ID A4JUG2_BURVG Unreviewed; 238 AA.
AC A4JUG2;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN OrderedLocusNames=Bcep1808_7029 {ECO:0000313|EMBL:ABO59915.1};
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OG Plasmid pBVIE01 {ECO:0000313|EMBL:ABO59915.1,
OG ECO:0000313|Proteomes:UP000002287}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO59915.1, ECO:0000313|Proteomes:UP000002287};
RN [1] {ECO:0000313|EMBL:ABO59915.1, ECO:0000313|Proteomes:UP000002287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RC PLASMID=pBVIE01 {ECO:0000313|EMBL:ABO59915.1,
RC ECO:0000313|Proteomes:UP000002287};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of plasmid pBVIE01 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) 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}.
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DR EMBL; CP000617; ABO59915.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JUG2; -.
DR KEGG; bvi:Bcep1808_7029; -.
DR HOGENOM; CLU_083593_1_1_4; -.
DR Proteomes; UP000002287; Plasmid pBVIE01.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 Isomerase {ECO:0000313|EMBL:ABO59915.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Plasmid {ECO:0000313|EMBL:ABO59915.1};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000002287};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 20..238
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010007944"
FT DOMAIN 28..80
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 108..234
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 238 AA; 25970 MW; 7B300D347CC85E1E CRC64;
MKKFAAALLL AGLSVAAFAS PETDSVLATL KSKYPNTNFT SIEASPLPGI YELTMGKNIA
YTDKEGHYFL FGSLYDMEKR QDLTAPKREA ASKIDVSKLP LKDAIVRVKG KGTRKLYLFT
DPDCPFCKEL ERDTLPKLDD VTIYTFMFPL DSLHPQARAK SESIWCLPEK ERGAAWDKLL
TTGTPPAMAK CDNPLAALSS LGDSLGVRGT PTMFSEDGRI LPGAAAPERI DAFLNAGK
//
