -.
DR Proteomes; UP000193495; Unassembled WGS sequence.
DR Proteomes; UP000240624; 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; IPR006311; TAT_signal.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51318; TAT; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:PSK80844.1}.
FT DOMAIN 25..210
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 210 AA; 22366 MW; 2371228A5CB706EE CRC64;
MTNLTRRTAL TGGLLALGGI TLWTATRSAR AQEQPLRPTI DEVMFDPANP VLGNPEGDVT
IVEFFDYQCP YCKANHPVLN EVVEADGNVR LVMKDWPIFG APSVRAAQLA LGAASLDSYL
TANDALMATE GRLDDTLIEE TLAEAGLDVA ALDAAYGENR DKWDGLLTRN GAQAAAFQLR
GTPAFIIGTV IYPGAMDKAG LENAIAMARG
//