ID   A0A1G7ZYN4_9BURK        Unreviewed;       242 AA.
AC   A0A1G7ZYN4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   ORFNames=SAMN05216320_11018 {ECO:0000313|EMBL:SDH13320.1};
OS   Duganella sp. OV458.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1855290 {ECO:0000313|EMBL:SDH13320.1, ECO:0000313|Proteomes:UP000199454};
RN   [1] {ECO:0000313|EMBL:SDH13320.1, ECO:0000313|Proteomes:UP000199454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV458 {ECO:0000313|EMBL:SDH13320.1,
RC   ECO:0000313|Proteomes:UP000199454};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNCD01000010; SDH13320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7ZYN4; -.
DR   OrthoDB; 12976at2; -.
DR   Proteomes; UP000199454; 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   InterPro; IPR017937; Thioredoxin_CS.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU364038};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT   CHAIN           22..242
FT                   /note="Thiol:disulfide interchange protein"
FT                   /evidence="ECO:0000256|RuleBase:RU364038"
FT                   /id="PRO_5011329853"
FT   DOMAIN          32..84
FT                   /note="Disulphide bond isomerase DsbC/G N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10411"
FT   DOMAIN          113..235
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13098"
SQ   SEQUENCE   242 AA;  26738 MW;  50CF2E0BC819BDFC CRC64;
     MRKTKIALLS LSVLMASCVE AQTPPSTDAI KKLIEPRLGA NVKVDSVTET PYSGLYEVRI
     GSDILYTDKT ATYLINGHIF NLTTGADLTR ERIEEVTKIK FSDLPLDKAI KSVKGDGSRV
     IAVFEDPNCG YCKRLRQTTL KETDNVTIYT FMYNILSEDS FVKSKNVWCA PDRQKAWDDW
     MLSGKVPATA ATSCDSPNEE VLALGRKLAI QGTPAIFFAD GSRIPGAIDT KALEDKFSKL
     KK
//