ID A0A3N1WTD1_9BURK Unreviewed; 248 AA.
AC A0A3N1WTD1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=EC845_3696 {ECO:0000313|EMBL:ROR17894.1};
OS Comamonas sp. BIGb0124.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2485130 {ECO:0000313|EMBL:ROR17894.1, ECO:0000313|Proteomes:UP000267274};
RN [1] {ECO:0000313|EMBL:ROR17894.1, ECO:0000313|Proteomes:UP000267274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIGb0124 {ECO:0000313|EMBL:ROR17894.1,
RC ECO:0000313|Proteomes:UP000267274};
RA Samuel B.;
RT "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Acts by transferring its disulfide bond to other proteins and
CC is reduced in the process. {ECO:0000256|RuleBase:RU364038}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU364038}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000256|ARBA:ARBA00009813, ECO:0000256|RuleBase:RU364038}.
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:ROR17894.1}.
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DR EMBL; RJVF01000014; ROR17894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1WTD1; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000267274; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR Gene3D; 3.10.450.70; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR Pfam; PF10411; DsbC_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000267274};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 30..248
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5017845310"
FT DOMAIN 35..89
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 118..242
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 248 AA; 27103 MW; DE7CA8D356263CAF CRC64;
MTRSPLFFRL ISRLATAALL ACAALPALAQ EAAIRKALPD RLPSLPAIDE VRTTPWSGLY
EVRMGSDVLY TDAGGNFLIQ GELLDLKTKA NLTQQRIAEL SAVDVSKLPL DDAFVTKRGK
GERKLVVFAD PNCGYCKRFE SELAKVDNVT VHTFLYPILG QDSVEKSRNI WCAKSPSQVW
DDWMLRGKSI PSASCSGDRE AALKRNVAFG QKHKIEGTPT LLFVDGQRVP GAISAAQIES
LLVASSKK
//