ID Q3BT76_XANC5 Unreviewed; 257 AA.
AC Q3BT76;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN Name=dsbG {ECO:0000313|EMBL:CAJ23983.1};
GN OrderedLocusNames=XCV2306 {ECO:0000313|EMBL:CAJ23983.1};
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273 {ECO:0000313|Proteomes:UP000007069};
RN [1] {ECO:0000313|EMBL:CAJ23983.1, ECO:0000313|Proteomes:UP000007069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10 {ECO:0000313|EMBL:CAJ23983.1,
RC ECO:0000313|Proteomes:UP000007069};
RX PubMed=16237009; DOI=10.1128/JB.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneicker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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; AM039952; CAJ23983.1; -; Genomic_DNA.
DR RefSeq; WP_011347503.1; NZ_CP017190.1.
DR AlphaFoldDB; Q3BT76; -.
DR KEGG; xcv:XCV2306; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_080090_0_0_6; -.
DR Proteomes; UP000007069; Chromosome.
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; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR PANTHER; PTHR35272:SF4; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBG; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 26..257
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010004580"
FT DOMAIN 122..253
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 257 AA; 27365 MW; 1799989259292653 CRC64;
MFAKRSRISL FLAASLLLVT GCSQAETANQ PPALKALEDQ GLTVMQEFKV GGGLRAFAAV
AGDRPVAIYI TSDGNAIVGT RLNAKGEPID EAALNNLAAK PLSDKEWAQL QSATSVRDGQ
ANAPRIVYAF SDANCPYCHR FWEAARPWVD AGKVQIRHIM VGIIREDSPA KAAAILGAAD
PSAALLENER KYSQGGITPA KSIPANVRKT LDDNQMLMLS MGFRGTPGIV VRGPDGVLKK
YNGMPQGPQL AEVLGPR
//
